European contribution to the study of ROS: A summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS)
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, přehledy, práce podpořená grantem
Grantová podpora
G0900224
Medical Research Council - United Kingdom
R01 DK103750
NIDDK NIH HHS - United States
RG/13/7/30099
British Heart Foundation - United Kingdom
PubMed
28577489
PubMed Central
PMC5458069
DOI
10.1016/j.redox.2017.05.007
PII: S2213-2317(17)30337-3
Knihovny.cz E-zdroje
- Klíčová slova
- Antioxidants, Oxidative stress, Reactive nitrogen species, Reactive oxygen species, Redox signaling, Redox therapeutics,
- MeSH
- Evropská unie MeSH
- lidé MeSH
- mezinárodní spolupráce * MeSH
- molekulární biologie organizace a řízení trendy MeSH
- oxidace-redukce MeSH
- reaktivní formy kyslíku chemie metabolismus MeSH
- signální transdukce MeSH
- společnosti vědecké MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- přehledy MeSH
- Názvy látek
- reaktivní formy kyslíku MeSH
The European Cooperation in Science and Technology (COST) provides an ideal framework to establish multi-disciplinary research networks. COST Action BM1203 (EU-ROS) represents a consortium of researchers from different disciplines who are dedicated to providing new insights and tools for better understanding redox biology and medicine and, in the long run, to finding new therapeutic strategies to target dysregulated redox processes in various diseases. This report highlights the major achievements of EU-ROS as well as research updates and new perspectives arising from its members. The EU-ROS consortium comprised more than 140 active members who worked together for four years on the topics briefly described below. The formation of reactive oxygen and nitrogen species (RONS) is an established hallmark of our aerobic environment and metabolism but RONS also act as messengers via redox regulation of essential cellular processes. The fact that many diseases have been found to be associated with oxidative stress established the theory of oxidative stress as a trigger of diseases that can be corrected by antioxidant therapy. However, while experimental studies support this thesis, clinical studies still generate controversial results, due to complex pathophysiology of oxidative stress in humans. For future improvement of antioxidant therapy and better understanding of redox-associated disease progression detailed knowledge on the sources and targets of RONS formation and discrimination of their detrimental or beneficial roles is required. In order to advance this important area of biology and medicine, highly synergistic approaches combining a variety of diverse and contrasting disciplines are needed.
A 1 Virtanen Institute for Molecular Sciences University of Eastern Finland Kuopio Finland
Bellvitge Biomedical Research Institute L'Hospitalet Barcelona Spain
Brighton and Sussex Medical School Brighton UK
CBIOS Universidade Lusófona Research Center for Biosciences and Health Technologies Lisboa Portugal
Centro de Biología Molecular Severo Ochoa Madrid Spain
Conway Institute School of Medicine University College Dublin Dublin Ireland
Danylo Halytsky Lviv National Medical University Lviv Ukraine
Department of Biochemistry Molecular Biology and Biophysics University of Minnesota Twin Cities USA
Department of Biochemistry School of Medicine Marmara University İstanbul Turkey
Department of Biomedical Sciences University of Padova via Ugo Bassi 58 b 35131 Padova Italy
Department of Biophysics Ankara University Faculty of Medicine 06100 Ankara Turkey
Department of Medical Biochemistry Faculty of Medicine Akdeniz University Antalya Turkey
Department of Medicine University of Cambridge UK
Department of Molecular Biology University of Bergen Bergen Norway
Department of Molecular Medicine University of Padova Padova Italy
Department of Nephrology and Hypertension University Medical Center Utrecht The Netherlands
Department of Neurology Medical Faculty Heinrich Heine University Düsseldorf Germany
Department of Pathology University of Cambridge Cambridge UK
Department of Pharmacology Johannes Gutenberg University Medical Center Mainz Germany
Department of Physiology 2nd Faculty of Medicine Charles University Prague Czech Republic
Department of Physiology University of Valencia Spain
Dept of Pathology and Immunology Centre Médical Universitaire Geneva Switzerland
Faculty of Biochemistry and Molecular Medicine and Biocenter Oulu University of Oulu Oulu Finland
Faculty of Medical Sciences Goce Delcev University Stip Republic of Macedonia
Fundación para la Investigación Biomédica del Hospital Universitario de Getafe Getafe Spain
Helmholtz Center Munich Institute of Developmental Genetics Neuherberg Germany
Institute for Biology Microbiology Freie Universität Berlin Berlin Germany
Institute for Biomedical Aging Research University of Innsbruck Innsbruck Austria
Institute of Cardiovascular and Medical Sciences University of Glasgow UK
Institute of Neuroscience Padova Italy
Institute of Nutrition Department of Nutrigenomics Friedrich Schiller University Jena Germany
Institute of Physiology JLU Giessen Giessen Germany
Instituto de Investigaciones Biomédicas Alberto Sols Madrid Spain
Laboratory for Oxidative Stress Rudjer Boskovic Institute Bijenicka 54 10000 Zagreb Croatia
Laboratory of Pharmacology Faculty of Pharmacy National and Kapodistrian University of Athens Greece
Laboratoty of Pharmacology Faculty of Pharmacy National and Kapodistrian University of Athens Greece
LCBPT UMR 8601 CNRS Paris Descartes University Sorbonne Paris Cité Paris France
Medical College of Wisconsin Milwaukee USA
Research Institute for Medicines Faculty of Pharmacy Universidade de Lisboa Lisboa Portugal
Ruđer Bošković Institute Division of Molecular Medicine Zagreb Croatia
School of Biology Aristotle University of Thessaloniki Thessaloniki 54124 Greece
School of Life and Health Sciences Aston University Aston Triangle Birmingham B47ET UK
The Research Institute of University of Bucharest Bucharest Romania
University of Belgrade Faculty of Physical Chemistry Studentski trg 12 16 11000 Belgrade Serbia
University of Exeter Medical School St Luke's Campus Exeter EX1 2LU UK
Zobrazit více v PubMed
Virtual Collection, Emerging concepts in redox biology and oxidative stress, Redox Biol. (18 articles plus editorial), in: Santiago Lamas, Fabio Di Lisa, Andreas Daiber (eds.). 〈https://www.journals.elsevier.com/redox-biology/virtual-collections/emerging-conceptsin-redox-biology-and-oxidative-stress-virt〉. PubMed PMC
Forum Issue, Redox medicine, Antioxid. Redox Signal. (9 articles), in: Harald H.H.W. Schmidt, Fabio Di Lisa (eds.) 〈http://online.liebertpub.com/toc/ars/23/14〉.
Daiber A., Di Lisa F., Lamas S. Virtual issue by COST action BM1203 (EU-ROS). Emerging concepts in redox biology and oxidative stress. Redox Biol. 2016;8:439–441. PubMed PMC
Themed issue, Redox biology and oxidative stress in health and disease, Br. J. Pharmacol. (16 articles), in: Peter Ferdinandy and Andreas Daiber (eds.). 〈http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1476–5381/homepage/themed_issues.htm〉.
Augusto O., Miyamoto S. Oxygen radicals and related species. In: Pantopoulos K., Schipper H.M., editors. Principles of Free Radical Biomedicine. Nova Science Publishers, Inc; 2011.
Frijhoff J., Winyard P.G., Zarkovic N., Davies S.S., Stocker R., Cheng D., Knight A.R., Taylor E.L., Oettrich J., Ruskovska T., Gasparovic A.C., Cuadrado A., Weber D., Poulsen H.E., Grune T., Schmidt H.H., Ghezzi P. Clinical relevance of biomarkers of oxidative stress. Antioxid. Redox Signal. 2015;23:1144–1170. PubMed PMC
Griendling K.K., FitzGerald G.A. Oxidative stress and cardiovascular injury: part I: basic mechanisms and in vivo monitoring of ROS. Circulation. 2003;108:1912–1916. PubMed
Griendling K.K., FitzGerald G.A. Oxidative stress and cardiovascular injury: part II: animal and human studies. Circulation. 2003;108:2034–2040. PubMed
Daiber A., Steven S., Weber A., Shuvaev V.V., Muzykantov V.R., Laher I., Li H., Lamas S., Munzel T. Targeting vascular (endothelial) dysfunction. Br. J. Pharmacol. 2016 PubMed PMC
Giasson B.I., Duda J.E., Murray I.V., Chen Q., Souza J.M., Hurtig H.I., Ischiropoulos H., Trojanowski J.Q., Lee V.M. Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions. Science. 2000;290:985–989. PubMed
Ischiropoulos H., Beckman J.S. Oxidative stress and nitration in neurodegeneration: cause, effect, or association? J. Clin. Investig. 2003;111:163–169. PubMed PMC
Ceriello A. Oxidative stress and diabetes-associated complications. Endocr. Pract. 2006;12(Suppl 1):S60–S62. PubMed
Keaney J.F., Jr., Loscalzo J. Diabetes, oxidative stress, and platelet activation. Circulation. 1999;99:189–191. PubMed
Karbach S., Wenzel P., Waisman A., Munzel T., Daiber A. eNOS uncoupling in cardiovascular diseases–the role of oxidative stress and inflammation. Curr. Pharm. Des. 2014;20:3579–3594. PubMed
Szabo C. The pathophysiological role of peroxynitrite in shock, inflammation, and ischemia-reperfusion injury. Shock. 1996;6:79–88. PubMed
Kooy N.W., Lewis S.J., Royall J.A., Ye Y.Z., Kelly D.R., Beckman J.S. Extensive tyrosine nitration in human myocardial inflammation: evidence for the presence of peroxynitrite. Crit. Care Med. 1997;25:812–819. PubMed
Aviello G., Knaus U.G. ROS in gastrointestinal inflammation: rescue or Sabotage? Br. J. Pharmacol. 2016 PubMed PMC
Daiber A., Di Lisa F., Oelze M., Kroller-Schon S., Steven S., Schulz E., Munzel T. Crosstalk of mitochondria with NADPH oxidase via reactive oxygen and nitrogen species signalling and its role for vascular function. Br. J. Pharmacol. 2015 PubMed PMC
Steven S., Munzel T., Daiber A. Exploiting the pleiotropic antioxidant effects of established drugs in cardiovascular disease. Int. J. Mol. Sci. 2015;16:18185–18223. PubMed PMC
Wenzel P., Kossmann S., Munzel T., Daiber A. Redox regulation of cardiovascular inflammation – Immunomodulatory function of mitochondrial and Nox-derived reactive oxygen and nitrogen species. Free Radic. Biol. Med. 2017 PubMed
Schmidt H.H., Stocker R., Vollbracht C., Paulsen G., Riley D., Daiber A., Cuadrado A. Antioxidants in translational medicine. Antioxid. Redox Signal. 2015;23:1130–1143. PubMed PMC
Bjelakovic G., Nikolova D., Gluud L.L., Simonetti R.G., Gluud C. Mortality in randomized trials of antioxidant supplements for primary and secondary prevention: systematic review and meta-analysis. Jama. 2007;297:842–857. PubMed
Gori T., Munzel T. Oxidative stress and endothelial dysfunction: therapeutic implications. Ann. Med. 2011;43:259–272. PubMed
Ghezzi P., Jaquet V., Marcucci F., Schmidt H.H. The oxidative stress theory of disease: levels of evidence and epistemological aspects. Br. J. Pharmacol. 2016 PubMed PMC
P. Mustain Antioxidant Supplements: Too Much of a Kinda Good Thing 〈https://blogs.scientificamerican.com/food-matters/antioxidant-supplements-too-much-of-a-kinda-good-thing/〉.
A. Riley Why vitamin pills don't work, and may be bad for you. 〈http://www.bbc.com/future/story/20161208-why-vitamin-supplements-could-kill-you〉.
Scudellari M. The science myths that will not die. Nature. 2015;528:322–325. PubMed
Chen A.F., Chen D.D., Daiber A., Faraci F.M., Li H., Rembold C.M., Laher I. Free radical biology of the cardiovascular system. Clin. Sci. 2012;123:73–91. PubMed
Khaw K.T., Bingham S., Welch A., Luben R., Wareham N., Oakes S., Day N. Relation between plasma ascorbic acid and mortality in men and women in EPIC-Norfolk prospective study: a prospective population study. European prospective investigation into cancer and nutrition. Lancet. 2001;357:657–663. PubMed
Levonen A.L., Hill B.G., Kansanen E., Zhang J., Darley-Usmar V.M. Redox regulation of antioxidants, autophagy, and the response to stress: implications for electrophile therapeutics. Free Radic. Biol. Med. 2014;71:196–207. PubMed PMC
Forman H.J., Davies K.J., Ursini F. How do nutritional antioxidants really work: nucleophilic tone and para-hormesis versus free radical scavenging in vivo. Free Radic. Biol. Med. 2014;66:24–35. PubMed PMC
Casas A.I., Dao V.T., Daiber A., Maghzal G.J., Di Lisa F., Kaludercic N., Leach S., Cuadrado A., Jaquet V., Seredenina T., Krause K.H., Lopez M.G., Stocker R., Ghezzi P., Schmidt H.H. Reactive oxygen-related diseases: therapeutic targets and emerging clinical indications. Antioxid. Redox Signal. 2015;23:1171–1185. PubMed PMC
Hancock J.T., Whiteman M. Hydrogen sulfide signaling: interactions with nitric oxide and reactive oxygen species. Ann. N. Y. Acad. Sci. 2016;1365:5–14. PubMed
Vile G.F., Basu-Modak S., Waltner C., Tyrrell R.M. Heme oxygenase 1 mediates an adaptive response to oxidative stress in human skin fibroblasts. Proc. Natl. Acad. Sci. USA. 1994;91:2607–2610. PubMed PMC
Daiber A. Redox signaling (cross-talk) from and to mitochondria involves mitochondrial pores and reactive oxygen species. Biochim. Biophys. Acta. 2010;1797:897–906. PubMed
Zorov D.B., Juhaszova M., Sollott S.J. Mitochondrial Reactive Oxygen Species (ROS) and ROS-induced ROS release. Physiol. Rev. 2014;94:909–950. PubMed PMC
Larson M.C., Hillery C.A., Hogg N. Circulating membrane-derived microvesicles in redox biology. Free Radic. Biol. Med. 2014;73:214–228. PubMed PMC
Camus S.M., De Moraes J.A., Bonnin P., Abbyad P., Le Jeune S., Lionnet F., Loufrani L., Grimaud L., Lambry J.C., Charue D., Kiger L., Renard J.M., Larroque C., Le Clesiau H., Tedgui A., Bruneval P., Barja-Fidalgo C., Alexandrou A., Tharaux P.L., Boulanger C.M., Blanc-Brude O.P. Circulating cell membrane microparticles transfer heme to endothelial cells and trigger vasoocclusions in sickle cell disease. Blood. 2015;125:3805–3814. PubMed PMC
Tsiantoulas D., Perkmann T., Afonyushkin T., Mangold A., Prohaska T.A., Papac-Milicevic N., Millischer V., Bartel C., Horkko S., Boulanger C.M., Tsimikas S., Fischer M.B., Witztum J.L., Lang I.M., Binder C.J. Circulating microparticles carry oxidation-specific epitopes and are recognized by natural IgM antibodies. J. Lipid Res. 2015;56:440–448. PubMed PMC
Jung T., Hohn A., Grune T. The proteasome and the degradation of oxidized proteins: part II – protein oxidation and proteasomal degradation. Redox Biol. 2014;2:99–104. PubMed PMC
Kriegenburg F., Poulsen E.G., Koch A., Kruger E., Hartmann-Petersen R. Redox control of the ubiquitin-proteasome system: from molecular mechanisms to functional significance. Antioxid. Redox Signal. 2011;15:2265–2299. PubMed
Sigala F., Efentakis P., Karageorgiadi D., Filis K., Zampas P., Iliodromitis E.K., Zografos G., Papapetropoulos A., Andreadou I. Reciprocal regulation of eNOS, H2S and CO-synthesizing enzymes in human atheroma: correlation with plaque stability and effects of simvastatin. Redox Biol. 2017;12:70–81. PubMed PMC
Morgan B., Ezerina D., Amoako T.N., Riemer J., Seedorf M., Dick T.P. Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis. Nat. Chem. Biol. 2013;9:119–125. PubMed
Dunnill C., Patton T., Brennan J., Barrett J., Dryden M., Cooke J., Leaper D., Georgopoulos N.T. Reactive oxygen species (ROS) and wound healing: the functional role of ROS and emerging ROS-modulating technologies for augmentation of the healing process. Int. Wound J. 2017;14:89–96. PubMed PMC
Cheresh P., Kim S.J., Tulasiram S., Kamp D.W. Oxidative stress and pulmonary fibrosis. Biochim. Biophys. Acta. 2013;1832:1028–1040. PubMed PMC
Colgan S.P., Ehrentraut S.F., Glover L.E., Kominsky D.J., Campbell E.L. Contributions of neutrophils to resolution of mucosal inflammation. Immunol. Res. 2013;55:75–82. PubMed PMC
Mittal M., Siddiqui M.R., Tran K., Reddy S.P., Malik A.B. Reactive oxygen species in inflammation and tissue injury. Antioxid. Redox Signal. 2014;20:1126–1167. PubMed PMC
O'Neill S., Brault J., Stasia M.J., Knaus U.G. Genetic disorders coupled to ROS deficiency. Redox Biol. 2015;6:135–156. PubMed PMC
Yao H., Edirisinghe I., Yang S.R., Rajendrasozhan S., Kode A., Caito S., Adenuga D., Rahman I. Genetic ablation of NADPH oxidase enhances susceptibility to cigarette smoke-induced lung inflammation and emphysema in mice. Am. J. Pathol. 2008;172:1222–1237. PubMed PMC
Won H.Y., Jang E.J., Min H.J., Hwang E.S. Enhancement of allergen-induced airway inflammation by NOX2 deficiency. Immune Netw. 2011;11:169–174. PubMed PMC
Davies M.J. Protein oxidation and peroxidation. Biochem. J. 2016;473:805–825. PubMed PMC
Brautigam L., Schutte L.D., Godoy J.R., Prozorovski T., Gellert M., Hauptmann G., Holmgren A., Lillig C.H., Berndt C. Vertebrate-specific glutaredoxin is essential for brain development. Proc. Natl. Acad. Sci. USA. 2011;108:20532–20537. PubMed PMC
Brautigam L., Jensen L.D., Poschmann G., Nystrom S., Bannenberg S., Dreij K., Lepka K., Prozorovski T., Montano S.J., Aktas O., Uhlen P., Stuhler K., Cao Y., Holmgren A., Berndt C. Glutaredoxin regulates vascular development by reversible glutathionylation of sirtuin 1. Proc. Natl. Acad. Sci. USA. 2013;110:20057–20062. PubMed PMC
Prozorovski T., Schneider R., Berndt C., Hartung H.P., Aktas O. Redox-regulated fate of neural stem progenitor cells. Biochim. Biophys. Acta. 2015;1850:1543–1554. PubMed
Gascon S., Murenu E., Masserdotti G., Ortega F., Russo G.L., Petrik D., Deshpande A., Heinrich C., Karow M., Robertson S.P., Schroeder T., Beckers J., Irmler M., Berndt C., Angeli J.P., Conrad M., Berninger B., Gotz M. Identification and successful negotiation of a metabolic checkpoint in direct neuronal reprogramming. Cell Stem Cell. 2016;18:396–409. PubMed
Morgan B., Van Laer K., Owusu T.N., Ezerina D., Pastor-Flores D., Amponsah P.S., Tursch A., Dick T.P. Real-time monitoring of basal H2O2 levels with peroxiredoxin-based probes. Nat. Chem. Biol. 2016;12:437–443. PubMed
Friedmann Angeli J.P., Schneider M., Proneth B., Tyurina Y.Y., Tyurin V.A., Hammond V.J., Herbach N., Aichler M., Walch A., Eggenhofer E., Basavarajappa D., Radmark O., Kobayashi S., Seibt T., Beck H., Neff F., Esposito I., Wanke R., Forster H., Yefremova O., Heinrichmeyer M., Bornkamm G.W., Geissler E.K., Thomas S.B., Stockwell B.R., O'Donnell V.B., Kagan V.E., Schick J.A., Conrad M. Inactivation of the ferroptosis regulator Gpx4 triggers acute renal failure in mice. Nat. Cell Biol. 2014;16:1180–1191. PubMed PMC
Dikalov S. Cross talk between mitochondria and NADPH oxidases. Free Radic. Biol. Med. 2011;51:1289–1301. PubMed PMC
Zorov D.B., Filburn C.R., Klotz L.O., Zweier J.L., Sollott S.J. Reactive oxygen species (ROS)-induced ROS release: a new phenomenon accompanying induction of the mitochondrial permeability transition in cardiac myocytes. J. Exp. Med. 2000;192:1001–1014. PubMed PMC
Schulz E., Wenzel P., Munzel T., Daiber A. Mitochondrial redox signaling: interaction of mitochondrial reactive oxygen species with other sources of oxidative stress. Antioxid. Redox Signal. 2014;20:308–324. PubMed PMC
Wenzel P., Mollnau H., Oelze M., Schulz E., Wickramanayake J.M., Muller J., Schuhmacher S., Hortmann M., Baldus S., Gori T., Brandes R.P., Munzel T., Daiber A. First evidence for a crosstalk between mitochondrial and NADPH oxidase-derived reactive oxygen species in nitroglycerin-triggered vascular dysfunction. Antioxid. Redox Signal. 2008;10:1435–1447. PubMed
Oelze M., Kroller-Schon S., Steven S., Lubos E., Doppler C., Hausding M., Tobias S., Brochhausen C., Li H., Torzewski M., Wenzel P., Bachschmid M., Lackner K.J., Schulz E., Munzel T., Daiber A. Glutathione peroxidase-1 deficiency potentiates dysregulatory modifications of endothelial nitric oxide synthase and vascular dysfunction in aging. Hypertension. 2014;63:390–396. PubMed
Kroller-Schon S., Steven S., Kossmann S., Scholz A., Daub S., Oelze M., Xia N., Hausding M., Mikhed Y., Zinssius E., Mader M., Stamm P., Treiber N., Scharffetter-Kochanek K., Li H., Schulz E., Wenzel P., Munzel T., Daiber A. Molecular mechanisms of the crosstalk between mitochondria and NADPH oxidase through reactive oxygen species-studies in white blood cells and in animal models. Antioxid. Redox Signal. 2014;20:247–266. PubMed PMC
Jankovic A., Korac A., Buzadzic B., Otasevic V., Stancic A., Daiber A., Korac B. Redox implications in adipose tissue (dys)function – a new look at old acquaintances. Redox Biol. 2015;6:19–32. PubMed PMC
Lambeth J.D., Neish A.S. Nox enzymes and new thinking on reactive oxygen: a double-edged sword revisited. Annu. Rev. Pathol. 2014;9:119–145. PubMed
Sommer F., Backhed F. The gut microbiota engages different signaling pathways to induce Duox2 expression in the ileum and colon epithelium. Mucosal Immunol. 2015;8:372–379. PubMed
Corcionivoschi N., Alvarez L.A., Sharp T.H., Strengert M., Alemka A., Mantell J., Verkade P., Knaus U.G., Bourke B. Mucosal reactive oxygen species decrease virulence by disrupting campylobacter jejuni phosphotyrosine signaling. Cell Host Microbe. 2012;12:47–59. PubMed PMC
Alvarez L.A., Kovacic L., Rodriguez J., Gosemann J.H., Kubica M., Pircalabioru G.G., Friedmacher F., Cean A., Ghise A., Sarandan M.B., Puri P., Daff S., Plettner E., von Kriegsheim A., Bourke B., Knaus U.G. NADPH oxidase-derived H2O2 subverts pathogen signaling by oxidative phosphotyrosine conversion to PB-DOPA. Proc. Natl. Acad. Sci. USA. 2016;113:10406–10411. PubMed PMC
Pircalabioru G., Aviello G., Kubica M., Zhdanov A., Paclet M.H., Brennan L., Hertzberger R., Papkovsky D., Bourke B., Knaus U.G. Defensive mutualism rescues NADPH oxidase inactivation in gut infection. Cell Host Microbe. 2016;19:651–663. PubMed
Neish A.S., Jones R.M. Redox signaling mediates symbiosis between the gut microbiota and the intestine. Gut Microbes. 2014;5:250–253. PubMed PMC
Rimessi A., Previati M., Nigro F., Wieckowski M.R., Pinton P. Mitochondrial reactive oxygen species and inflammation: molecular mechanisms, diseases and promising therapies. Int. J. Biochem. Cell Biol. 2016;81:281–293. PubMed
Hertzberger R., Arents J., Dekker H.L., Pridmore R.D., Gysler C., Kleerebezem M., de Mattos M.J. H(2)O(2) production in species of the Lactobacillus acidophilus group: a central role for a novel NADH-dependent flavin reductase. Appl. Environ. Microbiol. 2014;80:2229–2239. PubMed PMC
Ito A., Sato Y., Kudo S., Sato S., Nakajima H., Toba T. The screening of hydrogen peroxide-producing lactic acid bacteria and their application to inactivating psychrotrophic food-borne pathogens. Curr. Microbiol. 2003;47:231–236. PubMed
Benisty R., Cohen A.Y., Feldman A., Cohen Z., Porat N. Endogenous H2O2 produced by Streptococcus pneumoniae controls FabF activity. Biochim. Biophys. Acta. 2010;1801:1098–1104. PubMed
Pericone C.D., Overweg K., Hermans P.W., Weiser J.N. Inhibitory and bactericidal effects of hydrogen peroxide production by Streptococcus pneumoniae on other inhabitants of the upper respiratory tract. Infect. Immun. 2000;68:3990–3997. PubMed PMC
Moy T.I., Mylonakis E., Calderwood S.B., Ausubel F.M. Cytotoxicity of hydrogen peroxide produced by Enterococcus faecium. Infect. Immun. 2004;72:4512–4520. PubMed PMC
