Molecular Mechanisms Underlying Intensive Care Unit-Acquired Weakness and Sarcopenia

. 2022 Jul 29 ; 23 (15) : . [epub] 20220729

Jazyk angličtina Země Švýcarsko Médium electronic

Typ dokumentu časopisecké články, přehledy

Perzistentní odkaz   https://www.medvik.cz/link/pmid35955530

Skeletal muscle is a highly adaptable organ, and its amount declines under catabolic conditions such as critical illness. Aging is accompanied by a gradual loss of muscle, especially when physical activity decreases. Intensive care unit-acquired weakness is a common and highly serious neuromuscular complication in critically ill patients. It is a consequence of critical illness and is characterized by a systemic inflammatory response, leading to metabolic stress, that causes the development of multiple organ dysfunction. Muscle dysfunction is an important component of this syndrome, and the degree of catabolism corresponds to the severity of the condition. The population of critically ill is aging; thus, we face another negative effect-sarcopenia-the age-related decline of skeletal muscle mass and function. Low-grade inflammation gradually accumulates over time, inhibits proteosynthesis, worsens anabolic resistance, and increases insulin resistance. The cumulative consequence is a gradual decline in muscle recovery and muscle mass. The clinical manifestation for both of the above conditions is skeletal muscle weakness, with macromolecular damage, and a common mechanism-mitochondrial dysfunction. In this review, we compare the molecular mechanisms underlying the two types of muscle atrophy, and address questions regarding possible shared molecular mechanisms, and whether critical illness accelerates the aging process.

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Kress J.P., Hall J.B. ICU-acquired weakness and recovery from critical illness. N. Eng. J. Med. 2014;370:17. doi: 10.1056/NEJMra1209390. PubMed DOI

Schefold J.C., Wollersheim T., Grunow J.J., Luedi M.M., Z’Graggen W.J., Weber-Carstens S. Muscular weakness and muscle wasting in the critically ill. J. Cachexia Sarcopenia Muscle. 2020;11:1399–1412. doi: 10.1002/jcsm.12620. PubMed DOI PMC

Wang W., Xu C., Ma X., Zhang X., Xie P. Intensive Care Unit-acquired weakness: A review of recent progress with a look toward the future. Front. Med. 2020;7:559789. doi: 10.3389/fmed.2020.559789. PubMed DOI PMC

Lad H., Saumur T.M., Herridge M.S., Cdos Santos C., Mathur S., Batt J., Gilbert P.M. Intensive Care Unit-Acquired Weakness: Not just another muscle atrophying condition. Int. J. Mol. Sci. 2020;21:7840. doi: 10.3390/ijms21217840. PubMed DOI PMC

Hawkins R.B., Raymond S.L., Stortz J.A., Hiroyuki H., Brakenridge S.C., Gardner A., Efron P.A., Bihorac A., Segal M., Moore F.A., et al. Chronic critical illness and Persistent Inflammation, Immunosuppression and catabolism syndrome. Front. Immunol. 2018;9:1511. doi: 10.3389/fimmu.2018.01511. PubMed DOI PMC

Cruz-Jentoft A.J., Bahat G., Bauer J., Boirie Y., Bruyère O., Cederholm T., Cooper C., Landi F., Rolland Y., Sayer A.A., et al. Writing Group for the European Working Group on Sarcopenia in Older People 2 (EWGSOP2), and the Extended Group for EWGSOP2. Sarcopenia: Revised European consensus on definition and diagnosis. Age Ageing. 2019;48:601. doi: 10.1093/ageing/afz046. PubMed DOI PMC

Kizilarslanoglu M.C., Kuyumcu M.E., Yesil Y., Halil M. Sarcopenia in critically ill patients. J. Anesth. 2016;30:884–890. doi: 10.1007/s00540-016-2211-4. PubMed DOI

Hoffmann C., Weigert C. Skeletal Muscle as an endocrine organ: The role of myokines in exercise adaptations. Cold Spring Harb. Perspect. Med. 2017;7:a029793. doi: 10.1101/cshperspect.a029793. PubMed DOI PMC

Ottens F., Franz A., Hoppe T. Build-UPS and break-downs: Metabolism impacts on proteostasis and aging. Cell Death Differ. 2021;28:505–521. doi: 10.1038/s41418-020-00682-y. PubMed DOI PMC

Flick K., Kaiser P. Protein degradation and the stress response. Semin. Cell Dev. Biol. 2012;23:515–522. doi: 10.1016/j.semcdb.2012.01.019. PubMed DOI PMC

Dillon E.L. Nutritionally essential amino acids and metabolic signaling in aging. Amino Acids. 2013;45:431–441. doi: 10.1007/s00726-012-1438-0. PubMed DOI PMC