Marsh E.K., May R.C. Caenorhabditis elegans, a model organism for investigating immunity. Appl. Environ. Microbiol. 2012;78:2075–2081. PubMed PMC
van der Hoeven R., McCallum K.C., Garsin D.A. Speculations on the activation of ROS generation in C. elegans innate immune signaling. Worm. 2012;1:160–163. PubMed PMC
Balla K.M., Troemel E.R. Caenorhabditis elegans as a model for intracellular pathogen infection. Cell Microbiol. 2013;15:1313–1322. PubMed PMC
Mora-Lorca J.A., Saenz-Narciso B., Gaffney C.J., Naranjo-Galindo F.J., Pedrajas J.R., Guerrero-Gomez D., Dobrzynska A., Askjaer P., Szewczyk N.J., Cabello J., Miranda-Vizuete A. Glutathione reductase gsr-1 is an essential gene required for Caenorhabditis elegans early embryonic development. Free Radic. Biol. Med. 2016;96:446–461. PubMed PMC
Stenvall J., Fierro-Gonzalez J.C., Swoboda P., Saamarthy K., Cheng Q., Cacho-Valadez B., Arner E.S., Persson O.P., Miranda-Vizuete A., Tuck S. Selenoprotein TRXR-1 and GSR-1 are essential for removal of old cuticle during molting in Caenorhabditis elegans. Proc Natl. Acad. Sci. USA. 2011;108:1064–1069. PubMed PMC
Bhatla N., Horvitz H.R. Light and hydrogen peroxide inhibit C. elegans Feeding through gustatory receptor orthologs and pharyngeal neurons. Neuron. 2015;85:804–818. PubMed PMC
Olahova M., Veal E.A. A peroxiredoxin, PRDX-2, is required for insulin secretion and insulin/IIS-dependent regulation of stress resistance and longevity. Aging Cell. 2015;14:558–568. PubMed PMC
Shadel G.S., Horvath T.L. Mitochondrial ROS signaling in organismal homeostasis. Cell. 2015;163:560–569. PubMed PMC
Blackwell T.K., Steinbaugh M.J., Hourihan J.M., Ewald C.Y., Isik M. SKN-1/Nrf, stress responses, and aging in Caenorhabditis elegans. Free Radic. Biol. Med. 2015;88:290–301. PubMed PMC
Lapierre L.R., Hansen M. Lessons from C. elegans: signaling pathways for longevity. Trends Endocrinol. Metab. 2012;23:637–644. PubMed PMC
Cabreiro F., Gems D. Worms need microbes too: microbiota, health and aging in Caenorhabditis elegans. EMBO Mol. Med. 2013;5:1300–1310. PubMed PMC
Knoefler D., Thamsen M., Koniczek M., Niemuth N.J., Diederich A.K., Jakob U. Quantitative in vivo redox sensors uncover oxidative stress as an early event in life. Mol. Cell. 2012;47:767–776. PubMed PMC
Yang J., Carroll K.S., Liebler D.C. The expanding landscape of the thiol redox proteome. Mol. Cell Proteom. 2016;15:1–11. PubMed PMC
Truong T.H., Carroll K.S. Redox regulation of protein kinases. Crit. Rev. Biochem. Mol. Biol. 2013;48:332–356. PubMed PMC
Westermarck J., Ivaska J., Corthals G.L. Identification of protein interactions involved in cellular signaling. Mol. Cell Proteom. 2013;12:1752–1763. PubMed PMC
Arts I.S., Vertommen D., Baldin F., Laloux G., Collet J.F. Comprehensively characterizing the thioredoxin interactome in vivo highlights the central role played by this ubiquitous oxidoreductase in redox control. Mol. Cell Proteom. 2016;15:2125–2140. PubMed PMC
Bartolini D., Galli F. The functional interactome of GSTP: a regulatory biomolecular network at the interface with the Nrf2 adaption response to oxidative stress. J. Chromatogr. B Anal. Technol. Biomed. Life Sci. 2016;1019:29–44. PubMed
Zolotukhin P., Kozlova Y., Dovzhik A., Kovalenko K., Kutsyn K., Aleksandrova A., Shkurat T. Oxidative status interactome map: towards novel approaches in experiment planning, data analysis, diagnostics and therapy. Mol. Biosyst. 2013;9:2085–2096. PubMed
Verrastro I., Tveen-Jensen K., Woscholski R., Spickett C.M., Pitt A.R. Reversible oxidation of phosphatase and tensin homolog (PTEN) alters its interactions with signaling and regulatory proteins. Free Radic. Biol. Med. 2016;90:24–34. PubMed
Petry A., Djordjevic T., Weitnauer M., Kietzmann T., Hess J., Gorlach A. NOX2 and NOX4 mediate proliferative response in endothelial cells. Antioxid. Redox Signal. 2006;8:1473–1484. PubMed
Rzymski T., Petry A., Kracun D., Riess F., Pike L., Harris A.L., Gorlach A. The unfolded protein response controls induction and activation of ADAM17/TACE by severe hypoxia and ER stress. Oncogene. 2012;31:3621–3634. PubMed
Janiszewski M., Lopes L.R., Carmo A.O., Pedro M.A., Brandes R.P., Santos C.X., Laurindo F.R. Regulation of NAD(P)H oxidase by associated protein disulfide isomerase in vascular smooth muscle cells. J. Biol. Chem. 2005;280:40813–40819. PubMed
He C., Zhu H., Zhang W., Okon I., Wang Q., Li H., Le Y.Z., Xie Z. 7-Ketocholesterol induces autophagy in vascular smooth muscle cells through Nox4 and Atg4B. Am. J. Pathol. 2013;183:626–637. PubMed PMC
Pedruzzi E., Guichard C., Ollivier V., Driss F., Fay M., Prunet C., Marie J.C., Pouzet C., Samadi M., Elbim C., O'Dowd Y., Bens M., Vandewalle A., Gougerot-Pocidalo M.A., Lizard G., Ogier-Denis E. NAD(P)H oxidase Nox-4 mediates 7-ketocholesterol-induced endoplasmic reticulum stress and apoptosis in human aortic smooth muscle cells. Mol. Cell Biol. 2004;24:10703–10717. PubMed PMC
Santos C.X., Hafstad A.D., Beretta M., Zhang M., Molenaar C., Kopec J., Fotinou D., Murray T.V., Cobb A.M., Martin D., Zeh Silva M., Anilkumar N., Schroder K., Shanahan C.M., Brewer A.C., Brandes R.P., Blanc E., Parsons M., Belousov V., Cammack R., Hider R.C., Steiner R.A., Shah A.M. Targeted redox inhibition of protein phosphatase 1 by Nox4 regulates eIF2alpha-mediated stress signaling. EMBO J. 2016;35:319–334. PubMed PMC
Li B., Tian J., Sun Y., Xu T.R., Chi R.F., Zhang X.L., Hu X.L., Zhang Y.A., Qin F.Z., Zhang W.F. Activation of NADPH oxidase mediates increased endoplasmic reticulum stress and left ventricular remodeling after myocardial infarction in rabbits. Biochim. Biophys. Acta. 2015;1852:805–815. PubMed
Li G., Scull C., Ozcan L., Tabas I. NADPH oxidase links endoplasmic reticulum stress, oxidative stress, and PKR activation to induce apoptosis. J. Cell Biol. 2010;191:1113–1125. PubMed PMC
Pavoine C., Pecker F. Sphingomyelinases: their regulation and roles in cardiovascular pathophysiology. Cardiovasc. Res. 2009;82:175–183. PubMed PMC
Corda S., Laplace C., Vicaut E., Duranteau J. Rapid reactive oxygen species production by mitochondria in endothelial cells exposed to tumor necrosis factor-alpha is mediated by ceramide. Am. J. Respir. Cell Mol. Biol. 2001;24:762–768. PubMed
Lecour S., der Merwe Van, Opie E., Sack L.H., Ceramide M.N. attenuates hypoxic cell death via reactive oxygen species signaling. J. Cardiovasc. Pharmacol. 2006;47:158–163. PubMed
Won J.S., Im Y.B., Khan M., Singh A.K., Singh I. The role of neutral sphingomyelinase produced ceramide in lipopolysaccharide-mediated expression of inducible nitric oxide synthase. J. Neurochem. 2004;88:583–593. PubMed
Hernandez O.M., Discher D.J., Bishopric N.H., Webster K.A. Rapid activation of neutral sphingomyelinase by hypoxia-reoxygenation of cardiac myocytes. Circ. Res. 2000;86:198–204. PubMed
Unal B., Ozcan F., Tuzcu H., Kirac E., Elpek G.O., Aslan M. Inhibition of neutral sphingomyelinase decreases elevated levels of nitrative and oxidative stress markers in liver ischemia-reperfusion injury. Redox Rep. 2016:1–13. PubMed PMC
Adamy C., Mulder P., Khouzami L., Andrieu-abadie N., Defer N., Candiani G., Pavoine C., Caramelle P., Souktani R., Le Corvoisier P., Perier M., Kirsch M., Damy T., Berdeaux A., Levade T., Thuillez C., Hittinger L., Pecker F. Neutral sphingomyelinase inhibition participates to the benefits of N-acetylcysteine treatment in post-myocardial infarction failing heart rats. J. Mol. Cell Cardiol. 2007;43:344–353. PubMed
Sawai H., Hannun Y.A. Ceramide and sphingomyelinases in the regulation of stress responses. Chem. Phys. Lipids. 1999;102:141–147. PubMed
Perrotta C., Clementi E. Biological roles of Acid and neutral sphingomyelinases and their regulation by nitric oxide. Physiology. 2010;25:64–71. PubMed
Pahan K., Sheikh F.G., Khan M., Namboodiri A.M., Singh I. Sphingomyelinase and ceramide stimulate the expression of inducible nitric-oxide synthase in rat primary astrocytes. J. Biol. Chem. 1998;273:2591–2600. PubMed
Katsuyama K., Shichiri M., Marumo F., Hirata Y. Role of nuclear factor-kappaB activation in cytokine- and sphingomyelinase-stimulated inducible nitric oxide synthase gene expression in vascular smooth muscle cells. Endocrinology. 1998;139:4506–4512. PubMed
Yang M.S., Jou I., Inn-Oc H., Joe E. Sphingomyelinase but not ceramide induces nitric oxide synthase expression in rat brain microglia. Neurosci. Lett. 2001;311:133–136. PubMed
Aslan M., Basaranlar G., Unal M., Ciftcioglu A., Derin N., Mutus B. Inhibition of neutral sphingomyelinase decreases elevated levels of inducible nitric oxide synthase and apoptotic cell death in ocular hypertensive rats. Toxicol. Appl. Pharmacol. 2014;280:389–398. PubMed
Masseret E., Banack S., Boumediene F., Abadie E., Brient L., Pernet F., Juntas-Morales R., Pageot N., Metcalf J., Cox P., Camu W., French Network on, A. L. S. C. D. Investigation Dietary BMAA exposure in an amyotrophic lateral sclerosis cluster from southern France. PLoS ONE. 2013;8:e83406. PubMed PMC
Huang X., Chen L., Liu W., Qiao Q., Wu K., Wen J., Huang C., Tang R., Zhang X. Involvement of oxidative stress and cytoskeletal disruption in microcystin-induced apoptosis in CIK cells. Aquat. Toxicol. 2015;165:41–50. PubMed
Krakstad C., Herfindal L., Gjertsen B.T., Boe R., Vintermyr O.K., Fladmark K.E., Doskeland S.O. CaM-kinaseII-dependent commitment to microcystin-induced apoptosis is coupled to cell budding, but not to shrinkage or chromatin hypercondensation. Cell Death Differ. 2006;13:1191–1202. PubMed
Hjornevik L.V., Fismen L., Young F.M., Solstad T., Fladmark K.E. Nodularin exposure induces SOD1 phosphorylation and disrupts SOD1 co-localization with actin filaments. Toxins. 2012;4:1482–1499. PubMed PMC
Okle O., Stemmer K., Deschl U., Dietrich D.R. L-BMAA induced ER stress and enhanced caspase 12 cleavage in human neuroblastoma SH-SY5Y cells at low nonexcitotoxic concentrations. Toxicol. Sci. 2013;131:217–224. PubMed
Chiu A.S., Gehringer M.M., Braidy N., Guillemin G.J., Welch J.H., Neilan B.A. Excitotoxic potential of the cyanotoxin beta-methyl-amino-L-alanine (BMAA) in primary human neurons. Toxicon. 2012;60:1159–1165. PubMed
Erickson J.R., Joiner M.L., Guan X., Kutschke W., Yang J., Oddis C.V., Bartlett R.K., Lowe J.S., O'Donnell S.E., Aykin-Burns N., Zimmerman M.C., Zimmerman K., Ham A.J., Weiss R.M., Spitz D.R., Shea M.A., Colbran R.J., Mohler P.J., Anderson M.E. A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation. Cell. 2008;133:462–474. PubMed PMC
Arif M., Kazim S.F., Grundke-Iqbal I., Garruto R.M., Iqbal K. Tau pathology involves protein phosphatase 2A in parkinsonism-dementia of Guam. Proc. Natl. Acad. Sci. USA. 2014;111:1144–1149. PubMed PMC
Raka F., Di Sebastiano A.R., Kulhawy S.C., Ribeiro F.M., Godin C.M., Caetano F.A., Angers S., Ferguson S.S. Ca(2+)/calmodulin-dependent protein kinase II interacts with group I metabotropic glutamate and facilitates receptor endocytosis and ERK1/2 signaling: role of beta-amyloid. Mol. Brain. 2015;8:21. PubMed PMC
Fahey R.C. Glutathione analogs in prokaryotes. Biochim. Biophys. Acta. 2013;1830:3182–3198. PubMed
Loi V.V., Rossius M., Antelmann H. Redox regulation by reversible protein S-thiolation in bacteria. Front. Microbiol. 2015;6:187. PubMed PMC
Lee J.W., Soonsanga S., Helmann J.D. A complex thiolate switch regulates the Bacillus subtilis organic peroxide sensor OhrR. Proc. Natl. Acad. Sci. USA. 2007;104:8743–8748. PubMed PMC
Gaballa A., Chi B.K., Roberts A.A., Becher D., Hamilton C.J., Antelmann H., Helmann J.D. Redox regulation in Bacillus subtilis: the bacilliredoxins BrxA(YphP) and BrxB(YqiW) function in de-bacillithiolation of S-bacillithiolated OhrR and MetE. Antioxid. Redox Signal. 2014;21:357–367. PubMed PMC
Chi B.K., Busche T., Van Laer K., Basell K., Becher D., Clermont L., Seibold G.M., Persicke M., Kalinowski J., Messens J., Antelmann H. Protein S-mycothiolation functions as redox-switch and thiol protection mechanism in Corynebacterium glutamicum under hypochlorite stress. Antioxid. Redox Signal. 2014;20:589–605. PubMed PMC
Pedre B., Van Molle I., Villadangos A.F., Wahni K., Vertommen D., Turell L., Erdogan H., Mateos L.M., Messens J. The Corynebacterium glutamicum mycothiol peroxidase is a reactive oxygen species-scavenging enzyme that shows promiscuity in thiol redox control. Mol. Microbiol. 2015;96:1176–1191. PubMed
Tossounian M.A., Pedre B., Wahni K., Erdogan H., Vertommen D., Van Molle I., Messens J. Corynebacterium diphtheriae methionine sulfoxide reductase a exploits a unique mycothiol redox relay mechanism. J. Biol. Chem. 2015;290:11365–11375. PubMed PMC
Gilroy S., Suzuki N., Miller G., Choi W.G., Toyota M., Devireddy A.R., Mittler R. A tidal wave of signals: calcium and ROS at the forefront of rapid systemic signaling. Trends Plant Sci. 2014;19:623–630. PubMed
Calabrese E.J., Iavicoli I., Calabrese V. Hormesis: its impact on medicine and health. Hum. Exp. Toxicol. 2013;32:120–152. PubMed
Yelisyeyeva O., Semen K., Zarkovic N., Kaminskyy D., Lutsyk O., Rybalchenko V. Activation of aerobic metabolism by Amaranth oil improves heart rate variability both in athletes and patients with type 2 diabetes mellitus. Arch. Physiol. Biochem. 2012;118:47–57. PubMed
Chouchani E.T., Pell V.R., Gaude E., Aksentijevic D., Sundier S.Y., Robb E.L., Logan A., Nadtochiy S.M., Ord E.N., Smith A.C., Eyassu F., Shirley R., Hu C.H., Dare A.J., James A.M., Rogatti S., Hartley R.C., Eaton S., Costa A.S., Brookes P.S., Davidson S.M., Duchen M.R., Saeb-Parsy K., Shattock M.J., Robinson A.J., Work L.M., Frezza C., Krieg T., Murphy M.P. Ischaemic accumulation of succinate controls reperfusion injury through mitochondrial ROS. Nature. 2014;515:431–435. PubMed PMC
Yin F., Sancheti H., Liu Z., Cadenas E. Mitochondrial function in ageing: coordination with signalling and transcriptional pathways. J. Physiol. 2016;594:2025–2042. PubMed PMC
Go Y.M., Jones D.P. The redox proteome. J. Biol. Chem. 2013;288:26512–26520. PubMed PMC
Buettner G.R., Wagner B.A., Rodgers V.G. Quantitative redox biology: an approach to understand the role of reactive species in defining the cellular redox environment. Cell Biochem. Biophys. 2013;67:477–483. PubMed PMC
Pillay C.S., Eagling B.D., Driscoll S.R., Rohwer J.M. Quantitative measures for redox signaling. Free Radic. Biol. Med. 2016;96:290–303. PubMed
Marinho H.S., Real C., Cyrne L., Soares H., Antunes F. Hydrogen peroxide sensing, signaling and regulation of transcription factors. Redox Biol. 2014;2:535–562. PubMed PMC
Rodrigo R., Libuy M., Feliu F., Hasson D. Oxidative stress-related biomarkers in essential hypertension and ischemia-reperfusion myocardial damage. Dis. Markers. 2013;35:773–790. PubMed PMC
Leonetti D., Reimund J.M., Tesse A., Viennot S., Martinez M.C., Bretagne A.L., Andriantsitohaina R. Circulating microparticles from Crohn's disease patients cause endothelial and vascular dysfunctions. PLoS One. 2013;8:e73088. PubMed PMC
Bhullar J., Bhopale V.M., Yang M., Sethuraman K., Thom S.R. Microparticle formation by platelets exposed to high gas pressures – an oxidative stress response. Free Radic. Biol. Med. 2016;101:154–162. PubMed
Han W.Q., Chang F.J., Wang Q.R., Pan J.Q. Microparticles from patients with the acute coronary syndrome impair vasodilatation by inhibiting the Akt/eNOS-Hsp90 signaling pathway. Cardiology. 2015;132:252–260. PubMed
Pitanga T.N., de Aragao Franca L., Rocha V.C., Meirelles T., Borges V.M., Goncalves M.S., Pontes-de-Carvalho L.C., Noronha-Dutra A.A., dos-Santos W.L. Neutrophil-derived microparticles induce myeloperoxidase-mediated damage of vascular endothelial cells. BMC Cell Biol. 2014;15:21. PubMed PMC
Fleury A., Martinez M.C., Le Lay S. Extracellular vesicles as therapeutic tools in cardiovascular diseases. Front. Immunol. 2014;5:370. PubMed PMC
Burger D., Kwart D.G., Montezano A.C., Read N.C., Kennedy C.R., Thompson C.S., Touyz R.M. Microparticles induce cell cycle arrest through redox-sensitive processes in endothelial cells: implications in vascular senescence. J. Am. Heart Assoc. 2012;1:e001842. PubMed PMC
Burger D., Turner M., Munkonda M.N., Touyz R.M. Endothelial microparticle-derived reactive oxygen species: role in endothelial signaling and vascular function. Oxid. Med. Cell Longev. 2016;2016:5047954. PubMed PMC
Safiedeen Z., Rodriguez-Gomez I., Vergori L., Soleti R., Vaithilingam D., Douma I., Agouni A., Leiber D., Dubois S., Simard G., Zibara K., Andriantsitohaina R., Martinez M.C. Temporal cross talk between endoplasmic reticulum and mitochondria regulates oxidative stress and mediates microparticle-induced endothelial dysfunction. Antioxid. Redox Signal. 2017;26:15–27. PubMed
Cai H. Hydrogen peroxide regulation of endothelial function: origins, mechanisms, and consequences. Cardiovasc. Res. 2005;68:26–36. PubMed
Skinner H.D., Zheng J.Z., Fang J., Agani F., Jiang B.H. Vascular endothelial growth factor transcriptional activation is mediated by hypoxia-inducible factor 1alpha, HDM2, and p70S6K1 in response to phosphatidylinositol 3-kinase/AKT signaling. J. Biol. Chem. 2004;279:45643–45651. PubMed
Ryu J.H., Li S.H., Park H.S., Park J.W., Lee B., Chun Y.S. Hypoxia-inducible factor alpha subunit stabilization by NEDD8 conjugation is reactive oxygen species-dependent. J. Biol. Chem. 2011;286:6963–6970. PubMed PMC
Patel S.A., Simon M.C. Biology of hypoxia-inducible factor-2alpha in development and disease. Cell Death Differ. 2008;15:628–634. PubMed PMC
Arany Z., Foo S.Y., Ma Y., Ruas J.L., Bommi-Reddy A., Girnun G., Cooper M., Laznik D., Chinsomboon J., Rangwala S.M., Baek K.H., Rosenzweig A., Spiegelman B.M. HIF-independent regulation of VEGF and angiogenesis by the transcriptional coactivator PGC-1alpha. Nature. 2008;451:1008–1012. PubMed
Ushio-Fukai M., Alexander R.W. Reactive oxygen species as mediators of angiogenesis signaling: role of NAD(P)H oxidase. Mol. Cell Biochem. 2004;264:85–97. PubMed
Colavitti R., Pani G., Bedogni B., Anzevino R., Borrello S., Waltenberger J., Galeotti T. Reactive oxygen species as downstream mediators of angiogenic signaling by vascular endothelial growth factor receptor-2/KDR. J. Biol. Chem. 2002;277:3101–3108. PubMed
Kang D.H., Lee D.J., Lee K.W., Park Y.S., Lee J.Y., Lee S.H., Koh Y.J., Koh G.Y., Choi C., Yu D.Y., Kim J., Kang S.W. Peroxiredoxin II is an essential antioxidant enzyme that prevents the oxidative inactivation of VEGF receptor-2 in vascular endothelial cells. Mol. Cell. 2011;44:545–558. PubMed
Tonks N.K. Redox redux: revisiting PTPs and the control of cell signaling. Cell. 2005;121:667–670. PubMed
Oshikawa J., Urao N., Kim H.W., Kaplan N., Razvi M., McKinney R., Poole L.B., Fukai T., Ushio-Fukai M. Extracellular SOD-derived H2O2 promotes VEGF signaling in caveolae/lipid rafts and post-ischemic angiogenesis in mice. PLoS One. 2010;5:e10189. PubMed PMC
Abid M.R., Spokes K.C., Shih S.C., Aird W.C. NADPH oxidase activity selectively modulates vascular endothelial growth factor signaling pathways. J. Biol. Chem. 2007;282:35373–35385. PubMed
Kobayashi S., Nojima Y., Shibuya M., Maru Y. Nox1 regulates apoptosis and potentially stimulates branching morphogenesis in sinusoidal endothelial cells. Exp. Cell Res. 2004;300:455–462. PubMed
Ushio-Fukai M., Tang Y., Fukai T., Dikalov S.I., Ma Y., Fujimoto M., Quinn M.T., Pagano P.J., Johnson C., Alexander R.W. Novel role of gp91(phox)-containing NAD(P)H oxidase in vascular endothelial growth factor-induced signaling and angiogenesis. Circ. Res. 2002;91:1160–1167. PubMed
Tojo T., Ushio-Fukai M., Yamaoka-Tojo M., Ikeda S., Patrushev N., Alexander R.W. Role of gp91phox (Nox2)-containing NAD(P)H oxidase in angiogenesis in response to hindlimb ischemia. Circulation. 2005;111:2347–2355. PubMed
Datla S.R., Peshavariya H., Dusting G.J., Mahadev K., Goldstein B.J., Jiang F. Important role of Nox4 type NADPH oxidase in angiogenic responses in human microvascular endothelial cells in vitro. Arterioscler. Thromb. Vasc. Biol. 2007;27:2319–2324. PubMed
Yamaoka-Tojo M., Tojo T., Kim H.W., Hilenski L., Patrushev N.A., Zhang L., Fukai T., Ushio-Fukai M. IQGAP1 mediates VE-cadherin-based cell-cell contacts and VEGF signaling at adherence junctions linked to angiogenesis. Arterioscler. Thromb. Vasc. Biol. 2006;26:1991–1997. PubMed
Ikeda S., Yamaoka-Tojo M., Hilenski L., Patrushev N.A., Anwar G.M., Quinn M.T., Ushio-Fukai M. IQGAP1 regulates reactive oxygen species-dependent endothelial cell migration through interacting with Nox2. Arterioscler. Thromb. Vasc. Biol. 2005;25:2295–2300. PubMed
Wang Y., Zang Q.S., Liu Z., Wu Q., Maass D., Dulan G., Shaul P.W., Melito L., Frantz D.E., Kilgore J.A., Williams N.S., Terada L.S., Nwariaku F.E. Regulation of VEGF-induced endothelial cell migration by mitochondrial reactive oxygen species. Am. J. Physiol. Cell Physiol. 2011;301:C695–C704. PubMed PMC
Borniquel S., Garcia-Quintans N., Valle I., Olmos Y., Wild B., Martinez-Granero F., Soria E., Lamas S., Monsalve M. Inactivation of Foxo3a and subsequent downregulation of PGC-1 alpha mediate nitric oxide-induced endothelial cell migration. Mol. Cell Biol. 2010;30:4035–4044. PubMed PMC
Garcia-Quintans N., Prieto I., Sanchez-Ramos C., Luque A., Arza E., Olmos Y., Monsalve M. Regulation of endothelial dynamics by PGC-1alpha relies on ROS control of VEGF-A signaling. Free Radic. Biol. Med. 2016;93:41–51. PubMed
Garcia-Quintans N., Sanchez-Ramos C., Prieto I., Tierrez A., Arza E., Alfranca A., Redondo J.M., Monsalve M. Oxidative stress induces loss of pericyte coverage and vascular instability in PGC-1alpha-deficient mice. Angiogenesis. 2016;19:217–228. PubMed
Massague J. TGFbeta signalling in context. Nat. Rev. Mol. Cell Biol. 2012;13:616–630. PubMed PMC
Fabregat I., Moreno-Caceres J., Sanchez A., Dooley S., Dewidar B., Giannelli G., Ten Dijke P., Consortium I.-L. TGF-beta signalling and liver disease. FEBS J. 2016;283:2219–2232. PubMed
Sanchez A., Alvarez A.M., Benito M., Fabregat I. Apoptosis induced by transforming growth factor-beta in fetal hepatocyte primary cultures: involvement of reactive oxygen intermediates. J. Biol. Chem. 1996;271:7416–7422. PubMed
Thannickal V.J., Fanburg B.L. Activation of an H2O2-generating NADH oxidase in human lung fibroblasts by transforming growth factor beta 1. J. Biol. Chem. 1995;270:30334–30338. PubMed
Herrera B., Murillo M.M., Alvarez-Barrientos A., Beltran J., Fernandez M., Fabregat I. Source of early reactive oxygen species in the apoptosis induced by transforming growth factor-beta in fetal rat hepatocytes. Free Radic. Biol. Med. 2004;36:16–26. PubMed
Carmona-Cuenca I., Roncero C., Sancho P., Caja L., Fausto N., Fernandez M., Fabregat I. Upregulation of the NADPH oxidase NOX4 by TGF-beta in hepatocytes is required for its pro-apoptotic activity. J. Hepatol. 2008;49:965–976. PubMed
Carnesecchi S., Deffert C., Donati Y., Basset O., Hinz B., Preynat-Seauve O., Guichard C., Arbiser J.L., Banfi B., Pache J.C., Barazzone-Argiroffo C., Krause K.H. A key role for NOX4 in epithelial cell death during development of lung fibrosis. Antioxid. Redox Signal. 2011;15:607–619. PubMed PMC
Moreno-Caceres J., Mainez J., Mayoral R., Martin-Sanz P., Egea G., Fabregat I. Caveolin-1-dependent activation of the metalloprotease TACE/ADAM17 by TGF-beta in hepatocytes requires activation of Src and the NADPH oxidase NOX1. FEBS J. 2016;283:1300–1310. PubMed
Sancho P., Bertran E., Caja L., Carmona-Cuenca I., Murillo M.M., Fabregat I. The inhibition of the epidermal growth factor (EGF) pathway enhances TGF-beta-induced apoptosis in rat hepatoma cells through inducing oxidative stress coincident with a change in the expression pattern of the NADPH oxidases (NOX) isoforms. Biochim. Biophys. Acta. 2009;1793:253–263. PubMed
Boudreau H.E., Casterline B.W., Rada B., Korzeniowska A., Leto T.L. Nox4 involvement in TGF-beta and SMAD3-driven induction of the epithelial-to-mesenchymal transition and migration of breast epithelial cells. Free Radic. Biol. Med. 2012;53:1489–1499. PubMed PMC
Cucoranu I., Clempus R., Dikalova A., Phelan P.J., Ariyan S., Dikalov S., Sorescu D. NAD(P)H oxidase 4 mediates transforming growth factor-beta1-induced differentiation of cardiac fibroblasts into myofibroblasts. Circ. Res. 2005;97:900–907. PubMed
Hecker L., Vittal R., Jones T., Jagirdar R., Luckhardt T.R., Horowitz J.C., Pennathur S., Martinez F.J., Thannickal V.J. NADPH oxidase-4 mediates myofibroblast activation and fibrogenic responses to lung injury. Nat. Med. 2009;15:1077–1081. PubMed PMC
Sancho P., Mainez J., Crosas-Molist E., Roncero C., Fernandez-Rodriguez C.M., Pinedo F., Huber H., Eferl R., Mikulits W., Fabregat I. NADPH oxidase NOX4 mediates stellate cell activation and hepatocyte cell death during liver fibrosis development. PLoS One. 2012;7:e45285. PubMed PMC
Crosas-Molist E., Bertran E., Sancho P., Lopez-Luque J., Fernando J., Sanchez A., Fernandez M., Navarro E., Fabregat I. The NADPH oxidase NOX4 inhibits hepatocyte proliferation and liver cancer progression. Free Radic. Biol. Med. 2014;69:338–347. PubMed
Liou G.Y., Storz P. Reactive oxygen species in cancer. Free Radic. Res. 2010;44:479–496. PubMed PMC
Panieri E., Santoro M.M. ROS homeostasis and metabolism: a dangerous liaison in cancer cells. Cell Death Dis. 2016;7:e2253. PubMed PMC
Rojas-Rivera D., Hetz C. TMBIM protein family: ancestral regulators of cell death. Oncogene. 2015;34:269–280. PubMed
Hu L., Smith T.F., Goldberger G. LFG: a candidate apoptosis regulatory gene family. Apoptosis. 2009;14:1255–1265. PubMed
Carrara G., Saraiva N., Gubser C., Johnson B.F., Smith G.L. Six-transmembrane topology for Golgi anti-apoptotic protein (GAAP) and Bax inhibitor 1 (BI-1) provides model for the transmembrane Bax inhibitor-containing motif (TMBIM) family. J. Biol. Chem. 2012;287:15896–15905. PubMed PMC
Carrara G., Saraiva N., Parsons M., Byrne B., Prole D.L., Taylor C.W., Smith G.L. Golgi anti-apoptotic proteins are highly conserved ion channels that affect apoptosis and cell migration. J. Biol. Chem. 2015;290:11785–11801. PubMed PMC
Gubser C., Bergamaschi D., Hollinshead M., Lu X., van Kuppeveld F.J., Smith G.L. A new inhibitor of apoptosis from vaccinia virus and eukaryotes. PLoS Pathog. 2007;3:e17. PubMed PMC
Gubser C., Smith G.L. The sequence of camelpox virus shows it is most closely related to variola virus, the cause of smallpox. J. Gen. Virol. 2002;83:855–872. PubMed
de Mattia F., Gubser C., van Dommelen M.M., Visch H.J., Distelmaier F., Postigo A., Luyten T., Parys J.B., de Smedt H., Smith G.L., Willems P.H., van Kuppeveld F.J. Human Golgi antiapoptotic protein modulates intracellular calcium fluxes. Mol. Biol. Cell. 2009;20:3638–3645. PubMed PMC
Saraiva N., Prole D.L., Carrara G., Johnson B.F., Taylor C.W., Parsons M., Smith G.L. hGAAP promotes cell adhesion and migration via the stimulation of store-operated Ca2+ entry and calpain 2. J. Cell Biol. 2013;202:699–713. PubMed PMC
Boveri T. Concerning the origin of malignant tumours by Theodor Boveri. Translated and annotated by Henry Harris. J. Cell Sci. 2008;121(Suppl 1):S1–S84. PubMed
Basto R., Brunk K., Vinadogrova T., Peel N., Franz A., Khodjakov A., Raff J.W. Centrosome amplification can initiate tumorigenesis in flies. Cell. 2008;133:1032–1042. PubMed PMC
Fukasawa K. Centrosome amplification, chromosome instability and cancer development. Cancer Lett. 2005;230:6–19. PubMed
Nigg E.A., Stearns T. The centrosome cycle: centriole biogenesis, duplication and inherent asymmetries. Nat. Cell Biol. 2011;13:1154–1160. PubMed PMC
Chae S., Yun C., Um H., Lee J.H., Cho H. Centrosome amplification and multinuclear phenotypes are Induced by hydrogen peroxide. Exp. Mol. Med. 2005;37:482–487. PubMed
Ohshima S. Centrosome aberrations associated with cellular senescence and p53 localization at supernumerary centrosomes. Oxid. Med. Cell Longev. 2012;2012:217594. PubMed PMC
Manning J.A., Kumar S. A potential role for NEDD1 and the centrosome in senescence of mouse embryonic fibroblasts. Cell Death Dis. 2010;1:e35. PubMed PMC
Lim J.M., Lee K.S., Woo H.A., Kang D., Rhee S.G. Control of the pericentrosomal H2O2 level by peroxiredoxin I is critical for mitotic progression. J. Cell Biol. 2015;210:23–33. PubMed PMC
Ohshima S. Abnormal mitosis in hypertetraploid cells causes aberrant nuclear morphology in association with H2O2-induced premature senescence. Cytom. A. 2008;73:808–815. PubMed
Bindoli A., Rigobello M.P. Principles in redox signaling: from chemistry to functional significance. Antioxid. Redox Signal. 2013;18:1557–1593. PubMed
Biasutto L., Azzolini M., Szabo I., Zoratti M. The mitochondrial permeability transition pore in AD 2016: an update. Biochim. Biophys. Acta. 2016;1863:2515–2530. PubMed
Linard D., Kandlbinder A., Degand H., Morsomme P., Dietz K.J., Knoops B. Redox characterization of human cyclophilin D: identification of a new mammalian mitochondrial redox sensor? Arch. Biochem. Biophys. 2009;491:39–45. PubMed
Folda A., Citta A., Scalcon V., Cali T., Zonta F., Scutari G., Bindoli A., Rigobello M.P. Mitochondrial thioredoxin system as a modulator of cyclophilin D redox state. Sci. Rep. 2016;6:23071. PubMed PMC
Palikaras K., Tavernarakis N. Mitochondrial homeostasis: the interplay between mitophagy and mitochondrial biogenesis. Exp. Gerontol. 2014;56:182–188. PubMed
Ristow M., Zarse K. How increased oxidative stress promotes longevity and metabolic health: the concept of mitochondrial hormesis (mitohormesis) Exp. Gerontol. 2010;45:410–418. PubMed
Schulz T.J., Zarse K., Voigt A., Urban N., Birringer M., Ristow M. Glucose restriction extends Caenorhabditis elegans life span by inducing mitochondrial respiration and increasing oxidative stress. Cell Metab. 2007;6:280–293. PubMed
Dancy B.M., Sedensky M.M., Morgan P.G. Effects of the mitochondrial respiratory chain on longevity in C. elegans. Exp. Gerontol. 2014;56:245–255. PubMed
Marthandan S., Priebe S., Groth M., Guthke R., Platzer M., Hemmerich P., Diekmann S. Hormetic effect of rotenone in primary human fibroblasts. Immun. Ageing. 2015;12:11. PubMed PMC
Lamming D.W. Inhibition of the Mechanistic Target of Rapamycin (mTOR)-rapamycin and beyond. Cold Spring Harb. Perspect. Med. 2016;6 PubMed PMC
Song M., Chen Y., Gong G., Murphy E., Rabinovitch P.S., Dorn G.W., 2nd. Super-suppression of mitochondrial reactive oxygen species signaling impairs compensatory autophagy in primary mitophagic cardiomyopathy. Circ. Res. 2014;115:348–353. PubMed PMC
Gorlach A., Dimova E.Y., Petry A., Martinez-Ruiz A., Hernansanz-Agustin P., Rolo A.P., Palmeira C.M., Kietzmann T. Reactive oxygen species, nutrition, hypoxia and diseases: problems solved? Redox Biol. 2015;6:372–385. PubMed PMC
Fernández-Agüera M.C., Gao L., González-Rodríguez P., Pintado C.O., Arias-Mayenco I., García-Flores P., García-Pergañeda A., Pascual A., Ortega-Sáenz P., López-Barneo J. Oxygen sensing by arterial chemoreceptors depends on mitochondrial complex I signaling. Cell Metab. 2015;22:825–837. PubMed
Hernansanz-Agustin P., Izquierdo-Alvarez A., Sanchez-Gomez F.J., Ramos E., Villa-Pina T., Lamas S., Bogdanova A., Martinez-Ruiz A. Acute hypoxia produces a superoxide burst in cells. Free Radic. Biol. Med. 2014;71:146–156. PubMed
Yuan G., Vasavda C., Peng Y.J., Makarenko V.V., Raghuraman G., Nanduri J., Gadalla M.M., Semenza G.L., Kumar G.K., Snyder S.H., Prabhakar N.R. Protein kinase G-regulated production of H2S governs oxygen sensing. Sci. Signal. 2015;8:ra37. PubMed PMC
Moreno L., Moral-Sanz J., Morales-Cano D., Barreira B., Moreno E., Ferrarini A., Pandolfi R., Rupérez F.J., Cortijo J., Sánchez-Luna M., Villamor E., Perez-Vizcaíno F., Cogolludo A. Ceramide mediates acute oxygen sensing in vascular tissues. Antioxid. Redox Signal. 2014;20:1–14. PubMed PMC
Izquierdo-Álvarez A., Ramos E., Villanueva J., Hernansanz-Agustín P., Fernández-Rodríguez R., Tello D., Carrascal M., Martínez-Ruiz A. Differential redox proteomics allows identification of proteins reversibly oxidized at cysteine residues in endothelial cells in response to acute hypoxia. J. Proteom. 2012;75:5449–5462. PubMed
Bogdanova A., Petrushanko I.Y., Hernansanz-Agustin P., Martinez-Ruiz A. "Oxygen sensing" by Na,K-ATPase: these miraculous thiols. Front. Physiol. 2016;7:314. PubMed PMC
Forstermann U., Sessa W.C. Nitric oxide synthases: regulation and function. Eur. Heart J. 2012;33:829–837. (837a-837d) PubMed PMC
Jeffrey Man H.S., Tsui A.K., Marsden P.A. Nitric oxide and hypoxia signaling. Vitam. Horm. 2014;96:161–192. PubMed
Chalupsky K., Kracun D., Kanchev I., Bertram K., Gorlach A. Folic acid promotes recycling of tetrahydrobiopterin and protects against hypoxia-induced pulmonary hypertension by recoupling endothelial nitric oxide synthase. Antioxid. Redox Signal. 2015;23:1076–1091. PubMed PMC
Bendall J.K., Douglas G., McNeill E., Channon K.M., Crabtree M.J. Tetrahydrobiopterin in cardiovascular health and disease. Antioxid. Redox Signal. 2014;20:3040–3077. PubMed PMC
Gao L., Chalupsky K., Stefani E., Cai H. Mechanistic insights into folic acid-dependent vascular protection: dihydrofolate reductase (DHFR)-mediated reduction in oxidant stress in endothelial cells and angiotensin II-infused mice: a novel HPLC-based fluorescent assay for DHFR activity. J. Mol. Cell Cardiol. 2009;47:752–760. PubMed PMC
Dubois M., Delannoy E., Duluc L., Closs E., Li H., Toussaint C., Gadeau A.P., Godecke A., Freund-Michel V., Courtois A., Marthan R., Savineau J.P., Muller B. Biopterin metabolism and eNOS expression during hypoxic pulmonary hypertension in mice. PLoS One. 2013;8:e82594. PubMed PMC
Bigarella C.L., Liang R., Ghaffari S. Stem cells and the impact of ROS signaling. Development. 2014;141:4206–4218. PubMed PMC
Burgess R.J., Agathocleous M., Morrison S.J. Metabolic regulation of stem cell function. J. Intern. Med. 2014;276:12–24. PubMed PMC
Klotz L.O., Sanchez-Ramos C., Prieto-Arroyo I., Urbanek P., Steinbrenner H., Monsalve M. Redox regulation of FoxO transcription factors. Redox Biol. 2015;6:51–72. PubMed PMC
Higuchi M., Dusting G.J., Peshavariya H., Jiang F., Hsiao S.T., Chan E.C., Liu G.S. Differentiation of human adipose-derived stem cells into fat involves reactive oxygen species and Forkhead box O1 mediated upregulation of antioxidant enzymes. Stem Cells Dev. 2013;22:878–888. PubMed PMC
Circu M.L., Aw T.Y. Redox biology of the intestine. Free Radic. Res. 2011;45:1245–1266. PubMed PMC
Speckmann B., Pinto A., Winter M., Forster I., Sies H., Steinbrenner H. Proinflammatory cytokines down-regulate intestinal selenoprotein P biosynthesis via NOS2 induction. Free Radic. Biol. Med. 2010;49:777–785. PubMed
Walter P.L., Steinbrenner H., Barthel A., Klotz L.O. Stimulation of selenoprotein P promoter activity in hepatoma cells by FoxO1a transcription factor. Biochem. Biophys. Res. Commun. 2008;365:316–321. PubMed
Baird A.-M., O’Byrne K., Gray S. Reactive oxygen species and reactive nitrogen species in epigenetic modifications. In: Laher I., editor. Systems Biology of Free Radicals and Antioxidants. Springer Berlin Heidelberg; 2014. pp. 437–455.
Niu Y., DesMarais T.L., Tong Z., Yao Y., Costa M. Oxidative stress alters global histone modification and DNA methylation. Free Radic. Biol. Med. 2015;82:22–28. PubMed PMC
Mikhed Y., Gorlach A., Knaus U.G., Daiber A. Redox regulation of genome stability by effects on gene expression, epigenetic pathways and DNA damage/repair. Redox Biol. 2015;5:275–289. PubMed PMC
Ito K., Ito M., Elliott W.M., Cosio B., Caramori G., Kon O.M., Barczyk A., Hayashi S., Adcock I.M., Hogg J.C., Barnes P.J. Decreased histone deacetylase activity in chronic obstructive pulmonary disease. N. Engl. J. Med. 2005;352:1967–1976. PubMed
Valinluck V., Sowers L.C. Endogenous cytosine damage products alter the site selectivity of human DNA maintenance methyltransferase DNMT1. Cancer Res. 2007;67:946–950. PubMed
O'Hagan H.M., Wang W., Sen S., Destefano Shields C., Lee S.S., Zhang Y.W., Clements E.G., Cai Y., Van Neste L., Easwaran H., Casero R.A., Sears C.L., Baylin S.B. Oxidative damage targets complexes containing DNA methyltransferases, SIRT1, and polycomb members to promoter CpG Islands. Cancer Cell. 2011;20:606–619. PubMed PMC
Kim G.H., Ryan J.J., Archer S.L. The role of redox signaling in epigenetics and cardiovascular disease. Antioxid. Redox Signal. 2013;18:1920–1936. PubMed PMC
Archer S.L., Marsboom G., Kim G.H., Zhang H.J., Toth P.T., Svensson E.C., Dyck J.R., Gomberg-Maitland M., Thebaud B., Husain A.N., Cipriani N., Rehman J. Epigenetic attenuation of mitochondrial superoxide dismutase 2 in pulmonary arterial hypertension: a basis for excessive cell proliferation and a new therapeutic target. Circulation. 2010;121:2661–2671. PubMed PMC
Matsushima S., Kuroda J., Ago T., Zhai P., Park J.Y., Xie L.H., Tian B., Sadoshima J. Increased oxidative stress in the nucleus caused by Nox4 mediates oxidation of HDAC4 and cardiac hypertrophy. Circ. Res. 2013;112:651–663. PubMed PMC
Zhang Q.J., Chen H.Z., Wang L., Liu D.P., Hill J.A., Liu Z.P. The histone trimethyllysine demethylase JMJD2A promotes cardiac hypertrophy in response to hypertrophic stimuli in mice. J. Clin. Investig. 2011;121:2447–2456. PubMed PMC
Stein A.B., Jones T.A., Herron T.J., Patel S.R., Day S.M., Noujaim S.F., Milstein M.L., Klos M., Furspan P.B., Jalife J., Dressler G.R. Loss of H3K4 methylation destabilizes gene expression patterns and physiological functions in adult murine cardiomyocytes. J. Clin. Investig. 2011;121:2641–2650. PubMed PMC
Kaneda R., Takada S., Yamashita Y., Choi Y.L., Nonaka-Sarukawa M., Soda M., Misawa Y., Isomura T., Shimada K., Mano H. Genome-wide histone methylation profile for heart failure. Genes Cells. 2009;14:69–77. PubMed
Khan M.A., Alam K., Dixit K., Rizvi M.M. Role of peroxynitrite induced structural changes on H2B histone by physicochemical method. Int. J. Biol. Macromol. 2016;82:31–38. PubMed
Khan M.A., Dixit K., Jabeen S., Moinuddin, Alam K. Impact of peroxynitrite modification on structure and immunogenicity of H2A histone. Scand. J. Immunol. 2009;69:99–109. PubMed
Ambros V. The functions of animal microRNAs. Nature. 2004;431:350–355. PubMed
Bartel D.P. MicroRNAs: genomics, biogenesis, mechanism, and function. Cell. 2004;116:281–297. PubMed
Hayes J.D., Dinkova-Kostova A.T. The Nrf2 regulatory network provides an interface between redox and intermediary metabolism. Trends Biochem. Sci. 2014;39:199–218. PubMed
Levonen A.L., Hill B.G., Kansanen E., Zhang J., Darley-Usmar V.M. Redox regulation of antioxidants, autophagy, and the response to stress: implications for electrophile therapeutics. Free Radic. Biol. Med. 2014;71:196–207. PubMed PMC
Espinosa-Diez C., Miguel V., Mennerich D., Kietzmann T., Sanchez-Perez P., Cadenas S., Lamas S. Antioxidant responses and cellular adjustments to oxidative stress. Redox Biol. 2015;6:183–197. PubMed PMC
Cheng X., Ku C.H., Siow R.C. Regulation of the Nrf2 antioxidant pathway by microRNAs: new players in micromanaging redox homeostasis. Free Radic. Biol. Med. 2013;64:4–11. PubMed
Wynn T.A. Common and unique mechanisms regulate fibrosis in various fibroproliferative diseases. J. Clin. Investig. 2007;117:524–529. PubMed PMC
Tomasek J.J., Gabbiani G., Hinz B., Chaponnier C., Brown R.A. Myofibroblasts and mechano-regulation of connective tissue remodelling. Nat. Rev. Mol. Cell Biol. 2002;3:349–363. PubMed
Leask A., Abraham D.J. TGF-beta signaling and the fibrotic response. FASEB J.: Off. Publ. Fed. Am. Soc. Exp. Biol. 2004;18:816–827. PubMed
Hinz B., Phan S.H., Thannickal V.J., Galli A., Bochaton-Piallat M.L., Gabbiani G. The myofibroblast: one function, multiple origins. Am. J. Pathol. 2007;170:1807–1816. PubMed PMC
Pottier N., Cauffiez C., Perrais M., Barbry P., Mari B. FibromiRs: translating molecular discoveries into new anti-fibrotic drugs. Trends Pharmacol. Sci. 2014;35:119–126. PubMed
O'Reilly S. MicroRNAs in fibrosis: opportunities and challenges. Arthritis Res. Ther. 2016;18:11. PubMed PMC
Davis B.N., Hilyard A.C., Lagna G., Hata A. SMAD proteins control DROSHA-mediated microRNA maturation. Nature. 2008;454:56–61. PubMed PMC
Fierro-Fernandez M., Miguel V., Lamas S. Role of redoximiRs in fibrogenesis. Redox Biol. 2016;7:58–67. PubMed PMC
Wei C., Li L., Kim I.K., Sun P., Gupta S. NF-kappaB mediated miR-21 regulation in cardiomyocytes apoptosis under oxidative stress. Free Radic. Res. 2014;48:282–291. PubMed
Thum T., Gross C., Fiedler J., Fischer T., Kissler S., Bussen M., Galuppo P., Just S., Rottbauer W., Frantz S., Castoldi M., Soutschek J., Koteliansky V., Rosenwald A., Basson M.A., Licht J.D., Pena J.T., Rouhanifard S.H., Muckenthaler M.U., Tuschl T., Martin G.R., Bauersachs J., Engelhardt S. MicroRNA-21 contributes to myocardial disease by stimulating MAP kinase signalling in fibroblasts. Nature. 2008;456:980–984. PubMed
Zhong X., Chung A.C., Chen H.Y., Meng X.M., Lan H.Y. Smad3-mediated upregulation of miR-21 promotes renal fibrosis. J. Am. Soc. Nephrol.: JASN. 2011;22:1668–1681. PubMed PMC
Wang B., Komers R., Carew R., Winbanks C.E., Xu B., Herman-Edelstein M., Koh P., Thomas M., Jandeleit-Dahm K., Gregorevic P., Cooper M.E., Kantharidis P. Suppression of microRNA-29 expression by TGF-beta1 promotes collagen expression and renal fibrosis. J. Am. Soc. Nephrol.: JASN. 2012;23:252–265. PubMed PMC
Cushing L., Kuang P., Lu J. The role of miR-29 in pulmonary fibrosis. Biochem. Cell Biol. Biochim. Biol. Cell. 2015;93:109–118. PubMed
Fierro-Fernandez M., Busnadiego O., Sandoval P., Espinosa-Diez C., Blanco-Ruiz E., Rodriguez M., Pian H., Ramos R., Lopez-Cabrera M., Garcia-Bermejo M.L., Lamas S. miR-9-5p suppresses pro-fibrogenic transformation of fibroblasts and prevents organ fibrosis by targeting NOX4 and TGFBR2. EMBO Rep. 2015;16:1358–1377. PubMed PMC
Miguel V., Busnadiego O., Fierro-Fernandez M., Lamas S. Protective role for miR-9-5p in the fibrogenic transformation of human dermal fibroblasts. Fibrogenes. Tissue Repair. 2016;9:7. PubMed PMC
Murakami Y., Toyoda H., Tanaka M., Kuroda M., Harada Y., Matsuda F., Tajima A., Kosaka N., Ochiya T., Shimotohno K. The progression of liver fibrosis is related with overexpression of the miR-199 and 200 families. PloS One. 2011;6:e16081. PubMed PMC
Espinosa-Diez C., Fierro-Fernandez M., Sanchez-Gomez F., Rodriguez-Pascual F., Alique M., Ruiz-Ortega M., Beraza N., Martinez-Chantar M.L., Fernandez-Hernando C., Lamas S. Targeting of gamma-glutamyl-cysteine ligase by miR-433 reduces glutathione biosynthesis and promotes TGF-beta-dependent fibrogenesis. Antioxid. Redox Signal. 2015;23:1092–1105. PubMed PMC
Chau B.N., Xin C., Hartner J., Ren S., Castano A.P., Linn G., Li J., Tran P.T., Kaimal V., Huang X., Chang A.N., Li S., Kalra A., Grafals M., Portilla D., MacKenna D.A., Orkin S.H., Duffield J.S. MicroRNA-21 promotes fibrosis of the kidney by silencing metabolic pathways. Sci. Transl. Med. 2012;4:121ra118. PubMed PMC
Gomez I.G., MacKenna D.A., Johnson B.G., Kaimal V., Roach A.M., Ren S., Nakagawa N., Xin C., Newitt R., Pandya S., Xia T.H., Liu X., Borza D.B., Grafals M., Shankland S.J., Himmelfarb J., Portilla D., Liu S., Chau B.N., Duffield J.S. Anti-microRNA-21 oligonucleotides prevent Alport nephropathy progression by stimulating metabolic pathways. J. Clin. Investig. 2015;125:141–156. PubMed PMC
Kang H.M., Ahn S.H., Choi P., Ko Y.A., Han S.H., Chinga F., Park A.S., Tao J., Sharma K., Pullman J., Bottinger E.P., Goldberg I.J., Susztak K. Defective fatty acid oxidation in renal tubular epithelial cells has a key role in kidney fibrosis development. Nat. Med. 2015;21:37–46. PubMed PMC
Bochkov V.N., Oskolkova O.V., Birukov K.G., Levonen A.L., Binder C.J., Stockl J. Generation and biological activities of oxidized phospholipids. Antioxid. Redox Signal. 2010;12:1009–1059. PubMed PMC
Greig F.H., Kennedy S., Spickett C.M. Physiological effects of oxidized phospholipids and their cellular signaling mechanisms in inflammation. Free Radic. Biol. Med. 2012;52:266–280. PubMed
Mauerhofer C., Philippova M., Oskolkova O.V., Bochkov V.N. Hormetic and anti-inflammatory properties of oxidized phospholipids. Mol. Asp. Med. 2016;49:78–90. PubMed
Leitinger N., Tyner T.R., Oslund L., Rizza C., Subbanagounder G., Lee H., Shih P.T., Mackman N., Tigyi G., Territo M.C., Berliner J.A., Vora D.K. Structurally similar oxidized phospholipids differentially regulate endothelial binding of monocytes and neutrophils. Proc. Natl. Acad. Sci. USA. 1999;96:12010–12015. PubMed PMC
Bretscher P., Egger J., Shamshiev A., Trotzmuller M., Kofeler H., Carreira E.M., Kopf M., Freigang S. Phospholipid oxidation generates potent anti-inflammatory lipid mediators that mimic structurally related pro-resolving eicosanoids by activating Nrf2. EMBO Mol. Med. 2015;7:593–607. PubMed PMC
Bochkov V.N., Kadl A., Huber J., Gruber F., Binder B.R., Leitinger N. Protective role of phospholipid oxidation products in endotoxin-induced tissue damage. Nature. 2002;419:77–81. PubMed
Dziubla T., Butterfield D.A. Academic Press; 2016. Oxidative Stress and Biomaterials.
Napoli A., Valentini M., Tirelli N., Muller M., Hubbell J.A. Oxidation-responsive polymeric vesicles. Nat. Mater. 2004;3:183–189. PubMed
Wattamwar P.P., Biswal D., Cochran D.B., Lyvers A.C., Eitel R.E., Anderson K.W., Hilt J.Z., Dziubla T.D. Synthesis and characterization of poly(antioxidant beta-amino esters) for controlled release of polyphenolic antioxidants. Acta Biomater. 2012;8:2529–2537. PubMed
Yang J., van Lith R., Baler K., Hoshi R.A., Ameer G.A. A thermoresponsive biodegradable polymer with intrinsic antioxidant properties. Biomacromolecules. 2014;15:3942–3952. PubMed
G. Svegliati Baroni, L. D’ Ambrosio, G. Ferretti, P. Biondi, A. Casini, A. Di Sario, S. Saccomanno, A.M. Jezequel, A. Benedetti, F. Orlandi, Proliferation of hepatic stellate cells and lipid peroxidation: changes due to polyphenols, in: P. Gentilini, M.U. Dianzani, (eds). New Trends in Hepatology: the Proceedings of the Annual Meeting of the Italian National Programme on Liver Cirrhosis and Viral Hepatitis, San Miniato (Pisa), Italy, 7–9 January 1996. Dordrecht: Springer Netherlands, 1996, pp. 93–103.