Preiser J.C., Ichai C., Orban J.C., Groeneveld A.B.J. Metabolic response to stress of critical illness. BJA. 2014;113:945–954. doi: 10.1093/bja/aeu187. PubMed DOI

Bloch S., Polkey M.I., Griffiths M., Kemp P. Molecular mechanisms of intensive care unit-acquired weakness. Eur. Respir. J. 2012;39:1000–1011. doi: 10.1183/09031936.00090011. PubMed DOI

Hermans G., Van den Berge G. Clinical review: Intensive care unit acquired weakness. Critical Care. 2015;19:274. doi: 10.1186/s13054-015-0993-7. PubMed DOI PMC

Marshall R.S., Vierstra R.D. Dynamic regulation of the 26S proteasome: From synthesis to degradation. Front. Mol. Biosci. 2019;6:40. doi: 10.3389/fmolb.2019.00040. PubMed DOI PMC

Wray C.J., Mammen J.M., Hershko D.D., Hasselgren P.-O. Sepsis upregulates the gene expression of multiple ubiquitin ligases in skeletal muscle. Int. J. Biochem Cell Biol. 2003;35:698–705. doi: 10.1016/S1357-2725(02)00341-2. PubMed DOI

Klaude M., Fredriksson K., Tjader I., Hammarqvist F., Ahlman B., Rooyackers O., Wernerman J. Proteasome proteolytic activity in skeletal muscle is increased in patients with sepsis. Clin. Sci. 2007;112:499–506. doi: 10.1042/CS20060265. PubMed DOI

Marshall R.S., Vierstra R.D. Eat or be eaten: The autophagic plight of inactive 26S proteasomes. Autophagy. 2015;11:1927–1928. doi: 10.1080/15548627.2015.1078961. PubMed DOI PMC

Du J., Hu Z., Mitch W.E. Molecular mechanisms activating muscle protein degradation in chronic kidney disease and other catabolic conditions. Eur. J. Clin. Investig. 2005;35:157–163. doi: 10.1111/j.1365-2362.2005.01473.x. PubMed DOI

Zhao J., Zhai B., Gygi S.P., Godberg L. mTOR inhibition activates overall protein degradation by the ubiquitin proteasome system as well as by autophagy. Proc. Natl. Acad. Sci. USA. 2015;112:15790–15796. doi: 10.1073/pnas.1521919112. PubMed DOI PMC

Zhao J., Goldberg A.L. Coordinate regulation of autophagy and the ubiquitin proteasome system by mTOR. Autophagy. 2016;12:1967–1970. doi: 10.1080/15548627.2016.1205770. PubMed DOI PMC

Folleta V.C., White L.J., Larsen A.E., Léger B., Russel A.P. The role and regulation of MAFbx/atrogin-1 and MuRF1 in skeletal muscle atrophy. Eur. J. Physiol. 2011;461:325–335. doi: 10.1007/s00424-010-0919-9. PubMed DOI

Combaret L., Taillandier D., Darvedet D., Bechet D., Rallière C., Claustre A., Grizard J., Attaix D. Glucocorticoids regulate mRNA levels for subunits of the 19 S regulatory complex of the 26 S proteasome in fast-twitch skeletal muscle. Biochem. J. 2004;378:239–246. doi: 10.1042/bj20031660. PubMed DOI PMC

Lang C.H., Frost R.A. Sepsis-induced suppression of skeletal muscle translation initiation mediated byx tumor necrosis factorα. Curr. Opin. Clin. Nutr. Metab. Care. 2006;9:185–189. PubMed

Showkat M., Beigh M.A., Andrabi K.I. mTOR signaling in protein translation regulation: Implications in cancer genesis and therapeutic interventions. Mol. Biol. Int. 2014;2014:686984. doi: 10.1155/2014/686984. PubMed DOI PMC

Tan V.P., Miyamoto S. Nutrient-sensing mTORC1: Integration of metabolic and autophagic signals. J. Mol. Cell Cardiol. 2016;95:31–41. doi: 10.1016/j.yjmcc.2016.01.005. PubMed DOI PMC

Zink W., Kaess M., Hofer S., Plachky J., Zausig Y.A., Sinner B., Weigand M.A., Fink R.H., Graf B.M. Alteration in intracellular Ca2+ homeostasis of skeletal muscle fibers during sepsis. Crit. Care Med. 2008;36:1559–1563. doi: 10.1097/CCM.0b013e318170aa97. PubMed DOI

Clark M.G., Rattigan S., Barrett E.J. Nutritive blood flow as and essential element supporting muscle anabolism. Curr. Opin. Clin. Nutr. Metab. Care. 2006;9:185–189. doi: 10.1097/01.mco.0000222097.90890.c2. PubMed DOI