Mrakovcic L., Wildburger R., Jaganjac M., Cindric M., Cipak A., Borovic-Sunjic S., Waeg G., Milankovic A.M., Zarkovic N. Lipid peroxidation product 4-hydroxynonenal as factor of oxidative homeostasis supporting bone regeneration with bioactive glasses. Acta Biochim. Pol. 2010;57:173–178. PubMed
Aldini G., Domingues M.R., Spickett C.M., Domingues P., Altomare A., Sanchez-Gomez F.J., Oeste C.L., Perez-Sala D. Protein lipoxidation: detection strategies and challenges. Redox Biol. 2015;5:253–266. PubMed PMC
Magni F., Galbusera C., Tremolada L., Ferrarese C., Kienle M.G. Characterisation of adducts of the lipid peroxidation product 4-hydroxy-2-nonenal and amyloid beta-peptides by liquid chromatography/electrospray ionisation mass spectrometry. Rapid Commun. Mass Spectrom. 2002;16:1485–1493. PubMed
Colzani M., Aldini G., Carini M. Mass spectrometric approaches for the identification and quantification of reactive carbonyl species protein adducts. J. Proteom. 2013;92:28–50. PubMed
Verrastro I., Pasha S., Jensen K.T., Pitt A.R., Spickett C.M. Mass spectrometry-based methods for identifying oxidized proteins in disease: advances and challenges. Biomolecules. 2015;5:378–411. PubMed PMC
Milic I., Kipping M., Hoffmann R., Fedorova M. Separation and characterization of oxidized isomeric lipid-peptide adducts by ion mobility mass spectrometry. J. Mass Spectrom. 2015;50:1386–1392. PubMed
Wang R. Physiological implications of hydrogen sulfide: a whiff exploration that blossomed. Physiol. Rev. 2012;92:791–896. PubMed
Polhemus D.J., Lefer D.J. Emergence of hydrogen sulfide as an endogenous gaseous signaling molecule in cardiovascular disease. Circ. Res. 2014;114:730–737. PubMed PMC
Kabil O., Motl N., Banerjee R. H2S and its role in redox signaling. Biochim. Biophys. Acta. 2014;1844:1355–1366. PubMed PMC
Ju Y., Zhang W., Pei Y., Yang G. H(2)S signaling in redox regulation of cellular functions. Can. J. Physiol. Pharmacol. 2013;91:8–14. PubMed
Li Q., Lancaster J.R., Jr. Chemical foundations of hydrogen sulfide biology. Nitric Oxide. 2013;35:21–34. PubMed PMC
Cortese-Krott M.M., Fernandez B.O., Kelm M., Butler A.R., Feelisch M. On the chemical biology of the nitrite/sulfide interaction. Nitric Oxide. 2015;46:14–24. PubMed
Ma Q. Role of nrf2 in oxidative stress and toxicity. Annu. Rev. Pharmacol. Toxicol. 2013;53:401–426. PubMed PMC
Jazwa A., Cuadrado A. Targeting heme oxygenase-1 for neuroprotection and neuroinflammation in neurodegenerative diseases. Curr. Drug Targets. 2010;11:1517–1531. PubMed
Xie Z.Z., Liu Y., Bian J.S. Hydrogen sulfide and cellular redox homeostasis. Oxid. Med. Cell Longev. 2016;2016:6043038. PubMed PMC
Garcia-Garcia A., Rodriguez-Rocha H., Madayiputhiya N., Pappa A., Panayiotidis M.I., Franco R. Biomarkers of protein oxidation in human disease. Curr. Mol. Med. 2012;12:681–697. PubMed
Esterbauer H., Schaur R.J., Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic. Biol. Med. 1991;11:81–128. PubMed
Wall S.B., Oh J.Y., Diers A.R., Landar A. Oxidative modification of proteins: an emerging mechanism of cell signaling. Front. Physiol. 2012;3:369. PubMed PMC
Ullrich V., Kissner R. Redox signaling: bioinorganic chemistry at its best. J. Inorg. Biochem. 2006;100:2079–2086. PubMed
Calcerrada P., Peluffo G., Radi R. Nitric oxide-derived oxidants with a focus on peroxynitrite: molecular targets, cellular responses and therapeutic implications. Curr. Pharm. Des. 2011;17:3905–3932. PubMed
Bottari S.P. Protein tyrosine nitration: a signaling mechanism conserved from yeast to man. Proteomics. 2015;15:185–187. PubMed
Daiber A., Frein D., Namgaladze D., Ullrich V. Oxidation and nitrosation in the nitrogen monoxide/superoxide system. J. Biol. Chem. 2002;277:11882–11888. PubMed
Houee-Levin C., Bobrowski K., Horakova L., Karademir B., Schoneich C., Davies M.J., Spickett C.M. Exploring oxidative modifications of tyrosine: an update on mechanisms of formation, advances in analysis and biological consequences. Free Radic. Res. 2015;49:347–373. PubMed
Wehr N.B., Levine R.L. Wanted and wanting: antibody against methionine sulfoxide. Free Radic. Biol. Med. 2012;53:1222–1225. PubMed PMC
Ghesquiere B., Gevaert K. Proteomics methods to study methionine oxidation. Mass Spectrom. Rev. 2014;33:147–156. PubMed
Rocha B.S., Gago B., Barbosa R.M., Lundberg J.O., Radi R., Laranjinha J. Intragastric nitration by dietary nitrite: implications for modulation of protein and lipid signaling. Free Radic. Biol. Med. 2012;52:693–698. PubMed
Wayenberg J.L., Ransy V., Vermeylen D., Damis E., Bottari S.P. Nitrated plasma albumin as a marker of nitrative stress and neonatal encephalopathy in perinatal asphyxia. Free Radic. Biol. Med. 2009;47:975–982. PubMed
Wayenberg J.L., Cavedon C., Ghaddhab C., Lefevre N., Bottari S.P. Early transient hypoglycemia is associated with increased albumin nitration in the preterm infant. Neonatology. 2011;100:387–397. PubMed
Kerstjens J.M., Bocca-Tjeertes I.F., de Winter A.F., Reijneveld S.A., Bos A.F. Neonatal morbidities and developmental delay in moderately preterm-born children. Pediatrics. 2012;130:e265–e272. PubMed
Lucas A., Morley R., Cole T.J. Adverse neurodevelopmental outcome of moderate neonatal hypoglycaemia. BMJ. 1988;297:1304–1308. PubMed PMC
Stenninger E., Flink R., Eriksson B., Sahlen C. Long-term neurological dysfunction and neonatal hypoglycaemia after diabetic pregnancy. Arch. Dis. Child Fetal Neonatal Ed. 1998;79:F174–F179. PubMed PMC
Deshpande S., Ward Platt M. The investigation and management of neonatal hypoglycaemia. Semin. Fetal Neonatal Med. 2005;10:351–361. PubMed
McKinlay C.J., Alsweiler J.M., Ansell J.M., Anstice N.S., Chase J.G., Gamble G.D., Harris D.L., Jacobs R.J., Jiang Y., Paudel N., Signal M., Thompson B., Wouldes T.A., Yu T.Y., Harding J.E., Group C.S. Neonatal glycemia and neurodevelopmental outcomes at 2 years. N. Engl. J. Med. 2015;373:1507–1518. PubMed PMC
Groenendaal F., Lammers H., Smit D., Nikkels P.G. Nitrotyrosine in brain tissue of neonates after perinatal asphyxia. Arch. Dis. Child Fetal Neonatal Ed. 2006;91:F429–F433. PubMed PMC
Groenendaal F., Vles J., Lammers H., De Vente J., Smit D., Nikkels P.G. Nitrotyrosine in human neonatal spinal cord after perinatal asphyxia. Neonatology. 2008;93:1–6. PubMed
Iuliano L. Pathways of cholesterol oxidation via non-enzymatic mechanisms. Chem. Phys. Lipids. 2011;164:457–468. PubMed
Griffiths H.R., Moller L., Bartosz G., Bast A., Bertoni-Freddari C., Collins A., Cooke M., Coolen S., Haenen G., Hoberg A.M., Loft S., Lunec J., Olinski R., Parry J., Pompella A., Poulsen H., Verhagen H., Astley S.B. Biomarkers. Mol. Asp. Med. 2002;23:101–208. PubMed
Tsikas D., Rothmann S., Schneider J.Y., Suchy M.T., Trettin A., Modun D., Stuke N., Maassen N., Frolich J.C. Development, validation and biomedical applications of stable-isotope dilution GC-MS and GC-MS/MS techniques for circulating malondialdehyde (MDA) after pentafluorobenzyl bromide derivatization: mda as a biomarker of oxidative stress and its relation to 15(S)−8-iso-prostaglandin F2alpha and nitric oxide (NO) J. Chromatogr. B Anal. Technol. Biomed. Life Sci. 2016;1019:95–111. PubMed
Sobsey C.A., Han J., Lin K., Swardfager W., Levitt A., Borchers C.H. Development and evaluation of a liquid chromatography-mass spectrometry method for rapid, accurate quantitation of malondialdehyde in human plasma. J. Chromatogr. B Anal. Technol. Biomed. Life Sci. 2016;1029–1030:205–212. PubMed
Zelzer S., Mangge H., Oberreither R., Bernecker C., Gruber H.J., Pruller F., Fauler G. Oxidative stress: determination of 4-hydroxy-2-nonenal by gas chromatography/mass spectrometry in human and rat plasma. Free Radic. Res. 2015;49:1233–1238. PubMed
Chafer-Pericas C., Rahkonen L., Sanchez-Illana A., Kuligowski J., Torres-Cuevas I., Cernada M., Cubells E., Nunez-Ramiro A., Andersson S., Vento M., Escobar J. Ultra high performance liquid chromatography coupled to tandem mass spectrometry determination of lipid peroxidation biomarkers in newborn serum samples. Anal. Chim. Acta. 2015;886:214–220. PubMed
Dias I.H., Polidori M.C., Griffiths H.R. Hypercholesterolaemia-induced oxidative stress at the blood-brain barrier. Biochem. Soc. Trans. 2014;42:1001–1005. PubMed
Helmschrodt C., Becker S., Schroter J., Hecht M., Aust G., Thiery J., Ceglarek U. Fast LC-MS/MS analysis of free oxysterols derived from reactive oxygen species in human plasma and carotid plaque. Clin. Chim. Acta. 2013;425:3–8. PubMed
Haller E., Stubiger G., Lafitte D., Lindner W., Lammerhofer M. Chemical recognition of oxidation-specific epitopes in low-density lipoproteins by a nanoparticle based concept for trapping, enrichment, and liquid chromatography-tandem mass spectrometry analysis of oxidative stress biomarkers. Anal. Chem. 2014;86:9954–9961. PubMed
Kasai H., Crain P.F., Kuchino Y., Nishimura S., Ootsuyama A., Tanooka H. Formation of 8-hydroxyguanine moiety in cellular DNA by agents producing oxygen radicals and evidence for its repair. Carcinogenesis. 1986;7:1849–1851. PubMed
Rasmussen S.T., Andersen J.T., Nielsen T.K., Cejvanovic V., Petersen K.M., Henriksen T., Weimann A., Lykkesfeldt J., Poulsen H.E. Simvastatin and oxidative stress in humans: a randomized, double-blinded, placebo-controlled clinical trial. Redox Biol. 2016;9:32–38. PubMed PMC
Al-Salmani K., Abbas H.H., Schulpen S., Karbaschi M., Abdalla I., Bowman K.J., So K.K., Evans M.D., Jones G.D., Godschalk R.W., Cooke M.S. Simplified method for the collection, storage, and comet assay analysis of DNA damage in whole blood. Free Radic. Biol. Med. 2011;51:719–725. PubMed
Karbaschi M., Cooke M.S. Novel method for the high-throughput processing of slides for the comet assay. Sci. Rep. 2014;4:7200. PubMed PMC
Lam P.M., Mistry V., Marczylo T.H., Konje J.C., Evans M.D., Cooke M.S. Rapid measurement of 8-oxo-7,8-dihydro-2'-deoxyguanosine in human biological matrices using ultra-high-performance liquid chromatography-tandem mass spectrometry. Free Radic. Biol. Med. 2012;52:2057–2063. PubMed PMC
Rossner P., Jr., Orhan H., Koppen G., Sakai K., Santella R.M., Ambroz A., Rossnerova A., Sram R.J., Ciganek M., Neca J., Arzuk E., Mutlu N., Cooke M.S. Urinary 8-oxo-7,8-dihydro-2'-deoxyguanosine analysis by an improved ELISA: an inter-laboratory comparison study. Free Radic. Biol. Med. 2016;95:169–179. PubMed
Rossner P., Jr., Mistry V., Singh R., Sram R.J., Cooke M.S. Urinary 8-oxo-7,8-dihydro-2'-deoxyguanosine values determined by a modified ELISA improves agreement with HPLC-MS/MS. Biochem. Biophys. Res. Commun. 2013;440:725–730. PubMed
Cooke M.S., Evans M.D., Dizdaroglu M., Lunec J. Oxidative DNA damage: mechanisms, mutation, and disease. FASEB J. 2003;17:1195–1214. PubMed
Hill A.B. The environment and disease: association or causation? Proc. R. Soc. Med. 1965;58:295–300. PubMed PMC
Loft S., Svoboda P., Kawai K., Kasai H., Sorensen M., Tjonneland A., Vogel U., Moller P., Overvad K., Raaschou-Nielsen O. Association between 8-oxo-7,8-dihydroguanine excretion and risk of lung cancer in a prospective study. Free Radic. Biol. Med. 2012;52:167–172. PubMed
Loft S., Olsen A., Moller P., Poulsen H.E., Tjonneland A. Association between 8-oxo-7,8-dihydro-2'-deoxyguanosine excretion and risk of postmenopausal breast cancer: nested case-control study. Cancer Epidemiol. Biomark. Prev. 2013;22:1289–1296. PubMed
Hromockyj A.E., Maurelli A.T. Identification of an Escherichia coli gene homologous to virR, a regulator of Shigella virulence. J. Bacteriol. 1989;171:2879–2881. PubMed PMC
Broedbaek K., Poulsen H.E., Weimann A., Kom G.D., Schwedhelm E., Nielsen P., Boger R.H. Urinary excretion of biomarkers of oxidatively damaged DNA and RNA in hereditary hemochromatosis. Free Radic. Biol. Med. 2009;47:1230–1233. PubMed
Poulsen H.E., Specht E., Broedbaek K., Henriksen T., Ellervik C., Mandrup-Poulsen T., Tonnesen M., Nielsen P.E., Andersen H.U., Weimann A. RNA modifications by oxidation: a novel disease mechanism? Free Radic. Biol. Med. 2012;52:1353–1361. PubMed
Broedbaek K., Siersma V., Henriksen T., Weimann A., Petersen M., Andersen J.T., Jimenez-Solem E., Hansen L.J., Henriksen J.E., Bonnema S.J., de Fine Olivarius N., Poulsen H.E. Association between urinary markers of nucleic acid oxidation and mortality in type 2 diabetes: a population-based cohort study. Diabetes Care. 2013;36:669–676. PubMed PMC
Poulsen H.E., Nadal L.L., Broedbaek K., Nielsen P.E., Weimann A. Detection and interpretation of 8-oxodG and 8-oxoGua in urine, plasma and cerebrospinal fluid. Biochim. Biophys. Acta. 2014;1840:801–808. PubMed
Kadiiska M.B., Gladen B.C., Baird D.D., Germolec D., Graham L.B., Parker C.E., Nyska A., Wachsman J.T., Ames B.N., Basu S., Brot N., Fitzgerald G.A., Floyd R.A., George M., Heinecke J.W., Hatch G.E., Hensley K., Lawson J.A., Marnett L.J., Morrow J.D., Murray D.M., Plastaras J., Roberts L.J., 2nd, Rokach J., Shigenaga M.K., Sohal R.S., Sun J., Tice R.R., Van Thiel D.H., Wellner D., Walter P.B., Tomer K.B., Mason R.P., Barrett J.C. Biomarkers of oxidative stress study II: are oxidation products of lipids, proteins, and DNA markers of CCl4 poisoning? Free Radic. Biol. Med. 2005;38:698–710. PubMed
Daiber A., Oelze M., Steven S., Kroller-Schon S., Munzel T. Taking up the cudgels for the traditional reactive oxygen and nitrogen species detection assays and their use in the cardiovascular system. Redox Biol. 2017;12:35–49. PubMed PMC
Margaritelis N.V., Cobley J.N., Paschalis V., Veskoukis A.S., Theodorou A.A., Kyparos A., Nikolaidis M.G. Principles for integrating reactive species into in vivo biological processes: examples from exercise physiology. Cell Signal. 2016;28:256–271. PubMed
Margaritelis N.V., Cobley J.N., Paschalis V., Veskoukis A.S., Theodorou A.A., Kyparos A., Nikolaidis M.G. Going retro: oxidative stress biomarkers in modern redox biology. Free Radic. Biol. Med. 2016;98:2–12. PubMed
Dalle-Donne I., Rossi R., Colombo R., Giustarini D., Milzani A. Biomarkers of oxidative damage in human disease. Clin. Chem. 2006;52:601–623. PubMed
Leiper J., Nandi M. The therapeutic potential of targeting endogenous inhibitors of nitric oxide synthesis. Nat. Rev. Drug Discov. 2011;10:277–291. PubMed
Valko M., Leibfritz D., Moncol J., Cronin M.T., Mazur M., Telser J. Free radicals and antioxidants in normal physiological functions and human disease. Int. J. Biochem. Cell Biol. 2007;39:44–84. PubMed
Mengozzi M., Ermilov P., Annenkov A., Ghezzi P., Pearl F. Definition of a family of tissue-protective cytokines using functional cluster analysis: a proof-of-concept study. Front. Immunol. 2014;5:115. PubMed PMC
Watanabe H., Kakihana M., Ohtsuka S., Sugishita Y. Randomized, double-blind, placebo-controlled study of ascorbate on the preventive effect of nitrate tolerance in patients with congestive heart failure. Circulation. 1998;97:886–891. PubMed
Takeshita K., Ozawa T. Recent progress in in vivo ESR spectroscopy. J. Radiol. Res. 2004;45:373–384. PubMed
Yu M., Beyers R.J., Gorden J.D., Cross J.N., Goldsmith C.R. A magnetic resonance imaging contrast agent capable of detecting hydrogen peroxide. Inorg. Chem. 2012;51:9153–9155. PubMed
Perng J.K., Lee S., Kundu K., Caskey C.F., Knight S.F., Satir S., Ferrara K.W., Taylor W.R., Degertekin F.L., Sorescu D., Murthy N. Ultrasound imaging of oxidative stress in vivo with chemically-generated gas microbubbles. Ann. Biomed. Eng. 2012;40:2059–2068. PubMed PMC
Jørgensen J.T., Persson M., Madsen J., Kjær A. High tumor uptake of 64Cu: implications for molecular imaging of tumor characteristics with copper-based PET tracers. Nucl. Med. Biol. 2013;40:345–350. PubMed
Mason R.P. Imaging free radicals in organelles, cells, tissue, and in vivo with immuno-spin trapping. Redox Biol. 2016;8:422–429. PubMed PMC
Maulucci G., Bacic G., Bridal L., Schmidt H.H., Tavitian B., Viel T., Utsumi H., Yalcin A.S., De Spirito M. Imaging reactive oxygen species-induced modifications in living systems. Antioxid. Redox Signal. 2016;24:939–958. PubMed PMC
Frejaville C., Karoui H., Tuccio B., Moigne F.L., Culcasi M., Pietri S., Lauricella R., Tordo P. 5-(Diethoxyphosphoryl)−5-methyl-1-pyrroline N-oxide: a new efficient phosphorylated nitrone for the in vitro and in vivo spin trapping of oxygen-centered radicals. J. Med. Chem. 1995;38:258–265. PubMed
Villamena F.A., Xia S., Merle J.K., Lauricella R., Tuccio B., Hadad C.M., Zweier J.L. Reactivity of superoxide radical anion with cyclic nitrones: role of intramolecular h-bond and electrostatic effects. J. Am. Chem. Soc. 2007;129:8177–8191. PubMed PMC
K. Abbas, N. Babić, F. Peyrot, Use of spin traps to detect superoxide production in living cells by electron paramagnetic resonance (EPR) spectroscopy. Methods,109, 2016, 31–43. PubMed
Beziere N., Decroos C., Mkhitaryan K., Kish E., Richard F., Bigot-Marchand S., Durand S., Cloppet F., Chauvet C., Corvol M.-T., Rannou F., Xu-Li Y., Mansuy D., Peyrot F., Frapart Y.-M. First combined in vivo X-ray tomography and high-resolution molecular electron paramagnetic resonance (EPR) imaging of the mouse knee joint taking into account the disappearance kinetics of the EPR probe. Mol. Imaging. 2012;11:220–228. PubMed
Bézière N., Hardy M., Poulhès F., Karoui H., Tordo P., Ouari O., Frapart Y.-M., Rockenbauer A., Boucher J.-L., Mansuy D., Peyrot F. Metabolic stability of superoxide adducts derived from newly developed cyclic nitrone spin traps. Free Radic. Biol. Med. 2014;67:150–158. PubMed
Leinisch F., Jiang J., DeRose E.F., Khramtsov V.V., Mason R.P. Investigation of spin-trapping artifacts formed by the Forrester-Hepburn mechanism. Free Radic. Biol. Med. 2013;65:1497–1505. PubMed PMC
Pou S., Cohen M.S., Britigan B.E., Rosen G.M. Spin-trapping and human neutrophils. Limits of detection of hydroxyl radical. J. Biol. Chem. 1989;264:12299–12302. PubMed
Abbas K., Hardy M., Poulhès F., Karoui H., Tordo P., Ouari O., Peyrot F. Detection of superoxide production in stimulated and unstimulated living cells using new cyclic nitrone spin traps. Free Radic. Biol. Med. 2014;71:281–290. PubMed
Kleschyov A.L., Munzel T. Advanced spin trapping of vascular nitric oxide using colloid iron diethyldithiocarbamate. Methods Enzymol. 2002;359:42–51. PubMed
Steven S., Hausding M., Kroller-Schon S., Mader M., Mikhed Y., Stamm P., Zinssius E., Pfeffer A., Welschof P., Agdauletova S., Sudowe S., Li H., Oelze M., Schulz E., Klein T., Munzel T., Daiber A. Gliptin and GLP-1 analog treatment improves survival and vascular inflammation/dysfunction in animals with lipopolysaccharide-induced endotoxemia. Basic Res. Cardiol. 2015;110:6. PubMed
Steven S., Jurk K., Kopp M., Kroller-Schon S., Mikhed Y., Schwierczek K., Roohani S., Kashani F., Oelze M., Klein T., Tokalov S., Danckwardt S., Strand S., Wenzel P., Munzel T., Daiber A. Glucagon-like peptide-1 receptor signalling reduces microvascular thrombosis, nitro-oxidative stress and platelet activation in endotoxaemic mice. Br. J. Pharmacol. 2016 PubMed PMC
Deng S., Kruger A., Kleschyov A.L., Kalinowski L., Daiber A., Wojnowski L. Gp91phox-containing NAD(P)H oxidase increases superoxide formation by doxorubicin and NADPH. Free Radic. Biol. Med. 2007;42:466–473. PubMed
Kuppusamy P., Li H., Ilangovan G., Cardounel A.J., Zweier J.L., Yamada K., Krishna M.C., Mitchell J.B. Noninvasive imaging of tumor redox status and its modification by tissue glutathione levels. Cancer Res. 2002;62:307–312. PubMed
Berliner L.J. From spin-labeled proteins to in vivo EPR applications. Eur. Biophys. J. 2010;39:579–588. PubMed
Klare J.P. Site-directed spin labeling EPR spectroscopy in protein research. Biol. Chem. 2013;394 PubMed
Klug C.S., Feix J.B. Methods and applications of site-directed spin labeling EPR spectroscopy. Methods Cell Biol. 2008:617–658. PubMed
Gurachevsky A., Kazmierczak S.C., Jörres A., Muravsky V. Application of spin label electron paramagnetic resonance in the diagnosis and prognosis of cancer and sepsis. Clin. Chem. Lab. Med. 2008;46 PubMed
Muravskaya E.V., Lapko A.G., Muravskii V.A. Modification of transport function of plasma albumin during atherosclerosis and diabetes mellitus. Bull. Exp. Biol. Med. 2003;135:433–435. PubMed
Jalan R., Schnurr K., Mookerjee R.P., Sen S., Cheshire L., Hodges S., Muravsky V., Williams R., Matthes G., Davies N.A. Alterations in the functional capacity of albumin in patients with decompensated cirrhosis is associated with increased mortality. Hepatology. 2009;50:555–564. PubMed
Roy D., Quiles J., Gaze D.C., Collinson P., Kaski J.C., Baxter G.F. Role of reactive oxygen species on the formation of the novel diagnostic marker ischaemia modified albumin. Heart. 2006;92:113–114. PubMed PMC
Pavićević A.A., Popović-Bijelić A.D., Mojović M.D., Šušnjar S.V., Bačić G.G. Binding of doxyl stearic spin labels to human serum albumin: an EPR study. J. Phys. Chem. B. 2014;118:10898–10905. PubMed
Junk M.J.N., Spiess H.W., Hinderberger D. The distribution of fatty acids reveals the functional structure of human serum albumin. Angew. Chem. Int. Ed. 2010;49:8755–8759. PubMed
Boutier-Pischon A., Auger F., Noël J.-M., Almario A., Frapart Y.-M. EPR and electrochemical quantification of oxygen using newly synthesized para-silylated triarylmethyl radicals. Free Radic. Res. 2015:1–8. PubMed
Li J., Liu Y., Kim E., March J.C., Bentley W.E., Payne G.F. Electrochemical reverse engineering: a systems-level tool to probe the redox-based molecular communication of biology. Free Radic. Biol. Med. 2017;105:110–131. PubMed
Lund A., Shiotani M., Shimada S. Springer Science & Business Media; 2011. Principles and Applications of ESR Spectroscopy.
Quideau S., Deffieux D., Douat-Casassus C., Pouységu L. Plant polyphenols: chemical properties, biological activities, and synthesis. Angew. Chem. Int. Ed. 2011;50:586–621. PubMed
Pyszková M., Biler M., Biedermann D., Valentová K., Kuzma M., Vrba J., Ulrichová J., Sokolová R., Mojović M., Popović-Bijelić A., Kubala M., Trouillas P., Křen V., Vacek J. Flavonolignan 2,3-dehydroderivatives: preparation, antiradical and cytoprotective activity. Free Radic. Biol. Med. 2016;90:114–125. PubMed
Vacek J., Zatloukalová M., Desmier T., Nezhodová V., Hrbáč J., Kubala M., Křen V., Ulrichová J., Trouillas P. Antioxidant, metal-binding and DNA-damaging properties of flavonolignans: a joint experimental and computational highlight based on 7-O-galloylsilybin. Chem.-Biol. Interact. 2013;205:173–180. PubMed
Dimitrić Marković J.M., Marković Z.S., Pašti I.A., Brdarić T.P., Popović-Bijelić A., Mojović M. A joint application of spectroscopic, electrochemical and theoretical approaches in evaluation of the radical scavenging activity of 3-OH flavones and their iron complexes towards different radical species. Dalton Trans. 2012;41:7295. PubMed
Sokolová R., Tarábek J., Papoušková B., Kocábová J., Fiedler J., Vacek J., Marhol P., Vavříková E., Křen V. Oxidation of the flavonolignan silybin. In situ EPR evidence of the spin-trapped silybin radical. Electrochim. Acta. 2016;205:118–123.
Naso L.G., Ferrer E.G., Butenko N., Cavaco I., Lezama L., Rojo T., Etcheverry S.B., Williams P.A.M. Antioxidant, DNA cleavage, and cellular effects of silibinin and a new oxovanadium(IV)/silibinin complex. JBIC J. Biol. Inorg. Chem. 2011;16:653–668. PubMed
Kalamkarov G.P., Bugrova A.E., Konstantinova T.S., Shevchenko T.F. [Endogenous content of the nitric oxide in the cell layers of the eye retina] Ross. Fiziol. Zhurnal Im. I. M. Sechenova/Ross. Akad. Nauk. 2014;100:852–860. PubMed
Lukyanov K.A., Belousov V.V. Genetically encoded fluorescent redox sensors. Biochim. Et. Biophys. Acta (BBA) – General. Subj. 2014;1840:745–756. PubMed
Ermakova Y.G., Bilan D.S., Matlashov M.E., Mishina N.M., Markvicheva K.N., Subach O.M., Subach F.V., Bogeski I., Hoth M., Enikolopov G., Belousov V.V. Red fluorescent genetically encoded indicator for intracellular hydrogen peroxide. Nat. Commun. 2014;5 PubMed PMC
Morgan B., Van Laer K., Owusu T.N.E., Ezerina D., Pastor-Flores D., Amponsah P.S., Tursch A., Dick T.P. Real-time monitoring of basal H2O2 levels with peroxiredoxin-based probes. Nat. Chem. Biol. 2016;12:437–443. PubMed
Belousov V.V., Fradkov A.F., Lukyanov K.A., Staroverov D.B., Shakhbazov K.S., Terskikh A.V., Lukyanov S. Genetically encoded fluorescent indicator for intracellular hydrogen peroxide. Nat. Methods. 2006;3:281–286. PubMed
Gutscher M., Sobotta M.C., Wabnitz G.H., Ballikaya S., Meyer A.J., Samstag Y., Dick T.P. Proximity-based protein thiol oxidation by H2O2-scavenging peroxidases. J. Biol. Chem. 2009;284:31532–31540. PubMed PMC
Mishina N.M., Tyurin-Kuzmin P.A., Markvicheva K.N., Vorotnikov A.V., Tkachuk V.A., Laketa V., Schultz C., Lukyanov S., Belousov V.V. Does cellular hydrogen peroxide diffuse or act locally? Antioxid. Redox Signal. 2010;14:1–7. PubMed
Pak Y., Swamy K., Yoon J. Recent progress in fluorescent imaging probes. Sensors. 2015;15:24374–24396. PubMed PMC
Guo Z., Park S., Yoon J., Shin I. Recent progress in the development of near-infrared fluorescent probes for bioimaging applications. Chem. Soc. Rev. 2013;43:16–29. PubMed
Lee D., Khaja S., Velasquez-Castano J.C., Dasari M., Sun C., Petros J., Taylor W.R., Murthy N. In vivo imaging of hydrogen peroxide with chemiluminescent nanoparticles. Nat. Mater. 2007;6:765–769. PubMed
Santra S., Xu J., Wang K., Tand W. Luminescent nanoparticle probes for bioimaging. J. Nanosci. Nanotechnol. 2004;4:590–599. PubMed
Uusitalo L.M., Hempel N. Recent advances in intracellular and in vivo ROS Sensing: focus on nanoparticle and nanotube applications. Int. J. Mol. Sci. 2012;13:10660–10679. PubMed PMC
Choi W.-G., Swanson S.J., Gilroy S. High-resolution imaging of Ca2+, redox status, ROS and pH using GFP biosensors: imaging of Ca2+, redox, ROS and pH using GFP biosensors. Plant J. 2012;70:118–128. PubMed
Chen Z., Liu Z., Li Z., Ju E., Gao N., Zhou L., Ren J., Qu X. Upconversion nanoprobes for efficiently in vitro imaging reactive oxygen species and in vivo diagnosing rheumatoid arthritis. Biomaterials. 2015;39:15–22. PubMed
Zielonka J., Lambeth J.D., Kalyanaraman B. On the use of L-012, a luminol-based chemiluminescent probe, for detecting superoxide and identifying inhibitors of NADPH oxidase: a reevaluation. Free Radic. Biol. Med. 2013;65:1310–1314. PubMed PMC
Seredenina T., Chiriano G., Filippova A., Nayernia Z., Mahiout Z., Fioraso-Cartier L., Plastre O., Scapozza L., Krause K.-H., Jaquet V. A subset of N-substituted phenothiazines inhibits NADPH oxidases. Free Radic. Biol. Med. 2015;86:239–249. PubMed
Zielonka J., Cheng G., Zielonka M., Ganesh T., Sun A., Joseph J., Michalski R., O'Brien W.J., Lambeth J.D., Kalyanaraman B. High-throughput assays for superoxide and hydrogen peroxide design of a screening workflow to identify inhibitors of NADPH oxidases. J. Biol. Chem. 2014;289:16176–16189. PubMed PMC
Zielonka J., Zielonka M., VerPlank L., Cheng G., Hardy M., Ouari O., Ayhan M.M., Podsiadły R., Sikora A., Lambeth J.D., Kalyanaraman B. Mitigation of NADPH oxidase 2 activity as a strategy to inhibit peroxynitrite formation. J. Biol. Chem. 2016;291:7029–7044. PubMed PMC
Michalski R., Zielonka J., Hardy M., Joseph J., Kalyanaraman B. Hydropropidine: a novel, cell-impermeant fluorogenic probe for detecting extracellular superoxide. Free Radic. Biol. Med. 2013;54:135–147. PubMed PMC
Waszczak C., Akter S., Jacques S., Huang J., Messens J., Breusegem F.V. Oxidative post-translational modifications of cysteine residues in plant signal transduction. J. Exp. Bot. 2015;66:2923–2934. PubMed
Cao J., Ying M., Xie N., Lin G., Dong R., Zhang J., Yan H., Yang X., He Q., Yang B. The oxidation states of DJ-1 dictate the cell fate in response to oxidative stress triggered by 4-HPR: autophagy or apoptosis? Antioxid. Redox Signal. 2014;21:1443–1459. PubMed PMC
Waszczak C., Akter S., Eeckhout D., Persiau G., Wahni K., Bodra N., Molle I.V., Smet B.D., Vertommen D., Gevaert K., Jaeger G.D., Montagu M.V., Messens J., Breusegem F.V. Sulfenome mining in arabidopsis thaliana. Proc. Natl. Acad. Sci. USA. 2014;111:11545–11550. PubMed PMC
Akter S., Huang J., Bodra N., Smet B.D., Wahni K., Rombaut D., Pauwels J., Gevaert K., Carroll K., Breusegem F.V., Messens J. DYn-2 based identification of arabidopsis sulfenomes. Mol. Cell. Proteom. 2015;14:1183–1200. PubMed PMC
Oger E., Marino D., Guigonis J.-M., Pauly N., Puppo A. Sulfenylated proteins in the medicago truncatula–sinorhizobium meliloti symbiosis. J. Proteom. 2012;75:4102–4113. PubMed
Benitez L.V., Allison W.S. The inactivation of the acyl phosphatase activity catalyzed by the sulfenic acid form of glyceraldehyde 3-phosphate dehydrogenase by dimedone and olefins. J. Biol. Chem. 1974;249:6234–6243. PubMed
Seo Y.H., Carroll K.S. Facile synthesis and biological evaluation of a cell-permeable probe to detect redox-regulated proteins. Bioorg. Med. Chem. Lett. 2009;19:356–359. PubMed
Schroder K., Vecchione C., Jung O., Schreiber J.G., Shiri-Sverdlov R., van Gorp P.J., Busse R., Brandes R.P. Xanthine oxidase inhibitor tungsten prevents the development of atherosclerosis in ApoE knockout mice fed a Western-type diet. Free Radic. Biol. Med. 2006;41:1353–1360. PubMed
Schroder K., Zhang M., Benkhoff S., Mieth A., Pliquett R., Kosowski J., Kruse C., Luedike P., Michaelis U.R., Weissmann N., Dimmeler S., Shah A.M., Brandes R.P. Nox4 is a protective reactive oxygen species generating vascular NADPH oxidase. Circ. Res. 2012;110:1217–1225. PubMed
Schurmann C., Rezende F., Kruse C., Yasar Y., Lowe O., Fork C., van de Sluis B., Bremer R., Weissmann N., Shah A.M., Jo H., Brandes R.P., Schroder K. The NADPH oxidase Nox4 has anti-atherosclerotic functions. Eur. Heart J. 2015;36:3447–3456. PubMed PMC
Langbein H., Brunssen C., Hofmann A., Cimalla P., Brux M., Bornstein S.R., Deussen A., Koch E., Morawietz H. NADPH oxidase 4 protects against development of endothelial dysfunction and atherosclerosis in LDL receptor deficient mice. Eur. Heart J. 2016;37:1753–1761. PubMed PMC
Craige S.M., Kant S., Reif M., Chen K., Pei Y., Angoff R., Sugamura K., Fitzgibbons T., Keaney J.F., Jr. Endothelial NADPH oxidase 4 protects ApoE-/- mice from atherosclerotic lesions. Free Radic. Biol. Med. 2015;89:1–7. PubMed PMC
Gray S.P., Di Marco E., Kennedy K., Chew P., Okabe J., El-Osta A., Calkin A.C., Biessen E.A., Touyz R.M., Cooper M.E., Schmidt H.H., Jandeleit-Dahm K.A. Reactive oxygen Species can provide atheroprotection via NOX4-dependent inhibition of inflammation and vascular remodeling. Arterioscler. Thromb. Vasc. Biol. 2016;36:295–307. PubMed
Wang Y., Yang J., Yi J. Redox sensing by proteins: oxidative modifications on cysteines and the consequent events. Antioxid. Redox Signal. 2012;16:649–657. PubMed
Klatt P., Lamas S. Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress. Eur. J. Biochem. 2000;267:4928–4944. PubMed
Mieyal J.J., Gallogly M.M., Qanungo S., Sabens E.A., Shelton M.D. Molecular mechanisms and clinical implications of reversible protein S-glutathionylation. Antioxid. Redox Signal. 2008;10:1941–1988. PubMed PMC
Watanabe Y., Murdoch C.E., Sano S., Ido Y., Bachschmid M.M., Cohen R.A., Matsui R. Glutathione adducts induced by ischemia and deletion of glutaredoxin-1 stabilize HIF-1alpha and improve limb revascularization. Proc. Natl. Acad. Sci. USA. 2016;113:6011–6016. PubMed PMC
O.G. Miller, J.B. Behring, S.L. Siedlak, S. Jiang, R. Matsui, M.M. Bachschmid, X. Zhu, J.J. Mieyal, Upregulation of glutaredoxin-1 activates microglia and promotes neurodegeneration: implications for parkinson’s disease. Antioxid. Redox Signal., 25, 2016, 967–982. PubMed PMC
Murdoch C.E., Shuler M., Haeussler D.J., Kikuchi R., Bearelly P., Han J., Watanabe Y., Fuster J.J., Walsh K., Ho Y.S., Bachschmid M.M., Cohen R.A., Matsui R. Glutaredoxin-1 up-regulation induces soluble vascular endothelial growth factor receptor 1, attenuating post-ischemia limb revascularization. J. Biol. Chem. 2014;289:8633–8644. PubMed PMC
Evangelista A.M., Thompson M.D., Weisbrod R.M., Pimental D.R., Tong X., Bolotina V.M., Cohen R.A. Redox regulation of SERCA2 is required for vascular endothelial growth factor-induced signaling and endothelial cell migration. Antioxid. Redox Signal. 2012;17:1099–1108. PubMed PMC
Hazarika S., Dokun A.O., Li Y., Popel A.S., Kontos C.D., Annex B.H. Impaired angiogenesis after hindlimb ischemia in type 2 diabetes mellitus: differential regulation of vascular endothelial growth factor receptor 1 and soluble vascular endothelial growth factor receptor 1. Circ. Res. 2007;101:948–956. PubMed
Okuda M., Inoue N., Azumi H., Seno T., Sumi Y., Hirata K., Kawashima S., Hayashi Y., Itoh H., Yodoi J., Yokoyama M. Expression of glutaredoxin in human coronary arteries: its potential role in antioxidant protection against atherosclerosis. Arterioscler. Thromb. Vasc. Biol. 2001;21:1483–1487. PubMed
Li F., Sonveaux P., Rabbani Z.N., Liu S., Yan B., Huang Q., Vujaskovic Z., Dewhirst M.W., Li C.Y. Regulation of HIF-1alpha stability through S-nitrosylation. Mol. Cell. 2007;26:63–74. PubMed PMC
Pagliaro P., Moro F., Tullio F., Perrelli M.G., Penna C. Cardioprotective pathways during reperfusion: focus on redox signaling and other modalities of cell signaling. Antioxid. Redox Signal. 2011;14:833–850. PubMed
Kalogeris T., Bao Y., Korthuis R.J. Mitochondrial reactive oxygen species: a double edged sword in ischemia/reperfusion vs preconditioning. Redox Biol. 2014;2:702–714. PubMed PMC
Yellon D.M., Hausenloy D.J. Myocardial reperfusion injury. N. Engl. J. Med. 2007;357:1121–1135. PubMed
D.J. Hausenloy, D. Garcia-Dorado, H. Erik Botker, S.M. Davidson, J. Downey, F.B. Engel, R. Jennings, S. Lecour, J. Leor, R. Madonna, M. Ovize, C. Perrino, F. Prunier, R. Schulz, J.P. Sluijter, L.W. Van Laake, J. Vinten-Johansen, D.M. Yellon, K. Ytrehus, G. Heusch, P. Ferdinandy, Novel targets and future strategies for acute cardioprotection: position paper of the european society of cardiology working group on cellular biology of the heart. Cardiovasc. Res., 113, 2017, 564-585. PubMed
Heusch G. Molecular basis of cardioprotection: signal transduction in ischemic pre-, post-, and remote conditioning. Circ. Res. 2015;116:674–699. PubMed
Andreadou I., Iliodromitis E.K., Farmakis D., Kremastinos D.T. To prevent, protect and save the ischemic heart: antioxidants revisited. Expert Opin. Ther. Targets. 2009;13:945–956. PubMed
Tsovolas K., Iliodromitis E.K., Andreadou I., Zoga A., Demopoulou M., Iliodromitis K.E., Manolaki T., Markantonis S.L., Kremastinos D.T. Acute administration of vitamin C abrogates protection from ischemic preconditioning in rabbits. Pharmacol. Res. 2008;57:283–289. PubMed
Skyschally A., Schulz R., Gres P., Korth H.G., Heusch G. Attenuation of ischemic preconditioning in pigs by scavenging of free oxyradicals with ascorbic acid. Am. J. Physiol. Heart Circ. Physiol. 2003;284:H698–H703. PubMed
Local Food-Nutraceuticals C. Understanding local Mediterranean diets: a multidisciplinary pharmacological and ethnobotanical approach. Pharmacol. Res. 2005;52:353–366. PubMed
Turan B., Fliss H., Desilets M. Oxidants increase intracellular free Zn2+ concentration in rabbit ventricular myocytes. Am. J. Physiol. 1997;272:H2095–H2106. PubMed
Tuncay E., Bilginoglu A., Sozmen N.N., Zeydanli E.N., Ugur M., Vassort G., Turan B. Intracellular free zinc during cardiac excitation-contraction cycle: calcium and redox dependencies. Cardiovasc Res. 2011;89:634–642. PubMed
Pisarenko O., Studneva I., Khlopkov V., Solomatina E., Ruuge E. An assessment of anaerobic metabolism during ischemia and reperfusion in isolated guinea pig heart. Biochim. Biophys. Acta. 1988;934:55–63. PubMed
Ashrafian H., Czibik G., Bellahcene M., Aksentijevic D., Smith A.C., Mitchell S.J., Dodd M.S., Kirwan J., Byrne J.J., Ludwig C., Isackson H., Yavari A., Stottrup N.B., Contractor H., Cahill T.J., Sahgal N., Ball D.R., Birkler R.I., Hargreaves I., Tennant D.A., Land J., Lygate C.A., Johannsen M., Kharbanda R.K., Neubauer S., Redwood C., de Cabo R., Ahmet I., Talan M., Gunther U.L., Robinson A.J., Viant M.R., Pollard P.J., Tyler D.J., Watkins H. Fumarate is cardioprotective via activation of the Nrf2 antioxidant pathway. Cell Metab. 2012;15:361–371. PubMed PMC
Chouchani E.T., Pell V.R., James A.M., Work L.M., Saeb-Parsy K., Frezza C., Krieg T., Murphy M.P. A unifying mechanism for mitochondrial superoxide production during ischemia-reperfusion injury. Cell Metab. 2016;23:254–263. PubMed
Valls-Lacalle L., Barba I., Miro-Casas E., Alburquerque-Bejar J.J., Ruiz-Meana M., Fuertes-Agudo M., Rodriguez-Sinovas A., Garcia-Dorado D. Succinate dehydrogenase inhibition with malonate during reperfusion reduces infarct size by preventing mitochondrial permeability transition. Cardiovasc. Res. 2016;109:374–384. PubMed
Gorenkova N., Robinson E., Grieve D.J., Galkin A. Conformational change of mitochondrial complex I increases ROS sensitivity during ischemia. Antioxid. Redox Signal. 2013;19:1459–1468. PubMed PMC
Chouchani E.T., Methner C., Nadtochiy S.M., Logan A., Pell V.R., Ding S., James A.M., Cocheme H.M., Reinhold J., Lilley K.S., Partridge L., Fearnley I.M., Robinson A.J., Hartley R.C., Smith R.A., Krieg T., Brookes P.S., Murphy M.P. Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I. Nat. Med. 2013;19:753–759. PubMed PMC
Varga Z.V., Giricz Z., Liaudet L., Hasko G., Ferdinandy P., Pacher P. Interplay of oxidative, nitrosative/nitrative stress, inflammation, cell death and autophagy in diabetic cardiomyopathy. Biochim. Biophys. Acta. 2015;1852:232–242. PubMed PMC
Pechanova O., Varga Z.V., Cebova M., Giricz Z., Pacher P., Ferdinandy P. Cardiac NO signalling in the metabolic syndrome. Br. J. Pharmacol. 2015;172:1415–1433. PubMed PMC
Frustaci A., Kajstura J., Chimenti C., Jakoniuk I., Leri A., Maseri A., Nadal-Ginard B., Anversa P. Myocardial cell death in human diabetes. Circ. Res. 2000;87:1123–1132. PubMed
Onody A., Csonka C., Giricz Z., Ferdinandy P. Hyperlipidemia induced by a cholesterol-rich diet leads to enhanced peroxynitrite formation in rat hearts. Cardiovasc. Res. 2003;58:663–670. PubMed
Varga Z.V., Kupai K., Szucs G., Gaspar R., Paloczi J., Farago N., Zvara A., Puskas L.G., Razga Z., Tiszlavicz L., Bencsik P., Gorbe A., Csonka C., Ferdinandy P., Csont T. MicroRNA-25-dependent up-regulation of NADPH oxidase 4 (NOX4) mediates hypercholesterolemia-induced oxidative/nitrative stress and subsequent dysfunction in the heart. J. Mol. Cell Cardiol. 2013;62:111–121. PubMed
Gorbe A., Varga Z.V., Kupai K., Bencsik P., Kocsis G.F., Csont T., Boengler K., Schulz R., Ferdinandy P. Cholesterol diet leads to attenuation of ischemic preconditioning-induced cardiac protection: the role of connexin 43. Am. J. Physiol. Heart Circ. Physiol. 2011;300:H1907–H1913. PubMed
Jeong E.M., Chung J., Liu H., Go Y., Gladstein S., Farzaneh-Far A., Lewandowski E.D., Dudley S.C., Jr. Role of mitochondrial oxidative stress in glucose tolerance, insulin resistance, and cardiac diastolic dysfunction. J. Am. Heart Assoc. 2016;5 PubMed PMC
Sverdlov A.L., Elezaby A., Qin F., Behring J.B., Luptak I., Calamaras T.D., Siwik D.A., Miller E.J., Liesa M., Shirihai O.S., Pimentel D.R., Cohen R.A., Bachschmid M.M., Colucci W.S. Mitochondrial reactive oxygen species mediate cardiac structural, functional, and mitochondrial consequences of diet-induced metabolic heart disease. J. Am. Heart Assoc. 2016;5 PubMed PMC
Luo M., Guan X., Luczak E.D., Lang D., Kutschke W., Gao Z., Yang J., Glynn P., Sossalla S., Swaminathan P.D., Weiss R.M., Yang B., Rokita A.G., Maier L.S., Efimov I.R., Hund T.J., Anderson M.E. Diabetes increases mortality after myocardial infarction by oxidizing CaMKII. J. Clin. Investig. 2013;123:1262–1274. PubMed PMC
Ni R., Cao T., Xiong S., Ma J., Fan G.C., Lacefield J.C., Lu Y., Le Tissier S., Peng T. Therapeutic inhibition of mitochondrial reactive oxygen species with mito-TEMPO reduces diabetic cardiomyopathy. Free Radic. Biol. Med. 2016;90:12–23. PubMed PMC
Sloan R.C., Moukdar F., Frasier C.R., Patel H.D., Bostian P.A., Lust R.M., Brown D.A. Mitochondrial permeability transition in the diabetic heart: contributions of thiol redox state and mitochondrial calcium to augmented reperfusion injury. J. Mol. Cell Cardiol. 2012;52:1009–1018. PubMed
Guo Y., Yu W., Sun D., Wang J., Li C., Zhang R., Babcock S.A., Li Y., Liu M., Ma M., Shen M., Zeng C., Li N., He W., Zou Q., Zhang Y., Wang H. A novel protective mechanism for mitochondrial aldehyde dehydrogenase (ALDH2) in type i diabetes-induced cardiac dysfunction: role of AMPK-regulated autophagy. Biochim. Biophys. Acta. 2015;1852:319–331. PubMed
Herlein J.A., Fink B.D., Sivitz W.I. Superoxide production by mitochondria of insulin-sensitive tissues: mechanistic differences and effect of early diabetes. Metabolism. 2010;59:247–257. PubMed PMC
Essop M.F., Anna Chan W.Y., Valle A., Garcia-Palmer F.J., Du Toit E.F. Impaired contractile function and mitochondrial respiratory capacity in response to oxygen deprivation in a rat model of pre-diabetes. Acta Physiol. 2009;197:289–296. PubMed
Radermacher K.A., Wingler K., Langhauser F., Altenhofer S., Kleikers P., Hermans J.J., Hrabe de Angelis M., Kleinschnitz C., Schmidt H.H. Neuroprotection after stroke by targeting NOX4 as a source of oxidative stress. Antioxid. Redox Signal. 2013;18:1418–1427. PubMed PMC
Kleikers P.W., Hooijmans C., Gob E., Langhauser F., Rewell S.S., Radermacher K., Ritskes-Hoitinga M., Howells D.W., Kleinschnitz C., Schmidt H.H. A combined pre-clinical meta-analysis and randomized confirmatory trial approach to improve data validity for therapeutic target validation. Sci. Rep. 2015;5:13428. PubMed PMC
Dao V.T., Casas A.I., Maghzal G.J., Seredenina T., Kaludercic N., Robledinos-Anton N., Di Lisa F., Stocker R., Ghezzi P., Jaquet V., Cuadrado A., Schmidt H.H. Pharmacology and clinical drug candidates in redox medicine. Antioxid. Redox Signal. 2015;23:1113–1129. PubMed PMC
C. Kleinschnitz, S. Mencl, P.W. Kleikers, M.K. Schuhmann, G.L. M, A.I. Casas, B. Surun, A. Reif, H.H. Schmidt, NOS knockout or inhibition but not disrupting PSD-95-NOS interaction protect against ischemic brain damage. J. Cereb. Blood Flow Metab., 36, 2016, 1508–12. PubMed PMC
Li H., Horke S., Forstermann U. Oxidative stress in vascular disease and its pharmacological prevention. Trends Pharmacol. Sci. 2013;34:313–319. PubMed
Munzel T., Daiber A., Ullrich V., Mulsch A. Vascular consequences of endothelial nitric oxide synthase uncoupling for the activity and expression of the soluble guanylyl cyclase and the cGMP-dependent protein kinase. Arterioscler. Thromb. Vasc. Biol. 2005;25:1551–1557. PubMed
Li H., Horke S., Forstermann U. Vascular oxidative stress, nitric oxide and atherosclerosis. Atherosclerosis. 2014;237:208–219. PubMed
Li H., Forstermann U. Prevention of atherosclerosis by interference with the vascular nitric oxide system. Curr. Pharm. Des. 2009;15:3133–3145. PubMed
Crabtree M.J., Brixey R., Batchelor H., Hale A.B., Channon K.M. Integrated redox sensor and effector functions for tetrahydrobiopterin- and glutathionylation-dependent endothelial nitric-oxide synthase uncoupling. J. Biol. Chem. 2013;288:561–569. PubMed PMC
Li H., Forstermann U. Uncoupling of endothelial NO synthase in atherosclerosis and vascular disease. Curr. Opin. Pharmacol. 2013;13:161–167. PubMed
Li H., Forstermann U. Pharmacological prevention of eNOS uncoupling. Curr. Pharm. Des. 2014;20:3595–3606. PubMed
Schuhmacher S., Oelze M., Bollmann F., Kleinert H., Otto C., Heeren T., Steven S., Hausding M., Knorr M., Pautz A., Reifenberg K., Schulz E., Gori T., Wenzel P., Munzel T., Daiber A. Vascular dysfunction in experimental diabetes is improved by pentaerithrityl tetranitrate but not isosorbide-5-mononitrate therapy. Diabetes. 2011;60:2608–2616. PubMed PMC
Knorr M., Hausding M., Kroller-Schuhmacher S., Steven S., Oelze M., Heeren T., Scholz A., Gori T., Wenzel P., Schulz E., Daiber A., Munzel T. Nitroglycerin-induced endothelial dysfunction and tolerance involve adverse phosphorylation and S-Glutathionylation of endothelial nitric oxide synthase: beneficial effects of therapy with the AT1 receptor blocker telmisartan. Arterioscler. Thromb. Vasc. Biol. 2011;31:2223–2231. PubMed
Kim J.H., Bugaj L.J., Oh Y.J., Bivalacqua T.J., Ryoo S., Soucy K.G., Santhanam L., Webb A., Camara A., Sikka G., Nyhan D., Shoukas A.A., Ilies M., Christianson D.W., Champion H.C., Berkowitz D.E. Arginase inhibition restores NOS coupling and reverses endothelial dysfunction and vascular stiffness in old rats. J. Appl. Physiol. (1985) 2009;107:1249–1257. PubMed PMC
Xia N., Horke S., Habermeier A., Closs E.I., Reifenberg G., Gericke A., Mikhed Y., Munzel T., Daiber A., Forstermann U., Li H. Uncoupling of endothelial nitric oxide synthase in perivascular adipose tissue of diet-induced obese mice. Arterioscler. Thromb. Vasc. Biol. 2016;36:78–85. PubMed
Bowler R.P., Arcaroli J., Crapo J.D., Ross A., Slot J.W., Abraham E. Extracellular superoxide dismutase attenuates lung injury after hemorrhage. Am. J. Respir. Crit. Care Med. 2001;164:290–294. PubMed
Atochina E.N., Balyasnikova I.V., Danilov S.M., Granger D.N., Fisher A.B., Muzykantov V.R. Immunotargeting of catalase to ACE or ICAM-1 protects perfused rat lungs against oxidative stress. Am. J. Physiol. 1998;275:L806–L817. PubMed
Dziubla T.D., Shuvaev V.V., Hong N.K., Hawkins B.J., Madesh M., Takano H., Simone E., Nakada M.T., Fisher A., Albelda S.M., Muzykantov V.R. Endothelial targeting of semi-permeable polymer nanocarriers for enzyme therapies. Biomaterials. 2008;29:215–227. PubMed PMC
Sweitzer T.D., Thomas A.P., Wiewrodt R., Nakada M.T., Branco F., Muzykantov V.R. PECAM-directed immunotargeting of catalase: specific, rapid and transient protection against hydrogen peroxide. Free Radic. Biol. Med. 2003;34:1035–1046. PubMed
Shuvaev V.V., Tliba S., Pick J., Arguiri E., Christofidou-Solomidou M., Albelda S.M., Muzykantov V.R. Modulation of endothelial targeting by size of antibody-antioxidant enzyme conjugates. J. Control Release. 2011;149:236–241. PubMed PMC
Kozower B.D., Christofidou-Solomidou M., Sweitzer T.D., Muro S., Buerk D.G., Solomides C.C., Albelda S.M., Patterson G.A., Muzykantov V.R. Immunotargeting of catalase to the pulmonary endothelium alleviates oxidative stress and reduces acute lung transplantation injury. Nat. Biotechnol. 2003;21:392–398. PubMed
Shuvaev V.V., Christofidou-Solomidou M., Bhora F., Laude K., Cai H., Dikalov S., Arguiri E., Solomides C.C., Albelda S.M., Harrison D.G., Muzykantov V.R. Targeted detoxification of selected reactive oxygen species in the vascular endothelium. J. Pharmacol. Exp. Ther. 2009;331:404–411. PubMed PMC
Hood E.D., Greineder C.F., Dodia C., Han J., Mesaros C., Shuvaev V.V., Blair I.A., Fisher A.B., Muzykantov V.R. Antioxidant protection by PECAM-targeted delivery of a novel NADPH-oxidase inhibitor to the endothelium in vitro and in vivo. J. Control Release. 2012;163:161–169. PubMed PMC
Howard M.D., Greineder C.F., Hood E.D., Muzykantov V.R. Endothelial targeting of liposomes encapsulating SOD/catalase mimetic EUK-134 alleviates acute pulmonary inflammation. J. Control Release. 2014;177:34–41. PubMed PMC
Dziubla T.D., Karim A., Muzykantov V.R. Polymer nanocarriers protecting active enzyme cargo against proteolysis. J. Control Release. 2005;102:427–439. PubMed
Barlaka E., Galatou E., Mellidis K., Ravingerova T., Lazou A. Role of pleiotropic properties of peroxisome proliferator-activated receptors in the heart: focus on the nonmetabolic effects in cardiac protection. Cardiovasc Ther. 2016;34:37–48. PubMed
Ibarra-Lara L., Hong E., Soria-Castro E., Torres-Narvaez J.C., Perez-Severiano F., Del Valle-Mondragon L., Cervantes-Perez L.G., Ramirez-Ortega M., Pastelin-Hernandez G.S., Sanchez-Mendoza A. Clofibrate PPARalpha activation reduces oxidative stress and improves ultrastructure and ventricular hemodynamics in no-flow myocardial ischemia. J. Cardiovasc Pharmacol. 2012;60:323–334. PubMed
Barlaka E., Ledvenyiova V., Galatou E., Ferko M., Carnicka S., Ravingerova T., Lazou A. Delayed cardioprotective effects of WY-14643 are associated with inhibition of MMP-2 and modulation of Bcl-2 family proteins through PPAR-alpha activation in rat hearts subjected to global ischaemia-reperfusion. Can. J. Physiol. Pharmacol. 2013;91:608–616. PubMed
Barlaka E., Gorbe A., Gaspar R., Paloczi J., Ferdinandy P., Lazou A. Activation of PPARbeta/delta protects cardiac myocytes from oxidative stress-induced apoptosis by suppressing generation of reactive oxygen/nitrogen species and expression of matrix metalloproteinases. Pharmacol. Res. 2015;95–96:102–110. PubMed
Lee H., Ham S.A., Kim M.Y., Kim J.H., Paek K.S., Kang E.S., Kim H.J., Hwang J.S., Yoo T., Park C., Kim J.H., Lim D.S., Han C.W., Seo H.G. Activation of PPARdelta counteracts angiotensin II-induced ROS generation by inhibiting rac1 translocation in vascular smooth muscle cells. Free Radic. Res. 2012;46:912–919. PubMed
Liu J., Wang P., Luo J., Huang Y., He L., Yang H., Li Q., Wu S., Zhelyabovska O., Yang Q. Peroxisome proliferator-activated receptor beta/delta activation in adult hearts facilitates mitochondrial function and cardiac performance under pressure-overload condition. Hypertension. 2011;57:223–230. PubMed PMC
Ravingerova T., Carnicka S., Nemcekova M., Ledvenyiova V., Adameova A., Kelly T., Barlaka E., Galatou E., Khandelwal V.K., Lazou A. PPAR-alpha activation as a preconditioning-like intervention in rats in vivo confers myocardial protection against acute ischaemia-reperfusion injury: involvement of PI3K-Akt. Can. J. Physiol. Pharmacol. 2012;90:1135–1144. PubMed
Ravingerova T., Ledvenyiova-Farkasova V., Ferko M., Bartekova M., Bernatova I., Pechanova O., Adameova A., Kolar F., Lazou A. Pleiotropic preconditioning-like cardioprotective effects of hypolipidemic drugs in acute ischemia-reperfusion in normal and hypertensive rats. Can. J. Physiol. Pharmacol. 2015;93:495–503. PubMed
Baggio L.L., Drucker D.J. Biology of incretins: glp-1 and GIP. Gastroenterology. 2007;132:2131–2157. PubMed
Lund P.K., Goodman R.H., Dee P.C., Habener J.F. Pancreatic preproglucagon cDNA contains two glucagon-related coding sequences arranged in tandem. Proc. Natl. Acad. Sci. USA. 1982;79:345–349. PubMed PMC
Mentlein R., Gallwitz B., Schmidt W.E. Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum. Eur. J. Biochem. 1993;214:829–835. PubMed
Kieffer T.J., McIntosh C.H., Pederson R.A. Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV. Endocrinology. 1995;136:3585–3596. PubMed
Matsubara J., Sugiyama S., Sugamura K., Nakamura T., Fujiwara Y., Akiyama E., Kurokawa H., Nozaki T., Ohba K., Konishi M., Maeda H., Izumiya Y., Kaikita K., Sumida H., Jinnouchi H., Matsui K., Kim-Mitsuyama S., Takeya M., Ogawa H. A dipeptidyl peptidase-4 inhibitor, des-fluoro-sitagliptin, improves endothelial function and reduces atherosclerotic lesion formation in apolipoprotein E-deficient mice. J. Am. Coll. Cardiol. 2012;59:265–276. PubMed
Shah Z., Kampfrath T., Deiuliis J.A., Zhong J., Pineda C., Ying Z., Xu X., Lu B., Moffatt-Bruce S., Durairaj R., Sun Q., Mihai G., Maiseyeu A., Rajagopalan S. Long-term dipeptidyl-peptidase 4 inhibition reduces atherosclerosis and inflammation via effects on monocyte recruitment and chemotaxis. Circulation. 2011;124:2338–2349. PubMed PMC
Nishioka T., Shinohara M., Tanimoto N., Kumagai C., Hashimoto K. Sitagliptin, a dipeptidyl peptidase-IV inhibitor, improves psoriasis. Dermatology. 2012;224:20–21. PubMed
Kern M., Kloting N., Niessen H.G., Thomas L., Stiller D., Mark M., Klein T., Bluher M. Linagliptin improves insulin sensitivity and hepatic steatosis in diet-induced obesity. PLoS One. 2012;7:e38744. PubMed PMC
Darsalia V., Ortsater H., Olverling A., Darlof E., Wolbert P., Nystrom T., Klein T., Sjoholm A., Patrone C. The DPP-4 inhibitor linagliptin counteracts stroke in the normal and diabetic mouse brain: a comparison with glimepiride. Diabetes. 2013;62:1289–1296. PubMed PMC
Kroller-Schon S., Knorr M., Hausding M., Oelze M., Schuff A., Schell R., Sudowe S., Scholz A., Daub S., Karbach S., Kossmann S., Gori T., Wenzel P., Schulz E., Grabbe S., Klein T., Munzel T., Daiber A. Glucose-independent improvement of vascular dysfunction in experimental sepsis by dipeptidyl-peptidase 4 inhibition. Cardiovasc Res. 2012;96:140–149. PubMed
Cameron-Vendrig A., Reheman A., Siraj M.A., Xu X.R., Wang Y., Lei X., Afroze T., Shikatani E., El-Mounayri O., Noyan H., Weissleder R., Ni H., Husain M. Glucagon-like peptide 1 receptor activation attenuates platelet aggregation and thrombosis. Diabetes. 2016;65:1714–1723. PubMed
Harman D. Aging: a theory based on free radical and radiation chemistry. J. Gerontol. 1956;11:298–300. PubMed
Miquel J., Economos A.C., Fleming J., Johnson J.E., Jr. Mitochondrial role in cell aging. Exp. Gerontol. 1980;15:575–591. PubMed
Kleikers P.W., Wingler K., Hermans J.J., Diebold I., Altenhofer S., Radermacher K.A., Janssen B., Gorlach A., Schmidt H.H. NADPH oxidases as a source of oxidative stress and molecular target in ischemia/reperfusion injury. J. Mol. Med. 2012;90:1391–1406. PubMed
Park L., Zhou P., Pitstick R., Capone C., Anrather J., Norris E.H., Younkin L., Younkin S., Carlson G., McEwen B.S., Iadecola C. Nox2-derived radicals contribute to neurovascular and behavioral dysfunction in mice overexpressing the amyloid precursor protein. Proc. Natl. Acad. Sci. USA. 2008;105:1347–1352. PubMed PMC
Chondrogianni N., Stratford F.L., Trougakos I.P., Friguet B., Rivett A.J., Gonos E.S. Central role of the proteasome in senescence and survival of human fibroblasts: induction of a senescence-like phenotype upon its inhibition and resistance to stress upon its activation. J. Biol. Chem. 2003;278:28026–28037. PubMed
Liu C.K., Lyass A., Larson M.G., Massaro J.M., Wang N., D'Agostino R.B., Sr., Benjamin E.J., Murabito J.M. Biomarkers of oxidative stress are associated with frailty: the Framingham offspring study. Age. 2016;38:1. PubMed PMC
Ingles M., Gambini J., Carnicero J.A., Garcia-Garcia F.J., Rodriguez-Manas L., Olaso-Gonzalez G., Dromant M., Borras C., Vina J. Oxidative stress is related to frailty, not to age or sex, in a geriatric population: lipid and protein oxidation as biomarkers of frailty. J. Am. Geriatr. Soc. 2014;62:1324–1328. PubMed
Gomez-Cabrera M.C., Ristow M., Vina J. Antioxidant supplements in exercise: worse than useless? Am. J. Physiol. Endocrinol. Metab. 2012;302:E476–E477. (author reply E478-E479) PubMed
Zhang Y., Ikeno Y., Qi W., Chaudhuri A., Li Y., Bokov A., Thorpe S.R., Baynes J.W., Epstein C., Richardson A., Van Remmen H. Mice deficient in both Mn superoxide dismutase and glutathione peroxidase-1 have increased oxidative damage and a greater incidence of pathology but no reduction in longevity. J. Gerontol. A Biol. Sci. Med. Sci. 2009;64:1212–1220. PubMed PMC
Jin K. Modern biological theories of aging. Aging Dis. 2010;1:72–74. PubMed PMC
Vina J., Borras C., Miquel J. Theories of ageing. IUBMB Life. 2007;59:249–254. PubMed
Bedard K., Krause K.H. The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol. Rev. 2007;87:245–313. PubMed
Geiszt M. NADPH oxidases: new kids on the block. Cardiovasc Res. 2006;71:289–299. PubMed
Liang S., Kisseleva T., Brenner D.A. The role of NADPH Oxidases (NOXs) in liver fibrosis and the activation of myofibroblasts. Front. Physiol. 2016;7:17. PubMed PMC
Lener B., Koziel R., Pircher H., Hutter E., Greussing R., Herndler-Brandstetter D., Hermann M., Unterluggauer H., Jansen-Durr P. The NADPH oxidase Nox4 restricts the replicative lifespan of human endothelial cells. Biochem. J. 2009;423:363–374. PubMed PMC
Koziel R., Pircher H., Kratochwil M., Lener B., Hermann M., Dencher N.A., Jansen-Durr P. Mitochondrial respiratory chain complex I is inactivated by NADPH oxidase Nox4. Biochem. J. 2013;452:231–239. PubMed
Weyemi U., Lagente-Chevallier O., Boufraqech M., Prenois F., Courtin F., Caillou B., Talbot M., Dardalhon M., Al Ghuzlan A., Bidart J.M., Schlumberger M., Dupuy C. ROS-generating NADPH oxidase NOX4 is a critical mediator in oncogenic H-Ras-induced DNA damage and subsequent senescence. Oncogene. 2012;31:1117–1129. PubMed PMC
Kodama R., Kato M., Furuta S., Ueno S., Zhang Y., Matsuno K., Yabe-Nishimura C., Tanaka E., Kamata T. ROS-generating oxidases Nox1 and Nox4 contribute to oncogenic Ras-induced premature senescence. Genes Cells. 2013;18:32–41. PubMed
Senturk S., Mumcuoglu M., Gursoy-Yuzugullu O., Cingoz B., Akcali K.C., Ozturk M. Transforming growth factor-beta induces senescence in hepatocellular carcinoma cells and inhibits tumor growth. Hepatology. 2010;52:966–974. PubMed
Ago T., Matsushima S., Kuroda J., Zablocki D., Kitazono T., Sadoshima J. The NADPH oxidase Nox4 and aging in the heart. Aging. 2010;2:1012–1016. PubMed PMC
Wang M., Zhang J., Walker S.J., Dworakowski R., Lakatta E.G., Shah A.M. Involvement of NADPH oxidase in age-associated cardiac remodeling. J. Mol. Cell Cardiol. 2010;48:765–772. PubMed PMC
Vendrov A.E., Vendrov K.C., Smith A., Yuan J., Sumida A., Robidoux J., Runge M.S., Madamanchi N.R. NOX4 NADPH oxidase-dependent mitochondrial oxidative stress in aging-associated cardiovascular disease. Antioxid. Redox Signal. 2015;23:1389–1409. PubMed PMC
Kleinschnitz C., Grund H., Wingler K., Armitage M.E., Jones E., Mittal M., Barit D., Schwarz T., Geis C., Kraft P., Barthel K., Schuhmann M.K., Herrmann A.M., Meuth S.G., Stoll G., Meurer S., Schrewe A., Becker L., Gailus-Durner V., Fuchs H., Klopstock T., de Angelis M.H., Jandeleit-Dahm K., Shah A.M., Weissmann N., Schmidt H.H. Post-stroke inhibition of induced NADPH oxidase type 4 prevents oxidative stress and neurodegeneration. PLoS Biol. 2010;8 PubMed PMC
Piera-Velazquez S., Jimenez S.A. Role of cellular senescence and NOX4-mediated oxidative stress in systemic sclerosis pathogenesis. Curr. Rheumatol. Rep. 2015;17:473. PubMed PMC
Hecker L., Logsdon N.J., Kurundkar D., Kurundkar A., Bernard K., Hock T., Meldrum E., Sanders Y.Y., Thannickal V.J. Reversal of persistent fibrosis in aging by targeting Nox4-Nrf2 redox imbalance. Sci. Transl. Med. 2014;6:231ra247. PubMed PMC
Armanios M. Telomerase and idiopathic pulmonary fibrosis. Mutat. Res. 2012;730:52–58. PubMed PMC
Stanley S.E., Noth I., Armanios M. What the genetics "RTEL"ing us about telomeres and pulmonary fibrosis. Am. J. Respir. Crit. Care Med. 2015;191:608–610. PubMed PMC
Zhang W., Wang T., Qin L., Gao H.M., Wilson B., Ali S.F., Zhang W., Hong J.S., Liu B. Neuroprotective effect of dextromethorphan in the MPTP Parkinson's disease model: role of NADPH oxidase. FASEB J. 2004;18:589–591. PubMed
Holl M., Koziel R., Schafer G., Pircher H., Pauck A., Hermann M., Klocker H., Jansen-Durr P., Sampson N. ROS signaling by NADPH oxidase 5 modulates the proliferation and survival of prostate carcinoma cells. Mol. Carcinog. 2016;55:27–39. PubMed PMC
Sampson N., Koziel R., Zenzmaier C., Bubendorf L., Plas E., Jansen-Durr P., Berger P. ROS signaling by NOX4 drives fibroblast-to-myofibroblast differentiation in the diseased prostatic stroma. Mol. Endocrinol. 2011;25:503–515. PubMed PMC
Ayala G., Tuxhorn J.A., Wheeler T.M., Frolov A., Scardino P.T., Ohori M., Wheeler M., Spitler J., Rowley D.R. Reactive stroma as a predictor of biochemical-free recurrence in prostate cancer. Clin. Cancer Res. 2003;9:4792–4801. PubMed
Hohn A., Jung T., Grimm S., Grune T. Lipofuscin-bound iron is a major intracellular source of oxidants: role in senescent cells. Free Radic. Biol. Med. 2010;48:1100–1108. PubMed
Kastle M., Grune T. Interactions of the proteasomal system with chaperones: protein triage and protein quality control. Prog. Mol. Biol. Transl. Sci. 2012;109:113–160. PubMed
Jung T., Catalgol B., Grune T. The proteasomal system. Mol. Asp. Med. 2009;30:191–296. PubMed
Hohn A., Jung T., Grimm S., Catalgol B., Weber D., Grune T. Lipofuscin inhibits the proteasome by binding to surface motifs. Free Radic. Biol. Med. 2011;50:585–591. PubMed
Keck S., Nitsch R., Grune T., Ullrich O. Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease. J. Neurochem. 2003;85:115–122. PubMed
Catalgol B., Ziaja I., Breusing N., Jung T., Hohn A., Alpertunga B., Schroeder P., Chondrogianni N., Gonos E.S., Petropoulos I., Friguet B., Klotz L.O., Krutmann J., Grune T. The proteasome is an integral part of solar ultraviolet a radiation-induced gene expression. J. Biol. Chem. 2009;284:30076–30086. PubMed PMC
Kastle M., Woschee E., Grune T. Histone deacetylase 6 (HDAC6) plays a crucial role in p38MAPK-dependent induction of heme oxygenase-1 (HO-1) in response to proteasome inhibition. Free Radic. Biol. Med. 2012;53:2092–2101. PubMed
Chondrogianni N., Georgila K., Kourtis N., Tavernarakis N., Gonos E.S. 20S proteasome activation promotes life span extension and resistance to proteotoxicity in Caenorhabditis elegans. FASEB J. 2015;29:611–622. PubMed PMC
Vilchez D., Morantte I., Liu Z., Douglas P.M., Merkwirth C., Rodrigues A.P., Manning G., Dillin A. RPN-6 determines C. elegans longevity under proteotoxic stress conditions. Nature. 2012;489:263–268. PubMed
Tonoki A., Kuranaga E., Tomioka T., Hamazaki J., Murata S., Tanaka K., Miura M. Genetic evidence linking age-dependent attenuation of the 26S proteasome with the aging process. Mol. Cell Biol. 2009;29:1095–1106. PubMed PMC
Kapeta S., Chondrogianni N., Gonos E.S. Nuclear erythroid factor 2-mediated proteasome activation delays senescence in human fibroblasts. J. Biol. Chem. 2010;285:8171–8184. PubMed PMC
Papaevgeniou N., Sakellari M., Jha S., Tavernarakis N., Holmberg C.I., Gonos E.S., Chondrogianni N. 18alpha-glycyrrhetinic acid proteasome activator decelerates aging and Alzheimer's disease progression in caenorhabditis elegans and neuronal cultures. Antioxid. Redox Signal. 2016;25:855–869. PubMed PMC
Chondrogianni N., Kapeta S., Chinou I., Vassilatou K., Papassideri I., Gonos E.S. Anti-ageing and rejuvenating effects of quercetin. Exp. Gerontol. 2010;45:763–771. PubMed
Regitz C., Dussling L.M., Wenzel U. Amyloid-beta (Abeta(1)(-)(4)(2))-induced paralysis in Caenorhabditis elegans is inhibited by the polyphenol quercetin through activation of protein degradation pathways. Mol. Nutr. Food Res. 2014;58:1931–1940. PubMed
Mikhed Y., Daiber A., Steven S. Mitochondrial oxidative stress, mitochondrial DNA damage and their role in age-related vascular dysfunction. Int. J. Mol. Sci. 2015;16:15918–15953. PubMed PMC
Moskalev A.A., Aliper A.M., Smit-McBride Z., Buzdin A., Zhavoronkov A. Genetics and epigenetics of aging and longevity. Cell Cycle. 2014;13:1063–1077. PubMed PMC
Perez V.I., Bokov A., Van Remmen H., Mele J., Ran Q., Ikeno Y., Richardson A. Is the oxidative stress theory of aging dead? Biochim. Biophys. Acta. 2009;1790:1005–1014. PubMed PMC
Muller F.L., Lustgarten M.S., Jang Y., Richardson A., Van Remmen H. Trends in oxidative aging theories. Free Radic. Biol. Med. 2007;43:477–503. PubMed
Li Y., Huang T.T., Carlson E.J., Melov S., Ursell P.C., Olson J.L., Noble L.J., Yoshimura M.P., Berger C., Chan P.H. Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase. Nat. Genet. 1995;11:376–381. PubMed
Camici G.G., Cosentino F., Tanner F.C., Luscher T.F. The role of p66Shc deletion in age-associated arterial dysfunction and disease states. J. Appl. Physiol. 2008;105:1628–1631. PubMed
Dai D.F., Chiao Y.A., Marcinek D.J., Szeto H.H., Rabinovitch P.S. Mitochondrial oxidative stress in aging and healthspan. Longev. Health. 2014;3:6. PubMed PMC
Hamilton R.T., Walsh M.E., Van Remmen H. Mouse models of oxidative stress indicate a role for modulating healthy aging. J. Clin. Exp. Pathol. 2012;Suppl 4 PubMed PMC
Wenzel P., Schuhmacher S., Kienhofer J., Muller J., Hortmann M., Oelze M., Schulz E., Treiber N., Kawamoto T., Scharffetter-Kochanek K., Munzel T., Burkle A., Bachschmid M.M., Daiber A. Manganese superoxide dismutase and aldehyde dehydrogenase deficiency increase mitochondrial oxidative stress and aggravate age-dependent vascular dysfunction. Cardiovasc. Res. 2008;80:280–289. PubMed PMC
Doughan A.K., Harrison D.G., Dikalov S.I. Molecular mechanisms of angiotensin II-mediated mitochondrial dysfunction: linking mitochondrial oxidative damage and vascular endothelial dysfunction. Circ. Res. 2008;102:488–496. PubMed
Schottker B., Brenner H., Jansen E.H., Gardiner J., Peasey A., Kubinova R., Pajak A., Topor-Madry R., Tamosiunas A., Saum K.U., Holleczek B., Pikhart H., Bobak M. Evidence for the free radical/oxidative stress theory of ageing from the CHANCES consortium: a meta-analysis of individual participant data. BMC Med. 2015;13:300. PubMed PMC
Capri M., Moreno-Villanueva M., Cevenini E., Pini E., Scurti M., Borelli V., Palmas M.G., Zoli M., Schon C., Siepelmeyer A., Bernhardt J., Fiegl S., Zondag G., de Craen A.J., Hervonen A., Hurme M., Sikora E., Gonos E.S., Voutetakis K., Toussaint O., Debacq-Chainiaux F., Grubeck-Loebenstein B., Burkle A., Franceschi C. MARK-AGE population: from the human model to new insights. Mech. Ageing Dev. 2015;151:13–17. PubMed
Rodriguez-Manas L., Fried L.P. Frailty in the clinical scenario. Lancet. 2015;385:e7–e9. PubMed
Lai H.Y., Chang H.T., Lee Y.L., Hwang S.J. Association between inflammatory markers and frailty in institutionalized older men. Maturitas. 2014;79:329–333. PubMed
Argiles J.M., Campos N., Lopez-Pedrosa J.M., Rueda R., Rodriguez-Manas L. Skeletal muscle regulates metabolism via interorgan crosstalk: roles in health and disease. J. Am. Med Dir. Assoc. 2016;17:789–796. PubMed
Sen C.K., Packer L. Antioxidant and redox regulation of gene transcription. FASEB J. 1996;10:709–720. PubMed
Suzuki Y.J., Forman H.J., Sevanian A. Oxidants as stimulators of signal transduction. Free Radic. Biol. Med. 1997;22:269–285. PubMed
Esposito F., Ammendola R., Faraonio R., Russo T., Cimino F. Redox control of signal transduction, gene expression and cellular senescence. Neurochem. Res. 2004;29:617–628. PubMed
Nauseef W.M., Borregaard N. Neutrophils at work. Nat. Immunol. 2014;15:602–611. PubMed
Forsberg K., Wuttke A., Quadrato G., Chumakov P.M., Wizenmann A., Di Giovanni S. The tumor suppressor p53 fine-tunes reactive oxygen species levels and neurogenesis via PI3 kinase signaling. J. Neurosci. 2013;33:14318–14330. PubMed PMC
Wang K., Zhang T., Dong Q., Nice E.C., Huang C., Wei Y. Redox homeostasis: the linchpin in stem cell self-renewal and differentiation. Cell Death Dis. 2013;4:e537. PubMed PMC
Lourenco C.F., Ledo A., Dias C., Barbosa R.M., Laranjinha J. Neurovascular and neurometabolic derailment in aging and Alzheimer's disease. Front. Aging Neurosci. 2015;7:103. PubMed PMC
McBean G.J. The transsulfuration pathway: a source of cysteine for glutathione in astrocytes. Amino Acids. 2012;42:199–205. PubMed
Biswas S.K. Does the interdependence between oxidative stress and inflammation explain the antioxidant paradox? Oxid. Med. Cell Longev. 2016;2016:5698931. PubMed PMC
Nauseef W.M. How human neutrophils kill and degrade microbes: an integrated view. Immunol. Rev. 2007;219:88–102. PubMed
Babior B.M. Phagocytes and oxidative stress. Am. J. Med. 2000;109:33–44. PubMed
Sareila O., Kelkka T., Pizzolla A., Hultqvist M., Holmdahl R. NOX2 complex-derived ROS as immune regulators. Antioxid. Redox Signal. 2011;15:2197–2208. PubMed
Gelderman K.A., Hultqvist M., Holmberg J., Olofsson P., Holmdahl R. T cell surface redox levels determine T cell reactivity and arthritis susceptibility. Proc. Natl. Acad. Sci. USA. 2006;103:12831–12836. PubMed PMC
El-Benna J., Dang P.M., Gougerot-Pocidalo M.A. Priming of the neutrophil NADPH oxidase activation: role of p47phox phosphorylation and NOX2 mobilization to the plasma membrane. Semin. Immunopathol. 2008;30:279–289. PubMed
Lee K., Won H.Y., Bae M.A., Hong J.H., Hwang E.S. Spontaneous and aging-dependent development of arthritis in NADPH oxidase 2 deficiency through altered differentiation of CD11b+ and Th/Treg cells. Proc. Natl. Acad. Sci. USA. 2011;108:9548–9553. PubMed PMC
Droge W. Free radicals in the physiological control of cell function. Physiol. Rev. 2002;82:47–95. PubMed
Miesel R., Kurpisz M., Kroger H. Suppression of inflammatory arthritis by simultaneous inhibition of nitric oxide synthase and NADPH oxidase. Free Radic. Biol. Med. 1996;20:75–81. PubMed
Roos D., Kuhns D.B., Maddalena A., Roesler J., Lopez J.A., Ariga T., Avcin T., de Boer M., Bustamante J., Condino-Neto A., Di Matteo G., He J., Hill H.R., Holland S.M., Kannengiesser C., Koker M.Y., Kondratenko I., van Leeuwen K., Malech H.L., Marodi L., Nunoi H., Stasia M.J., Ventura A.M., Witwer C.T., Wolach B., Gallin J.I. Hematologically important mutations: x-linked chronic granulomatous disease (third update) Blood Cells Mol. Dis. 2010;45:246–265. PubMed PMC
Roos D., Kuhns D.B., Maddalena A., Bustamante J., Kannengiesser C., de Boer M., van Leeuwen K., Koker M.Y., Wolach B., Roesler J., Malech H.L., Holland S.M., Gallin J.I., Stasia M.J. Hematologically important mutations: the autosomal recessive forms of chronic granulomatous disease (second update) Blood Cells Mol. Dis. 2010;44:291–299. PubMed PMC
Kuhns D.B., Alvord W.G., Heller T., Feld J.J., Pike K.M., Marciano B.E., Uzel G., DeRavin S.S., Priel D.A., Soule B.P., Zarember K.A., Malech H.L., Holland S.M., Gallin J.I. Residual NADPH oxidase and survival in chronic granulomatous disease. N. Engl. J. Med. 2010;363:2600–2610. PubMed PMC
van den Berg J.M., van Koppen E., Ahlin A., Belohradsky B.H., Bernatowska E., Corbeel L., Espanol T., Fischer A., Kurenko-Deptuch M., Mouy R., Petropoulou T., Roesler J., Seger R., Stasia M.J., Valerius N.H., Weening R.S., Wolach B., Roos D., Kuijpers T.W. Chronic granulomatous disease: the European experience. PLoS One. 2009;4:e5234. PubMed PMC
Boulais J., Trost M., Landry C.R., Dieckmann R., Levy E.D., Soldati T., Michnick S.W., Thibault P., Desjardins M. Molecular characterization of the evolution of phagosomes. Mol. Syst. Biol. 2010;6:423. PubMed PMC
Cosson P., Soldati T. Eat, kill or die: when amoeba meets bacteria. Curr. Opin. Microbiol. 2008;11:271–276. PubMed
Lardy B., Bof M., Aubry L., Paclet M.H., Morel F., Satre M., Klein G. NADPH oxidase homologs are required for normal cell differentiation and morphogenesis in Dictyostelium discoideum. Biochim. Biophys. Acta. 2005;1744:199–212. PubMed
Basu S., Fey P., Jimenez-Morales D., Dodson R.J., Chisholm R.L. dictyBase 2015: expanding data and annotations in a new software environment. Genesis. 2015;53:523–534. PubMed PMC
Tung S.M., Unal C., Ley A., Pena C., Tunggal B., Noegel A.A., Krut O., Steinert M., Eichinger L. Loss of Dictyostelium ATG9 results in a pleiotropic phenotype affecting growth, development, phagocytosis and clearance and replication of Legionella pneumophila. Cell. Microbiol. 2010;12:765–780. PubMed
Bloomfield G., Pears C. Superoxide signalling required for multicellular development of Dictyostelium. J. Cell Sci. 2003;116:3387–3397. PubMed
Garcia M.X., Alexander H., Mahadeo D., Cotter D.A., Alexander S. The Dictyostelium discoideum prespore-specific catalase B functions to control late development and to protect spore viability. Biochim. Biophys. Acta. 2003;1641:55–64. PubMed
Chen G., Zhuchenko O., Kuspa A. Immune-like phagocyte activity in the social amoeba. Science. 2007;317:678–681. PubMed PMC
Zhang X., Zhuchenko O., Kuspa A., Soldati T. Social amoebae trap and kill bacteria by casting DNA nets. Nat. Commun. 2016;7:10938. PubMed PMC
Zhang X., Soldati T. Of amoebae and men: extracellular DNA traps as an ancient cell-intrinsic defense mechanism. Front. Immunol. 2016;7:269. PubMed PMC
Rieber N., Hector A., Kuijpers T., Roos D., Hartl D. Current concepts of hyperinflammation in chronic granulomatous disease. Clin. Dev. Immunol. 2012;2012:252460. PubMed PMC
Brown K.L., Bylund J., MacDonald K.L., Song-Zhao G.X., Elliott M.R., Falsafi R., Hancock R.E., Speert D.P. ROS-deficient monocytes have aberrant gene expression that correlates with inflammatory disorders of chronic granulomatous disease. Clin. Immunol. 2008;129:90–102. PubMed
de Luca A., Smeekens S.P., Casagrande A., Iannitti R., Conway K.L., Gresnigt M.S., Begun J., Plantinga T.S., Joosten L.A., van der Meer J.W., Chamilos G., Netea M.G., Xavier R.J., Dinarello C.A., Romani L., van de Veerdonk F.L. IL-1 receptor blockade restores autophagy and reduces inflammation in chronic granulomatous disease in mice and in humans. Proc. Natl. Acad. Sci. USA. 2014;111:3526–3531. PubMed PMC
Harbort C.J., Soeiro-Pereira P.V., von Bernuth H., Kaindl A.M., Costa-Carvalho B.T., Condino-Neto A., Reichenbach J., Roesler J., Zychlinsky A., Amulic B. Neutrophil oxidative burst activates ATM to regulate cytokine production and apoptosis. Blood. 2015;126:2842–2851. PubMed PMC
Violi F., Sanguigni V., Carnevale R., Plebani A., Rossi P., Finocchi A., Pignata C., De Mattia D., Martire B., Pietrogrande M.C., Martino S., Gambineri E., Soresina A.R., Pignatelli P., Martino F., Basili S., Loffredo L. Hereditary deficiency of gp91(phox) is associated with enhanced arterial dilatation: results of a multicenter study. Circulation. 2009;120:1616–1622. PubMed
Kishida K.T., Hoeffer C.A., Hu D., Pao M., Holland S.M., Klann E. Synaptic plasticity deficits and mild memory impairments in mouse models of chronic granulomatous disease. Mol. Cell Biol. 2006;26:5908–5920. PubMed PMC
Pao M., Wiggs E.A., Anastacio M.M., Hyun J., DeCarlo E.S., Miller J.T., Anderson V.L., Malech H.L., Gallin J.I., Holland S.M. Cognitive function in patients with chronic granulomatous disease: a preliminary report. Psychosomatics. 2004;45:230–234. PubMed
Cole T.S., McKendrick F., Cant A.J., Pearce M.S., Cale C.M., Goldblatt D.R., Gennery A.R., Titman P. Cognitive ability in children with chronic granulomatous disease: a comparison of those managed conservatively with those who have undergone hematopoietic stem cell transplant. Neuropediatrics. 2013;44:230–232. PubMed
Iadecola C. Neurovascular regulation in the normal brain and in Alzheimer's disease. Nat. Rev. Neurosci. 2004;5:347–360. PubMed
Raichle M.E., Mintun M.A. Brain work and brain imaging. Annu. Rev. Neurosci. 2006;29:449–476. PubMed
Santos R.M., Lourenco C.F., Piedade A.P., Andrews R., Pomerleau F., Huettl P., Gerhardt G.A., Laranjinha J., Barbosa R.M. A comparative study of carbon fiber-based microelectrodes for the measurement of nitric oxide in brain tissue. Biosens. Bioelectron. 2008;24:704–709. PubMed
Lourenco C.F., Santos R.M., Barbosa R.M., Cadenas E., Radi R., Laranjinha J. Neurovascular coupling in hippocampus is mediated via diffusion by neuronal-derived nitric oxide. Free Radic. Biol. Med. 2014;73:421–429. PubMed
Cleeter M.W., Cooper J.M., Darley-Usmar V.M., Moncada S., Schapira A.H. Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide. Implications for neurodegenerative diseases. FEBS Lett. 1994;345:50–54. PubMed
Ledo A., Barbosa R., Cadenas E., Laranjinha J. Dynamic and interacting profiles of *NO and O2 in rat hippocampal slices. Free Radic. Biol. Med. 2010;48:1044–1050. PubMed PMC
Ledo A., Barbosa R.M., Gerhardt G.A., Cadenas E., Laranjinha J. Concentration dynamics of nitric oxide in rat hippocampal subregions evoked by stimulation of the NMDA glutamate receptor. Proc. Natl. Acad. Sci. USA. 2005;102:17483–17488. PubMed PMC
Dringen R., Pfeiffer B., Hamprecht B. Synthesis of the antioxidant glutathione in neurons: supply by astrocytes of CysGly as precursor for neuronal glutathione. J. Neurosci. 1999;19:562–569. PubMed PMC
Kandil S., Brennan L., McBean G.J. Glutathione depletion causes a JNK and p38MAPK-mediated increase in expression of cystathionine-gamma-lyase and upregulation of the transsulfuration pathway in C6 glioma cells. Neurochem. Int. 2010;56:611–619. PubMed
Mysona B., Dun Y., Duplantier J., Ganapathy V., Smith S.B. Effects of hyperglycemia and oxidative stress on the glutamate transporters GLAST and system xc- in mouse retinal Muller glial cells. Cell Tissue Res. 2009;335:477–488. PubMed PMC
Banjac A., Perisic T., Sato H., Seiler A., Bannai S., Weiss N., Kolle P., Tschoep K., Issels R.D., Daniel P.T., Conrad M., Bornkamm G.W. The cystine/cysteine cycle: a redox cycle regulating susceptibility versus resistance to cell death. Oncogene. 2008;27:1618–1628. PubMed
Pampliega O., Domercq M., Soria F.N., Villoslada P., Rodriguez-Antiguedad A., Matute C. Increased expression of cystine/glutamate antiporter in multiple sclerosis. J. Neuroinflamm. 2011;8:63. PubMed PMC
Mesci P., Zaidi S., Lobsiger C.S., Millecamps S., Escartin C., Seilhean D., Sato H., Mallat M., Boillee S. System xC- is a mediator of microglial function and its deletion slows symptoms in amyotrophic lateral sclerosis mice. Brain. 2015;138:53–68. PubMed PMC
Watkins S., Sontheimer H. Unique biology of gliomas: challenges and opportunities. Trends Neurosci. 2012;35:546–556. PubMed PMC
Chen L., Li X., Liu L., Yu B., Xue Y., Liu Y. Erastin sensitizes glioblastoma cells to temozolomide by restraining xCT and cystathionine-gamma-lyase function. Oncol. Rep. 2015;33:1465–1474. PubMed
Schliebs R., Arendt T. The significance of the cholinergic system in the brain during aging and in Alzheimer's disease. J. Neural Transm. 2006;113:1625–1644. PubMed
McKinney M., Jacksonville M.C. Brain cholinergic vulnerability: relevance to behavior and disease. Biochem. Pharmacol. 2005;70:1115–1124. PubMed
Wang H., Yu M., Ochani M., Amella C.A., Tanovic M., Susarla S., Li J.H., Wang H., Yang H., Ulloa L., Al-Abed Y., Czura C.J., Tracey K.J. Nicotinic acetylcholine receptor alpha7 subunit is an essential regulator of inflammation. Nature. 2003;421:384–388. PubMed
E. Navarro, L. Gonzalez-Lafuente, I. Perez-Liebana, I. Buendia, E. Lopez-Bernardo, C. Sanchez-Ramos, I. Prieto, A. Cuadrado, J. Satrustegui, S. Cadenas, M. Monsalve, M.G. Lopez, Heme-oxygenase I and PCG-1alpha regulate mitochondrial biogenesis via microglial activation of Alpha7 nicotinic acetylcholine receptors using PNU282987. Antioxid. Redox Signal., 2016. http://dx.doi.org/10.1089/ars.2016.6698. PubMed DOI
Parada E., Egea J., Buendia I., Negredo P., Cunha A.C., Cardoso S., Soares M.P., Lopez M.G. The microglial alpha7-acetylcholine nicotinic receptor is a key element in promoting neuroprotection by inducing heme oxygenase-1 via nuclear factor erythroid-2-related factor 2. Antioxid. Redox Signal. 2013;19:1135–1148. PubMed PMC
Egea J., Buendia I., Parada E., Navarro E., Leon R., Lopez M.G. Anti-inflammatory role of microglial alpha7 nAChRs and its role in neuroprotection. Biochem. Pharmacol. 2015;97:463–472. PubMed
Shakirzyanova A., Valeeva G., Giniatullin A., Naumenko N., Fulle S., Akulov A., Atalay M., Nikolsky E., Giniatullin R. Age-dependent action of reactive oxygen species on transmitter release in mammalian neuromuscular junctions. Neurobiol. Aging. 2016;38:73–81. PubMed
Bukharaeva E., Shakirzyanova A., Khuzakhmetova V., Sitdikova G., Giniatullin R. Homocysteine aggravates ROS-induced depression of transmitter release from motor nerve terminals: potential mechanism of peripheral impairment in motor neuron diseases associated with hyperhomocysteinemia. Front. Cell. Neurosci. 2015;9:391. PubMed PMC
Giniatullin A., Petrov A., Giniatullin R. The involvement of P2Y12 receptors, NADPH oxidase, and lipid rafts in the action of extracellular ATP on synaptic transmission at the frog neuromuscular junction. Neuroscience. 2015;285:324–332. PubMed
Giniatullin A.R., Darios F., Shakirzyanova A., Davletov B., Giniatullin R. SNAP25 is a pre-synaptic target for the depressant action of reactive oxygen species on transmitter release. J. Neurochem. 2006;98:1789–1797. PubMed
Debelec-Butuner B., Ertunc N., Korkmaz K.S. Inflammation contributes to NKX3.1 loss and augments DNA damage but does not alter the DNA damage response via increased SIRT1 expression. J. Inflamm. 2015;12:12. PubMed PMC
Zhao S., Zhang Y., Zhang Q., Wang F., Zhang D. Toll-like receptors and prostate cancer. Front. Immunol. 2014;5:352. PubMed PMC
Oblak A., Jerala R. Toll-like receptor 4 activation in cancer progression and therapy. Clin. Dev. Immunol. 2011;2011:609579. PubMed PMC
Kundu S.D., Lee C., Billips B.K., Habermacher G.M., Zhang Q., Liu V., Wong L.Y., Klumpp D.J., Thumbikat P. The toll-like receptor pathway: a novel mechanism of infection-induced carcinogenesis of prostate epithelial cells. Prostate. 2008;68:223–229. PubMed
Debelec-Butuner B., Alapinar C., Ertunc N., Gonen-Korkmaz C., Yorukoglu K., Korkmaz K.S. TNFalpha-mediated loss of beta-catenin/E-cadherin association and subsequent increase in cell migration is partially restored by NKX3.1 expression in prostate cells. PLoS One. 2014;9:e109868. PubMed PMC
Yang H., Zhou H., Feng P., Zhou X., Wen H., Xie X., Shen H., Zhu X. Reduced expression of Toll-like receptor 4 inhibits human breast cancer cells proliferation and inflammatory cytokines secretion. J. Exp. Clin. Cancer Res. 2010;29:92. PubMed PMC
Manda G., Isvoranu G., Comanescu M.V., Manea A., Debelec Butuner B., Korkmaz K.S. The redox biology network in cancer pathophysiology and therapeutics. Redox Biol. 2015;5:347–357. PubMed PMC
Winkelstein J.A., Marino M.C., Johnston R.B., Jr., Boyle J., Curnutte J., Gallin J.I., Malech H.L., Holland S.M., Ochs H., Quie P., Buckley R.H., Foster C.B., Chanock S.J., Dickler H. Chronic granulomatous disease. Report on a national registry of 368 patients. Medicine. 2000;79:155–169. PubMed
Quie P.G., White J.G., Holmes B., Good R.A. In vitro bactericidal capacity of human polymorphonuclear leukocytes: diminished activity in chronic granulomatous disease of childhood. J. Clin. Investig. 1967;46:668–679. PubMed PMC
Holmes B., Quie P.G., Windhorst D.B., Good R.A. Fatal granulomatous disease of childhood. An inborn abnormality of phagocytic function. Lancet. 1966;1:1225–1228. PubMed
Forfia P.R., Zhang X., Ochoa F., Ochoa M., Xu X., Bernstein R., Sehgal P.B., Ferreri N.R., Hintze T.H. Relationship between plasma NOx and cardiac and vascular dysfunction after LPS injection in anesthetized dogs. Am. J. Physiol. 1998;274:H193–H201. PubMed
Singel K.L., Segal B.H. NOX2-dependent regulation of inflammation. Clin. Sci. 2016;130:479–490. PubMed PMC
Han M., Zhang T., Yang L., Wang Z., Ruan J., Chang X. Association between NADPH oxidase (NOX) and lung cancer: a systematic review and meta-analysis. J. Thorac. Dis. 2016;8:1704–1711. PubMed PMC
Kaur A., Webster M.R., Marchbank K., Behera R., Ndoye A., Kugel C.H., 3rd, Dang V.M., Appleton J., O'Connell M.P., Cheng P., Valiga A.A., Morissette R., McDonnell N.B., Ferrucci L., Kossenkov A.V., Meeth K., Tang H.Y., Yin X., Wood W.H., 3rd, Lehrmann E., Becker K.G., Flaherty K.T., Frederick D.T., Wargo J.A., Cooper Z.A., Tetzlaff M.T., Hudgens C., Aird K.M., Zhang R., Xu X., Liu Q., Bartlett E., Karakousis G., Eroglu Z., Lo R.S., Chan M., Menzies A.M., Long G.V., Johnson D.B., Sosman J., Schilling B., Schadendorf D., Speicher D.W., Bosenberg M., Ribas A., Weeraratna A.T. sFRP2 in the aged microenvironment drives melanoma metastasis and therapy resistance. Nature. 2016;532:250–254. PubMed PMC
Piskounova E., Agathocleous M., Murphy M.M., Hu Z., Huddlestun S.E., Zhao Z., Leitch A.M., Johnson T.M., DeBerardinis R.J., Morrison S.J. Oxidative stress inhibits distant metastasis by human melanoma cells. Nature. 2015;527:186–191. PubMed PMC
Benhar M., Shytaj I.L., Stamler J.S., Savarino A. Dual targeting of the thioredoxin and glutathione systems in cancer and HIV. J. Clin. Investig. 2016;126:1630–1639. PubMed PMC
Delmaghani S., Defourny J., Aghaie A., Beurg M., Dulon D., Thelen N., Perfettini I., Zelles T., Aller M., Meyer A., Emptoz A., Giraudet F., Leibovici M., Dartevelle S., Soubigou G., Thiry M., Vizi E.S., Safieddine S., Hardelin J.P., Avan P., Petit C. Hypervulnerability to sound exposure through impaired adaptive proliferation of peroxisomes. Cell. 2015;163:894–906. PubMed
Rochette L., Zeller M., Cottin Y., Vergely C. Diabetes, oxidative stress and therapeutic strategies. Biochim. Biophys. Acta. 2014;1840:2709–2729. PubMed
Wang J., Yang X., Zhang J. Bridges between mitochondrial oxidative stress, ER stress and mTOR signaling in pancreatic beta cells. Cell Signal. 2016;28:1099–1104. PubMed
Jankovic A., Korac A., Buzadzic B., Stancic A., Otasevic V., Ferdinandy P., Daiber A., Korac B. Targeting the nitric oxide/superoxide ratio in adipose tissue: relevance in obesity and diabetes management. Br. J. Pharmacol. 2016 PubMed PMC
Tochhawng L., Deng S., Pervaiz S., Yap C.T. Redox regulation of cancer cell migration and invasion. Mitochondrion. 2013;13:246–253. PubMed
Diaz B., Courtneidge S.A. Redox signaling at invasive microdomains in cancer cells. Free Radic. Biol. Med. 2012;52:247–256. PubMed PMC
Goitre L., Pergolizzi B., Ferro E., Trabalzini L., Retta S.F. Molecular crosstalk between integrins and cadherins: do reactive oxygen species set the talk? J. Signal Transduct. 2012;2012:807682. PubMed PMC
Pani G., Galeotti T., Chiarugi P. Metastasis: cancer cell's escape from oxidative stress. Cancer Metastasis Rev. 2010;29:351–378. PubMed
Wu W.S. The signaling mechanism of ROS in tumor progression. Cancer Metastas-. Rev. 2006;25:695–705. PubMed
Kinnula V.L., Crapo J.D. Superoxide dismutases in malignant cells and human tumors. Free Radic. Biol. Med. 2004;36:718–744. PubMed
Crosas-Molist E., Fabregat I. Role of NADPH oxidases in the redox biology of liver fibrosis. Redox Biol. 2015;6:106–111. PubMed PMC
de Mochel N.S., Seronello S., Wang S.H., Ito C., Zheng J.X., Liang T.J., Lambeth J.D., Choi J. Hepatocyte NAD(P)H oxidases as an endogenous source of reactive oxygen species during hepatitis C virus infection. Hepatology. 2010;52:47–59. PubMed PMC
Evsev'eva A.I., Abramenko I.V., Gluzman D.F., Pisniachevskaia G.V., Filatov A.V. Immunophenotypic characteristics of lymphocytes in pleural cavity exudates. Vrachebnoe Delo. 1989:34–37. PubMed
Cui W., Matsuno K., Iwata K., Ibi M., Matsumoto M., Zhang J., Zhu K., Katsuyama M., Torok N.J., Yabe-Nishimura C. NOX1/nicotinamide adenine dinucleotide phosphate, reduced form (NADPH) oxidase promotes proliferation of stellate cells and aggravates liver fibrosis induced by bile duct ligation. Hepatology. 2011;54:949–958. PubMed
Sancho P., Martin-Sanz P., Fabregat I. Reciprocal regulation of NADPH oxidases and the cyclooxygenase-2 pathway. Free Radic. Biol. Med. 2011;51:1789–1798. PubMed
Jiang J.X., Venugopal S., Serizawa N., Chen X., Scott F., Li Y., Adamson R., Devaraj S., Shah V., Gershwin M.E., Friedman S.L., Torok N.J. Reduced nicotinamide adenine dinucleotide phosphate oxidase 2 plays a key role in stellate cell activation and liver fibrogenesis in vivo. Gastroenterology. 2010;139:1375–1384. PubMed PMC
Sancho P., Fabregat I. NADPH oxidase NOX1 controls autocrine growth of liver tumor cells through up-regulation of the epidermal growth factor receptor pathway. J. Biol. Chem. 2010;285:24815–24824. PubMed PMC
Ha S.Y., Paik Y.H., Yang J.W., Lee M.J., Bae H., Park C.K. NADPH oxidase 1 and NADPH oxidase 4 have opposite prognostic effects for patients with hepatocellular carcinoma after hepatectomy. Gut Liver. 2016;10:826–835. PubMed PMC
Jiang J.X., Chen X., Serizawa N., Szyndralewiez C., Page P., Schroder K., Brandes R.P., Devaraj S., Torok N.J. Liver fibrosis and hepatocyte apoptosis are attenuated by GKT137831, a novel NOX4/NOX1 inhibitor in vivo. Free Radic. Biol. Med. 2012;53:289–296. PubMed PMC
Jardri R., Hugdahl K., Hughes M., Brunelin J., Waters F., Alderson-Day B., Smailes D., Sterzer P., Corlett P.R., Leptourgos P., Debbane M., Cachia A., Deneve S. Are hallucinations due to an imbalance between excitatory and inhibitory influences on the brain? Schizophr. Bull. 2016;42:1124–1134. PubMed PMC
Trepanier M.O., Hopperton K.E., Mizrahi R., Mechawar N., Bazinet R.P. Postmortem evidence of cerebral inflammation in schizophrenia: a systematic review. Mol. Psychiatry. 2016;21:1009–1026. PubMed PMC
Hardingham G.E., Do K.Q. Linking early-life NMDAR hypofunction and oxidative stress in schizophrenia pathogenesis. Nat. Rev. Neurosci. 2016;17:125–134. PubMed
Gu F., Chauhan V., Chauhan A. Glutathione redox imbalance in brain disorders. Curr. Opin. Clin. Nutr. Metab. Care. 2015;18:89–95. PubMed
Steullet P., Cabungcal J.H., Kulak A., Kraftsik R., Chen Y., Dalton T.P., Cuenod M., Do K.Q. Redox dysregulation affects the ventral but not dorsal hippocampus: impairment of parvalbumin neurons, gamma oscillations, and related behaviors. J. Neurosci. 2010;30:2547–2558. PubMed PMC
Behrens M.M., Ali S.S., Dao D.N., Lucero J., Shekhtman G., Quick K.L., Dugan L.L. Ketamine-induced loss of phenotype of fast-spiking interneurons is mediated by NADPH-oxidase. Science. 2007;318:1645–1647. PubMed
Jiang Z., Rompala G.R., Zhang S., Cowell R.M., Nakazawa K. Social isolation exacerbates schizophrenia-like phenotypes via oxidative stress in cortical interneurons. Biol. Psychiatry. 2013;73:1024–1034. PubMed PMC
Lucas E.K., Markwardt S.J., Gupta S., Meador-Woodruff J.H., Lin J.D., Overstreet-Wadiche L., Cowell R.M. Parvalbumin deficiency and GABAergic dysfunction in mice lacking PGC-1alpha. J. Neurosci. 2010;30:7227–7235. PubMed PMC
Nayernia Z., Jaquet V., Krause K.H. New insights on NOX enzymes in the central nervous system. Antioxid. Redox Signal. 2014;20:2815–2837. PubMed PMC
Sorce S., Nuvolone M., Keller A., Falsig J., Varol A., Schwarz P., Bieri M., Budka H., Aguzzi A. The role of the NADPH oxidase NOX2 in prion pathogenesis. PLoS Pathog. 2014;10:e1004531. PubMed PMC
F. Vilhardt, J. Haslund-Vinding, V. Jaquet, G. McBean, Microglia antioxidant systems and redox signaling. Br. J. Pharmacol., 2016. http://dx.doi.org/10.1111/bph.13426. PubMed DOI PMC
Kopke R., Allen K.A., Henderson D., Hoffer M., Frenz D., Van de Water T. A radical demise. Toxins and trauma share common pathways in hair cell death. Ann. N. Y Acad. Sci. 1999;884:171–191. PubMed
Rousset F., Carnesecchi S., Senn P., Krause K.H. Nox3-targeted therapies for inner ear pathologies. Curr. Pharm. Des. 2015;21:5977–5987. PubMed
Paffenholz R., Bergstrom R.A., Pasutto F., Wabnitz P., Munroe R.J., Jagla W., Heinzmann U., Marquardt A., Bareiss A., Laufs J., Russ A., Stumm G., Schimenti J.C., Bergstrom D.E. Vestibular defects in head-tilt mice result from mutations in Nox3, encoding an NADPH oxidase. Genes Dev. 2004;18:486–491. PubMed PMC
Banfi B., Malgrange B., Knisz J., Steger K., Dubois-Dauphin M., Krause K.H. NOX3, a superoxide-generating NADPH oxidase of the inner ear. J. Biol. Chem. 2004;279:46065–46072. PubMed
Mukherjea D., Jajoo S., Kaur T., Sheehan K.E., Ramkumar V., Rybak L.P. Transtympanic administration of short interfering (si)RNA for the NOX3 isoform of NADPH oxidase protects against cisplatin-induced hearing loss in the rat. Antioxid. Redox Signal. 2010;13:589–598. PubMed PMC
Vasilijevic A., Buzadzic B., Korac A., Petrovic V., Jankovic A., Korac B. Beneficial effects of L-arginine nitric oxide-producing pathway in rats treated with alloxan. J. Physiol. 2007;584:921–933. PubMed PMC
Lajoix A.D., Reggio H., Chardes T., Peraldi-Roux S., Tribillac F., Roye M., Dietz S., Broca C., Manteghetti M., Ribes G., Wollheim C.B., Gross R. A neuronal isoform of nitric oxide synthase expressed in pancreatic beta-cells controls insulin secretion. Diabetes. 2001;50:1311–1323. PubMed
Jobgen W.S., Fried S.K., Fu W.J., Meininger C.J., Wu G. Regulatory role for the arginine-nitric oxide pathway in metabolism of energy substrates. J. Nutr. Biochem. 2006;17:571–588. PubMed
Petrovic V., Korac A., Buzadzic B., Korac B. The effects of L-arginine and L-NAME supplementation on redox-regulation and thermogenesis in interscapular brown adipose tissue. J. Exp. Biol. 2005;208:4263–4271. PubMed
Vasilijevic A., Vojcic L., Dinulovic I., Buzadzic B., Korac A., Petrovic V., Jankovic A., Korac B. Expression pattern of thermogenesis-related factors in interscapular brown adipose tissue of alloxan-treated rats: beneficial effect of L-arginine. Nitric Oxide. 2010;23:42–50. PubMed
Coppey L.J., Gellett J.S., Davidson E.P., Dunlap J.A., Lund D.D., Salvemini D., Yorek M.A. Effect of M40403 treatment of diabetic rats on endoneurial blood flow, motor nerve conduction velocity and vascular function of epineurial arterioles of the sciatic nerve. Br. J. Pharmacol. 2001;134:21–29. PubMed PMC
Otasevic V., Korac A., Vucetic M., Macanovic B., Garalejic E., Ivanovic-Burmazovic I., Filipovic M.R., Buzadzic B., Stancic A., Jankovic A., Velickovic K., Golic I., Markelic M., Korac B. Is manganese (II) pentaazamacrocyclic superoxide dismutase mimic beneficial for human sperm mitochondria function and motility? Antioxid. Redox Signal. 2013;18:170–178. PubMed PMC
Stancic A., Otasevic V., Jankovic A., Vucetic M., Ivanovic-Burmazovic I., Filipovic M.R., Korac A., Markelic M., Velickovic K., Golic I., Buzadzic B., Korac B. Molecular basis of hippocampal energy metabolism in diabetic rats: the effects of SOD mimic. Brain Res. Bull. 2013;99:27–33. PubMed
Hoehn K.L., Salmon A.B., Hohnen-Behrens C., Turner N., Hoy A.J., Maghzal G.J., Stocker R., Van Remmen H., Kraegen E.W., Cooney G.J., Richardson A.R., James D.E. Insulin resistance is a cellular antioxidant defense mechanism. Proc. Natl. Acad. Sci. USA. 2009;106:17787–17792. PubMed PMC
Wojdyla K., Rogowska-Wrzesinska A. Differential alkylation-based redox proteomics– lessons learnt. Redox Biol. 2015;6:240–252. PubMed PMC
Nakamura T., Tu S., Akhtar M.W., Sunico C.R., Okamoto S., Lipton S.A. Aberrant protein s-nitrosylation in neurodegenerative diseases. Neuron. 2013;78:596–614. PubMed PMC
Im H., Manolopoulou M., Malito E., Shen Y., Zhao J., Neant-Fery M., Sun C.Y., Meredith S.C., Sisodia S.S., Leissring M.A., Tang W.J. Structure of substrate-free human insulin-degrading enzyme (IDE) and biophysical analysis of ATP-induced conformational switch of IDE. J. Biol. Chem. 2007;282:25453–25463. PubMed
Durham T.B., Toth J.L., Klimkowski V.J., Cao J.X., Siesky A.M., Alexander-Chacko J., Wu G.Y., Dixon J.T., McGee J.E., Wang Y., Guo S.Y., Cavitt R.N., Schindler J., Thibodeaux S.J., Calvert N.A., Coghlan M.J., Sindelar D.K., Christe M., Kiselyov V.V., Michael M.D., Sloop K.W. Dual exosite-binding inhibitors of insulin-degrading enzyme challenge its role as the primary mediator of insulin clearance in vivo. J. Biol. Chem. 2015;290:20044–20059. PubMed PMC
Humphrey W., Dalke A., Schulten K. VMD: visual molecular dynamics. J. Mol. Graph. 1996;14(33–38):27–38. PubMed
Shen Y., Joachimiak A., Rosner M.R., Tang W.J. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Nature. 2006;443:870–874. PubMed PMC
Ralat L.A., Ren M., Schilling A.B., Tang W.J. Protective role of Cys-178 against the inactivation and oligomerization of human insulin-degrading enzyme by oxidation and nitrosylation. J. Biol. Chem. 2009;284:34005–34018. PubMed PMC
Akhtar M.W., Sanz-Blasco S., Dolatabadi N., Parker J., Chon K., Lee M.S., Soussou W., McKercher S.R., Ambasudhan R., Nakamura T., Lipton S.A. Elevated glucose and oligomeric beta-amyloid disrupt synapses via a common pathway of aberrant protein S-nitrosylation. Nat. Commun. 2016;7:10242. PubMed PMC
Cohen G., Riahi Y., Shamni O., Guichardant M., Chatgilialoglu C., Ferreri C., Kaiser N., Sasson S. Role of lipid peroxidation and PPAR-delta in amplifying glucose-stimulated insulin secretion. Diabetes. 2011;60:2830–2842. PubMed PMC
Cohen G., Shamni O., Avrahami Y., Cohen O., Broner E.C., Filippov-Levy N., Chatgilialoglu C., Ferreri C., Kaiser N., Sasson S. Beta cell response to nutrient overload involves phospholipid remodelling and lipid peroxidation. Diabetologia. 2015;58:1333–1343. PubMed
Kahremany S., Livne A., Gruzman A., Senderowitz H., Sasson S. Activation of PPARdelta: from computer modelling to biological effects. Br. J. Pharmacol. 2015;172:754–770. PubMed PMC
Maulucci G., Daniel B., Cohen O., Avrahami Y., Sasson S. Hormetic and regulatory effects of lipid peroxidation mediators in pancreatic beta cells. Mol. Asp. Med. 2016;49:49–77. PubMed
Zimniak P. 4-Hydroxynonenal and fat storage: a paradoxical pro-obesity mechanism? Cell Cycle. 2010;9:3393–3394. PubMed
Li X. SIRT1 and energy metabolism. Acta Biochim. Biophys. Sin. 2013;45:51–60. PubMed PMC
Baskaran P., Krishnan V., Ren J., Thyagarajan B. Capsaicin induces browning of white adipose tissue and counters obesity by activating TRPV1 channel-dependent mechanisms. Br. J. Pharmacol. 2016;173:2369–2389. PubMed PMC
Kanda Y., Hinata T., Kang S.W., Watanabe Y. Reactive oxygen species mediate adipocyte differentiation in mesenchymal stem cells. Life Sci. 2011;89:250–258. PubMed
Ruskovska T., Bernlohr D.A. Oxidative stress and protein carbonylation in adipose tissue – implications for insulin resistance and diabetes mellitus. J. Proteom. 2013;92:323–334. PubMed PMC
Kim S.H., Plutzky J. Brown fat and browning for the treatment of obesity and related metabolic disorders. Diabetes Metab. J. 2016;40:12–21. PubMed PMC
Chouchani E.T., Kazak L., Jedrychowski M.P., Lu G.Z., Erickson B.K., Szpyt J., Pierce K.A., Laznik-Bogoslavski D., Vetrivelan R., Clish C.B., Robinson A.J., Gygi S.P., Spiegelman B.M. Mitochondrial ROS regulate thermogenic energy expenditure and sulfenylation of UCP1. Nature. 2016;532:112–116. PubMed PMC
Schneider K., Valdez J., Nguyen J., Vawter M., Galke B., Kurtz T.W., Chan J.Y. Increased energy expenditure, Ucp1 expression, and resistance to diet-induced obesity in mice lacking nuclear factor-erythroid-2-related transcription factor-2 (Nrf2) J. Biol. Chem. 2016;291:7754–7766. PubMed PMC
Castro J.P., Grune T., Speckmann B. The two faces of reactive oxygen species (ROS) in adipocyte function and dysfunction. Biol. Chem. 2016;397:709–724. PubMed
Munzel T., Daiber A., Gori T. Nitrate therapy: new aspects concerning molecular action and tolerance. Circulation. 2011;123:2132–2144. PubMed
Daiber A., Munzel T. Organic nitrate therapy, nitrate tolerance, and nitrate-induced endothelial dysfunction: emphasis on redox biology and oxidative stress. Antioxid. Redox Signal. 2015;23:899–942. PubMed PMC
Munzel T., Daiber A., Gori T. More answers to the still unresolved question of nitrate tolerance. Eur. Heart J. 2013;34:2666–2673. PubMed
Daiber A., Oelze M., Sulyok S., Coldewey M., Schulz E., Treiber N., Hink U., Mulsch A., Scharffetter-Kochanek K., Munzel T. Heterozygous deficiency of manganese superoxide dismutase in mice (Mn-SOD+/-): a novel approach to assess the role of oxidative stress for the development of nitrate tolerance. Mol. Pharmacol. 2005;68:579–588. PubMed
Esplugues J.V., Rocha M., Nunez C., Bosca I., Ibiza S., Herance J.R., Ortega A., Serrador J.M., D'Ocon P., Victor V.M. Complex I dysfunction and tolerance to nitroglycerin: an approach based on mitochondrial-targeted antioxidants. Circ. Res. 2006;99:1067–1075. PubMed
Munzel T., Kurz S., Rajagopalan S., Tarpey M., Freeman B., Harrison D.G. Identification of the membrane bound NADH oxidase as the major source of superoxide anion in nitrate tolerance. Endothelium. 1995;3(Suppl):s14. (abstract)
Jabs A., Oelze M., Mikhed Y., Stamm P., Kroller-Schon S., Welschof P., Jansen T., Hausding M., Kopp M., Steven S., Schulz E., Stasch J.P., Munzel T., Daiber A. Effect of soluble guanylyl cyclase activator and stimulator therapy on nitroglycerin-induced nitrate tolerance in rats. Vasc. Pharmacol. 2015;71:181–191. PubMed
Daiber A., Oelze M., Coldewey M., Kaiser K., Huth C., Schildknecht S., Bachschmid M., Nazirisadeh Y., Ullrich V., Mulsch A., Munzel T., Tsilimingas N. Hydralazine is a powerful inhibitor of peroxynitrite formation as a possible explanation for its beneficial effects on prognosis in patients with congestive heart failure. Biochem. Biophys. Res. Commun. 2005;338:1865–1874. PubMed
Chen Z., Zhang J., Stamler J.S. Identification of the enzymatic mechanism of nitroglycerin bioactivation. Proc. Natl. Acad. Sci. USA. 2002;99:8306–8311. PubMed PMC
Wenzel P., Hink U., Oelze M., Schuppan S., Schaeuble K., Schildknecht S., Ho K.K., Weiner H., Bachschmid M., Munzel T., Daiber A. Role of reduced lipoic acid in the redox regulation of mitochondrial aldehyde dehydrogenase (ALDH-2) activity. Implications for mitochondrial oxidative stress and nitrate tolerance. J. Biol. Chem. 2007;282:792–799. PubMed
Schulz E., Tsilimingas N., Rinze R., Reiter B., Wendt M., Oelze M., Woelken-Weckmuller S., Walter U., Reichenspurner H., Meinertz T., Munzel T. Functional and biochemical analysis of endothelial (dys)function and NO/cGMP signaling in human blood vessels with and without nitroglycerin pretreatment. Circulation. 2002;105:1170–1175. PubMed
Andreassi M.G., Botto N., Simi S., Casella M., Manfredi S., Lucarelli M., Venneri L., Biagini A., Picano E. Diabetes and chronic nitrate therapy as co-determinants of somatic DNA damage in patients with coronary artery disease. J. Mol. Med. 2005;83:279–286. PubMed
Mikhed Y., Fahrer J., Oelze M., Kroller-Schon S., Steven S., Welschof P., Zinssius E., Stamm P., Kashani F., Roohani S., Kress J.M., Ullmann E., Tran L.P., Schulz E., Epe B., Kaina B., Munzel T., Daiber A. Nitroglycerin induces DNA damage and vascular cell death in the setting of nitrate tolerance. Basic Res. Cardiol. 2016;111:52. PubMed
Oelze M., Knorr M., Kroller-Schon S., Kossmann S., Gottschlich A., Rummler R., Schuff A., Daub S., Doppler C., Kleinert H., Gori T., Daiber A., Munzel T. Chronic therapy with isosorbide-5-mononitrate causes endothelial dysfunction, oxidative stress, and a marked increase in vascular endothelin-1 expression. Eur Heart J. 2013;34:3206–3216. PubMed
Oberle S., Abate A., Grosser N., Vreman H.J., Dennery P.A., Schneider H.T., Stalleicken D., Schroder H. Heme oxygenase-1 induction may explain the antioxidant profile of pentaerythrityl trinitrate. Biochem. Biophys. Res. Commun. 2002;290:1539–1544. PubMed
Oppermann M., Balz V., Adams V., Dao V.T., Bas M., Suvorava T., Kojda G. Pharmacological induction of vascular extracellular superoxide dismutase expression in vivo. J. Cell. Mol. Med. 2009;13:1271–1278. PubMed PMC
Pautz A., Rauschkolb P., Schmidt N., Art J., Oelze M., Wenzel P., Forstermann U., Daiber A., Kleinert H. Effects of nitroglycerin or pentaerithrityl tetranitrate treatment on the gene expression in rat hearts: evidence for cardiotoxic and cardioprotective effects. Physiol. Genom. 2009;38:176–185. PubMed
Wu Z., Siuda D., Xia N., Reifenberg G., Daiber A., Munzel T., Forstermann U., Li H. Maternal treatment of spontaneously hypertensive rats with pentaerythritol tetranitrate reduces blood pressure in female offspring. Hypertension. 2015;65:232–237. PubMed
Gamboa J.L., Billings F.T. t., Bojanowski M.T., Gilliam L.A., Yu C., Roshanravan B., Roberts L.J., 2nd, Himmelfarb J., Ikizler T.A., Brown N.J. Mitochondrial dysfunction and oxidative stress in patients with chronic kidney disease. Physiol. Rep. 2016;4 PubMed PMC
Makino A., Skelton M.M., Zou A.P., Roman R.J., Cowley A.W., Jr. Increased renal medullary oxidative stress produces hypertension. Hypertension. 2002;39:667–672. PubMed
Sindhu R.K., Ehdaie A., Farmand F., Dhaliwal K.K., Nguyen T., Zhan C.D., Roberts C.K., Vaziri N.D. Expression of catalase and glutathione peroxidase in renal insufficiency. Biochim. Biophys. Acta. 2005;1743:86–92. PubMed
Vaziri N.D., Dicus M., Ho N.D., Boroujerdi-Rad L., Sindhu R.K. Oxidative stress and dysregulation of superoxide dismutase and NADPH oxidase in renal insufficiency. Kidney Int. 2003;63:179–185. PubMed
Schnackenberg C.G., Wilcox C.S. Two-week administration of tempol attenuates both hypertension and renal excretion of 8-Iso prostaglandin f2alpha. Hypertension. 1999;33:424–428. PubMed
de Richelieu L.T., Sorensen C.M., Holstein-Rathlou N.H., Salomonsson M. NO-independent mechanism mediates tempol-induced renal vasodilation in SHR. Am. J. Physiol. Ren. Physiol. 2005;289:F1227–F1234. PubMed
Guron G.S., Grimberg E.S., Basu S., Herlitz H. Acute effects of the superoxide dismutase mimetic tempol on split kidney function in two-kidney one-clip hypertensive rats. J. Hypertens. 2006;24:387–394. PubMed
Papazova D.A., van Koppen A., Koeners M.P., Bleys R.L., Verhaar M.C., Joles J.A. Maintenance of hypertensive hemodynamics does not depend on ROS in established experimental chronic kidney disease. PLoS One. 2014;9:e88596. PubMed PMC
Herget J., Wilhelm J., Novotna J., Eckhardt A., Vytasek R., Mrazkova L., Ostadal M. A possible role of the oxidant tissue injury in the development of hypoxic pulmonary hypertension. Physiol. Res. 2000;49:493–501. PubMed
Hansen T., Galougahi K.K., Celermajer D., Rasko N., Tang O., Bubb K.J., Figtree G. Oxidative and nitrosative signalling in pulmonary arterial hypertension – implications for development of novel therapies. Pharmacol. Ther. 2016;165:50–62. PubMed
Hodyc D., Johnson E., Skoumalova A., Tkaczyk J., Maxova H., Vizek M., Herget J. Reactive oxygen species production in the early and later stage of chronic ventilatory hypoxia. Physiol. Res. 2012;61:145–151. PubMed
Jakoubek V., Bibova J., Herget J., Hampl V. Chronic hypoxia increases fetoplacental vascular resistance and vasoconstrictor reactivity in the rat. Am. J. Physiol. Heart Circ. Physiol. 2008;294:H1638–H1644. PubMed
Gao B., Doan A., Hybertson B.M. The clinical potential of influencing Nrf2 signaling in degenerative and immunological disorders. Clin. Pharmacol. 2014;6:19–34. PubMed PMC
O'Brien E., Dietrich D.R. Ochratoxin A: the continuing enigma. Crit. Rev. Toxicol. 2005;35:33–60. PubMed
Pfohl-Leszkowicz A., Manderville R.A. Ochratoxin A: an overview on toxicity and carcinogenicity in animals and humans. Mol. Nutr. Food Res. 2007;51:61–99. PubMed
Ringot D., Chango A., Schneider Y.J., Larondelle Y. Toxicokinetics and toxicodynamics of ochratoxin A, an update. Chem. Biol. Interact. 2006;159:18–46. PubMed
Schaaf G.J., Nijmeijer S.M., Maas R.F., Roestenberg P., de Groene E.M., Fink-Gremmels J. The role of oxidative stress in the ochratoxin A-mediated toxicity in proximal tubular cells. Biochim. Biophys. Acta. 2002;1588:149–158. PubMed
Costa J.G., Saraiva N., Guerreiro P.S., Louro H., Silva M.J., Miranda J.P., Castro M., Batinic-Haberle I., Fernandes A.S., Oliveira N.G. Ochratoxin A-induced cytotoxicity, genotoxicity and reactive oxygen species in kidney cells: an integrative approach of complementary endpoints. Food Chem. Toxicol. 2016;87:65–76. PubMed
Marin-Kuan M., Ehrlich V., Delatour T., Cavin C., Schilter B. Evidence for a role of oxidative stress in the carcinogenicity of ochratoxin a. J. Toxicol. 2011;2011:645361. PubMed PMC
Pfohl-Leszkowicz A., Manderville R.A. An update on direct genotoxicity as a molecular mechanism of ochratoxin a carcinogenicity. Chem. Res. Toxicol. 2012;25:252–262. PubMed
Cavin C., Delatour T., Marin-Kuan M., Fenaille F., Holzhauser D., Guignard G., Bezencon C., Piguet D., Parisod V., Richoz-Payot J., Schilter B. Ochratoxin A-mediated DNA and protein damage: roles of nitrosative and oxidative stresses. Toxicol. Sci. 2009;110:84–94. PubMed
Sorrenti V., Di Giacomo C., Acquaviva R., Barbagallo I., Bognanno M., Galvano F. Toxicity of ochratoxin a and its modulation by antioxidants: a review. Toxins. 2013;5:1742–1766. PubMed PMC
Newton G.L., Buchmeier N., Fahey R.C. Biosynthesis and functions of mycothiol, the unique protective thiol of actinobacteria. Microbiol. Mol. Biol. Rev. 2008;72:471–494. PubMed PMC
Van Laer K., Hamilton C.J., Messens J. Low-molecular-weight thiols in thiol-disulfide exchange. Antioxid. Redox Signal. 2013;18:1642–1653. PubMed
Van Laer K., Buts L., Foloppe N., Vertommen D., Van Belle K., Wahni K., Roos G., Nilsson L., Mateos L.M., Rawat M., van Nuland N.A., Messens J. Mycoredoxin-1 is one of the missing links in the oxidative stress defence mechanism of Mycobacteria. Mol. Microbiol. 2012;86:787–804. PubMed
Hugo M., Van Laer K., Reyes A.M., Vertommen D., Messens J., Radi R., Trujillo M. Mycothiol/mycoredoxin 1-dependent reduction of the peroxiredoxin AhpE from Mycobacterium tuberculosis. J. Biol. Chem. 2014;289:5228–5239. PubMed PMC
Chacinska A., Pfannschmidt S., Wiedemann N., Kozjak V., Sanjuan Szklarz L.K., Schulze-Specking A., Truscott K.N., Guiard B., Meisinger C., Pfanner N. Essential role of Mia40 in import and assembly of mitochondrial intermembrane space proteins. EMBO J. 2004;23:3735–3746. PubMed PMC
Herrmann J.M., Riemer J. Mitochondrial disulfide relay: redox-regulated protein import into the intermembrane space. J. Biol. Chem. 2012;287:4426–4433. PubMed PMC
Naoe M., Ohwa Y., Ishikawa D., Ohshima C., Nishikawa S., Yamamoto H., Endo T. Identification of Tim40 that mediates protein sorting to the mitochondrial intermembrane space. J. Biol. Chem. 2004;279:47815–47821. PubMed
Sideris D.P., Petrakis N., Katrakili N., Mikropoulou D., Gallo A., Ciofi-Baffoni S., Banci L., Bertini I., Tokatlidis K. A novel intermembrane space-targeting signal docks cysteines onto Mia40 during mitochondrial oxidative folding. J. Cell Biol. 2009;187:1007–1022. PubMed PMC
Bien M., Longen S., Wagener N., Chwalla I., Herrmann J.M., Riemer J. Mitochondrial disulfide bond formation is driven by intersubunit electron transfer in Erv1 and proofread by glutathione. Mol. Cell. 2010;37:516–528. PubMed
Vogtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J., Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C. Intermembrane space proteome of yeast mitochondria. Mol. Cell Proteom. 2012;11:1840–1852. PubMed PMC
Banci L., Bertini I., Cefaro C., Ciofi-Baffoni S., Gallo A., Martinelli M., Sideris D.P., Katrakili N., Tokatlidis K. MIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondria. Nat. Struct. Mol. Biol. 2009;16:198–206. PubMed
Milkovic L., Siems W., Siems R., Zarkovic N. Oxidative stress and antioxidants in carcinogenesis and integrative therapy of cancer. Curr. Pharm. Des. 2014;20:6529–6542. PubMed
Stepanic V., Gasparovic A.C., Troselj K.G., Amic D., Zarkovic N. Selected attributes of polyphenols in targeting oxidative stress in cancer. Curr. Top. Med. Chem. 2015;15:496–509. PubMed
Laurent A., Nicco C., Chereau C., Goulvestre C., Alexandre J., Alves A., Levy E., Goldwasser F., Panis Y., Soubrane O., Weill B., Batteux F. Controlling tumor growth by modulating endogenous production of reactive oxygen species. Cancer Res. 2005;65:948–956. PubMed
Holley A.K., Miao L., St Clair D.K., St Clair W.H. Redox-modulated phenomena and radiation therapy: the central role of superoxide dismutases. Antioxid. Redox Signal. 2014;20:1567–1589. PubMed PMC
Konzack A., Jakupovic M., Kubaichuk K., Gorlach A., Dombrowski F., Miinalainen I., Sormunen R., Kietzmann T. Mitochondrial dysfunction due to lack of manganese superoxide dismutase promotes hepatocarcinogenesis. Antioxid. Redox Signal. 2015;23:1059–1075. PubMed PMC
Zhang X.F., Tan X., Zeng G., Misse A., Singh S., Kim Y., Klaunig J.E., Monga S.P. Conditional beta-catenin loss in mice promotes chemical hepatocarcinogenesis: role of oxidative stress and platelet-derived growth factor receptor alpha/phosphoinositide 3-kinase signaling. Hepatology. 2010;52:954–965. PubMed PMC
Hayes J.D., Dinkova-Kostova A.T. The Nrf2 regulatory network provides an interface between redox and intermediary metabolism. Trends Biochem. Sci. 2014;39:199–218. PubMed
Rushmore T.H., Morton M.R., Pickett C.B. The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity. J. Biol. Chem. 1991;266:11632–11639. PubMed
Muscoli C., Cuzzocrea S., Riley D.P., Zweier J.L., Thiemermann C., Wang Z.Q., Salvemini D. On the selectivity of superoxide dismutase mimetics and its importance in pharmacological studies. Br. J. Pharmacol. 2003;140:445–460. PubMed PMC
Iranzo O. Manganese complexes displaying superoxide dismutase activity: a balance between different factors. Bioorg. Chem. 2011;39:73–87. PubMed
Batinic-Haberle I., Reboucas J.S., Spasojevic I. Superoxide dismutase mimics: chemistry, pharmacology, and therapeutic potential. Antioxid. Redox Signal. 2010;13:877–918. PubMed PMC
Batinic-Haberle I., Tovmasyan A., Spasojevic I. An educational overview of the chemistry, biochemistry and therapeutic aspects of Mn porphyrins – from superoxide dismutation to H2O2-driven pathways. Redox Biol. 2015;5:43–65. PubMed PMC
Fernandes A.S., Costa J., Gaspar J., Rueff J., Cabral M.F., Cipriano M., Castro M., Oliveira N.G. Development of pyridine-containing macrocyclic copper(II) complexes: potential role in the redox modulation of oxaliplatin toxicity in human breast cells. Free Radic. Res. 2012;46:1157–1166. PubMed
Wondrak G.T. Redox-directed cancer therapeutics: molecular mechanisms and opportunities. Antioxid. Redox Signal. 2009;11:3013–3069. PubMed PMC
Batinic-Haberle I., Tovmasyan A., Roberts E.R., Vujaskovic Z., Leong K.W., Spasojevic I. SOD therapeutics: latest insights into their structure-activity relationships and impact on the cellular redox-based signaling pathways. Antioxid. Redox Signal. 2014;20:2372–2415. PubMed PMC
Gorrini C., Harris I.S., Mak T.W. Modulation of oxidative stress as an anticancer strategy. Nat. Rev. Drug Discov. 2013;12:931–947. PubMed
Lu M.C., Ji J.A., Jiang Z.Y., You Q.D. The Keap1-Nrf2-ARE pathway as a potential preventive and therapeutic target: an update. Med. Res. Rev. 2016;36:924–963. PubMed
Voskou S., Aslan M., Fanis P., Phylactides M., Kleanthous M. Oxidative stress in beta-thalassaemia and sickle cell disease. Redox Biol. 2015;6:226–239. PubMed PMC
Yanpanitch O.U., Hatairaktham S., Charoensakdi R., Panichkul N., Fucharoen S., Srichairatanakool S., Siritanaratkul N., Kalpravidh R.W. Treatment of beta-thalassemia/hemoglobin E with antioxidant cocktails results in decreased oxidative stress, increased hemoglobin concentration, and improvement of the hypercoagulable state. Oxid. Med. Cell. Longev. 2015;2015:537954. PubMed PMC
Ozdemir Z.C., Koc A., Aycicek A., Kocyigit A. N-Acetylcysteine supplementation reduces oxidative stress and DNA damage in children with beta-thalassemia. Hemoglobin. 2014;38:359–364. PubMed
Pfeifer W.P., Degasperi G.R., Almeida M.T., Vercesi A.E., Costa F.F., Saad S.T. Vitamin E supplementation reduces oxidative stress in beta thalassaemia intermedia. Acta Haematol. 2008;120:225–231. PubMed
Tesoriere L., D'Arpa D., Butera D., Allegra M., Renda D., Maggio A., Bongiorno A., Livrea M.A. Oral supplements of vitamin E improve measures of oxidative stress in plasma and reduce oxidative damage to LDL and erythrocytes in beta-thalassemia intermedia patients. Free Radic. Res. 2001;34:529–540. PubMed
Franco S.S., De Falco L., Ghaffari S., Brugnara C., Sinclair D.A., Matte A., Iolascon A., Mohandas N., Bertoldi M., An X., Siciliano A., Rimmele P., Cappellini M.D., Michan S., Zoratti E., Anne J., De Franceschi L. Resveratrol accelerates erythroid maturation by activation of FoxO3 and ameliorates anemia in beta-thalassemic mice. Haematologica. 2014;99:267–275. PubMed PMC
Kalpravidh R.W., Siritanaratkul N., Insain P., Charoensakdi R., Panichkul N., Hatairaktham S., Srichairatanakool S., Phisalaphong C., Rachmilewitz E., Fucharoen S. Improvement in oxidative stress and antioxidant parameters in beta-thalassemia/Hb E patients treated with curcuminoids. Clin. Biochem. 2010;43:424–429. PubMed
Kalpravidh R.W., Wichit A., Siritanaratkul N., Fucharoen S. Effect of coenzyme Q10 as an antioxidant in beta-thalassemia/Hb E patients. Biofactors. 2005;25:225–234. PubMed
Ounjaijean S., Thephinlap C., Khansuwan U., Phisalapong C., Fucharoen S., Porter J.B., Srichairatanakool S. Effect of green tea on iron status and oxidative stress in iron-loaded rats. Med. Chem. 2008;4:365–370. PubMed
Fibach E., Tan E.S., Jamuar S., Ng I., Amer J., Rachmilewitz E.A. Amelioration of oxidative stress in red blood cells from patients with beta-thalassemia major and intermedia and E-beta-thalassemia following administration of a fermented papaya preparation. Phytother. Res. 2010;24:1334–1338. PubMed
Darvishi Khezri H., Salehifar E., Kosaryan M., Aliasgharian A., Jalali H., Hadian Amree A. Potential effects of silymarin and its flavonolignan components in patients with beta-thalassemia major: a comprehensive review in 2015. Adv. Pharmacol. Sci. 2016;2016:3046373. PubMed PMC
Alidoost F., Gharagozloo M., Bagherpour B., Jafarian A., Sajjadi S.E., Hourfar H., Moayedi B. Effects of silymarin on the proliferation and glutathione levels of peripheral blood mononuclear cells from beta-thalassemia major patients. Int. Immunopharmacol. 2006;6:1305–1310. PubMed
Biedermann D., Vavrikova E., Cvak L., Kren V. Chemistry of silybin. Nat. Prod. Rep. 2014;31:1138–1157. PubMed
Surai P.F. Silymarin as a natural antioxidant: an overview of the current evidence and perspectives. Antioxidants. 2015;4:204–247. PubMed PMC
Pliskova M., Vondracek J., Kren V., Gazak R., Sedmera P., Walterova D., Psotova J., Simanek V., Machala M. Effects of silymarin flavonolignans and synthetic silybin derivatives on estrogen and aryl hydrocarbon receptor activation. Toxicology. 2005;215:80–89. PubMed
Zheng N., Zhang P., Huang H., Liu W., Hayashi T., Zang L., Zhang Y., Liu L., Xia M., Tashiro S., Onodera S., Ikejima T. ERalpha down-regulation plays a key role in silibinin-induced autophagy and apoptosis in human breast cancer MCF-7 cells. J. Pharmacol. Sci. 2015;128:97–107. PubMed
Sadava D., Kane S.E. Silibinin reverses drug resistance in human small-cell lung carcinoma cells. Cancer Lett. 2013;339:102–106. PubMed PMC
Agarwal R., Agarwal C., Ichikawa H., Singh R.P., Aggarwal B.B. Anticancer potential of silymarin: from bench to bed side. Anticancer Res. 2006;26:4457–4498. PubMed
Hager H. [Problems in the treatment of ocular circulatory disturbances (author's transl)] Klin. Monbl Augenheilkd. 1974;165:127–136. PubMed
Garcia J., Carvalho A.T., Dourado D.F., Baptista P., de Lourdes Bastos M., Carvalho F. New in silico insights into the inhibition of RNAP II by alpha-amanitin and the protective effect mediated by effective antidotes. J. Mol. Graph. Model. 2014;51:120–127. PubMed
Senkiv J., Finiuk N., Kaminskyy D., Havrylyuk D., Wojtyra M., Kril I., Gzella A., Stoika R., Lesyk R. 5-Ene-4-thiazolidinones induce apoptosis in mammalian leukemia cells. Eur. J. Med Chem. 2016;117:33–46. PubMed
Yelisyeyeva O.P., Semen K.O., Ostrovska G.V., Kaminskyy D.V., Sirota T.V., Zarkovic N., Mazur D., Lutsyk O.D., Rybalchenko K., Bast A. The effect of Amaranth oil on monolayers of artificial lipids and hepatocyte plasma membranes with adrenalin-induced stress. Food Chem. 2014;147:152–159. PubMed
Bast A., Haenen G.R. Ten misconceptions about antioxidants. Trends Pharmacol. Sci. 2013;34:430–436. PubMed
Hirano K., Chen W.S., Chueng A.L., Dunne A.A., Seredenina T., Filippova A., Ramachandran S., Bridges A., Chaudry L., Pettman G., Allan C., Duncan S., Lee K.C., Lim J., Ma M.T., Ong A.B., Ye N.Y., Nasir S., Mulyanidewi S., Aw C.C., Oon P.P., Liao S., Li D., Johns D.G., Miller N.D., Davies C.H., Browne E.R., Matsuoka Y., Chen D.W., Jaquet V., Rutter A.R. Discovery of GSK2795039, a novel small molecule NADPH oxidase 2 inhibitor. Antioxid. Redox Signal. 2015;23:358–374. PubMed PMC
Maghzal G.J., Krause K.H., Stocker R., Jaquet V. Detection of reactive oxygen species derived from the family of NOX NADPH oxidases. Free Radic. Biol. Med. 2012;53:1903–1918. PubMed
Kalyanaraman B., Dranka B.P., Hardy M., Michalski R., Zielonka J. HPLC-based monitoring of products formed from hydroethidine-based fluorogenic probes--the ultimate approach for intra- and extracellular superoxide detection. Biochim. Biophys. Acta. 2014;1840:739–744. PubMed PMC
Seredenina T., Nayernia Z., Sorce S., Maghzal G.J., Filippova A., Ling S.C., Basset O., Plastre O., Daali Y., Rushing E.J., Giordana M.T., Cleveland D.W., Aguzzi A., Stocker R., Krause K.H., Jaquet V. Evaluation of NADPH oxidases as drug targets in a mouse model of familial amyotrophic lateral sclerosis. Free Radic. Biol. Med. 2016;97:95–108. PubMed
Talib J., Maghzal G.J., Cheng D., Stocker R. Detailed protocol to assess in vivo and ex vivo myeloperoxidase activity in mouse models of vascular inflammation and disease using hydroethidine. Free Radic. Biol. Med. 2016;97:124–135. PubMed
Fujikawa Y., Roma L.P., Sobotta M.C., Rose A.J., Diaz M.B., Locatelli G., Breckwoldt M.O., Misgeld T., Kerschensteiner M., Herzig S., Muller-Decker K., Dick T.P. Mouse redox histology using genetically encoded probes. Sci. Signal. 2016;9:rs1. PubMed
Alam M.N., Bristi N.J., Rafiquzzaman M. Review on in vivo and in vitro methods evaluation of antioxidant activity. Saudi Pharm. J. 2013;21:143–152. PubMed PMC
Agudo A., Cabrera L., Amiano P., Ardanaz E., Barricarte A., Berenguer T., Chirlaque M.D., Dorronsoro M., Jakszyn P., Larranaga N., Martinez C., Navarro C., Quiros J.R., Sanchez M.J., Tormo M.J., Gonzalez C.A. Fruit and vegetable intakes, dietary antioxidant nutrients, and total mortality in Spanish adults: findings from the Spanish cohort of the European prospective investigation into cancer and nutrition (EPIC-Spain) Am. J. Clin. Nutr. 2007;85:1634–1642. PubMed
Sies H., Berndt C., Jones D.P. Oxidative Stress. Ann. Rev. Biochem. 2017 PubMed
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