Friedrich O., Hund E., Weber C., Hacke W., Fink R.H.A. Critical illness myopathy serum fractions affect membrane excitability and intracellular calcium release in mammalian skeletal muscle. J. Neurol. 2004;251:53–65. doi: 10.1007/s00415-004-0272-z. PubMed DOI

Khan J., Harrison T., Rich M. Mechanisms of neuromuscular dysfunction in critical illness. Crit. Care Clin. 2008;24:165–177. doi: 10.1016/j.ccc.2007.10.004. PubMed DOI PMC

Z’Graggen W.J., Lin C.S.Y., Howard R.S., Beale R.J., Bostock H. Nerve excitability changes in critical illness polyneuromyopathy. Brain. 2006;129:2461–2470. doi: 10.1093/brain/awl191. PubMed DOI

Wu J., Yao Y.M., Lu Z.Q. Mitochondrial quality control mechanisms as potential therapeutic targets in sepsis-induced multiple organ failure. J. Mol. Med. 2019;97:451–462. doi: 10.1007/s00109-019-01756-2. PubMed DOI

Ferri E., Marzetti E., Calvani R., Picca A., Cesari M., Arosio B. Role of age-related mitochondrial dysfunction in sarcopenia. Int. J. Mol. Sci. 2020;21:5236. doi: 10.3390/ijms21155236. PubMed DOI PMC

Galley H.F. Oxidative stress and mitochondrial dysfunction in sepsis. Br. J. Anaesth. 2011;107:57–64. doi: 10.1093/bja/aer093. PubMed DOI

Boengler K., Kosiol M., Mayr M., Schulz R., Rohrbach S. Mitochondria in ageing. Role in heart, skeletal muscle and adipose tissue. J. Cachexia Sarcopenia Muscle. 2017;8:349–369. doi: 10.1002/jcsm.12178. PubMed DOI PMC

Short K.R., Vitone J.L., Bigelow M.L., Proctor D.N., Nair K.S. Age and aerobic exercise training effects on whole body and muscle protein metabolism. Am. J. Phyisiol. Endocrinol. Metab. 2004;286:E92–E101. doi: 10.1152/ajpendo.00366.2003. PubMed DOI

Leduc-Gaudet J.P., Hussain S.N.A., Barreiro E., Gouspillou G. Mitochondrial dynamics and mitophagy in skeletal muscle health and aging. Int. J. Mol. Sci. 2021;22:8179. doi: 10.3390/ijms22158179. PubMed DOI PMC

Frontera W.R., Ochala J. Skeletal muscle: A brief review of structure and function. Calcif. Tissue Int. 2015;96:183–195. doi: 10.1007/s00223-014-9915-y. PubMed DOI

Guidicde J., Taylor J.M. Muscle as a paracrine and endocrine organ. Curr. Opin. Pharmacol. 2017;34:49–55. PubMed PMC

Bar-Or D., Rael L.T., Madayag R.M., Banton K.L., Il A.T., Acune D.L., Liser M.J., Marshall G.T., Mains C.W., Brody E. Stress hyperglycemia in critically ill patients: Insight into possible molecular pathways. Front. Med. 2019;6:54. doi: 10.3389/fmed.2019.00054. PubMed DOI PMC

Brooks G.A. Role of the heart in lactate shuttling. Front. Nutr. 2021;8:663560. doi: 10.3389/fnut.2021.663560. PubMed DOI PMC

Smirnova E., Griparic L., Shurland D.L., van der Bliek A.M. Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells. Mol. Biol. Cell. 2001;12:2245–2256. doi: 10.1091/mbc.12.8.2245. PubMed DOI PMC

Kalia R., Wang R.Y.R., Yusuf A., Thomas P.V., Agard D.A., Shaw J.M., Frost A. Structural basis of mitochondrial receptor binding and constriction by DRP1. Nature. 2018;558:401–405. doi: 10.1038/s41586-018-0211-2. PubMed DOI PMC

Otera H., Wang C.X., Cleland M.M., Setoguchi K., Yokota S., Youle R.J., Mihara K. Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells. J. Cell Biol. 2010;191:1141–1158. doi: 10.1083/jcb.201007152. PubMed DOI PMC

Song Z.Y., Ghochani M., McCaffery J.M., Frey T.G., Chan D.C. Mitofusins and OPA1 Mediate Sequential Steps in Mitochondrial Membrane Fusion. Mol. Biol. Cell. 2009;20:3525–3532. doi: 10.1091/mbc.e09-03-0252. PubMed DOI PMC

Hansen M.E., Simmons K.J., Tippetts T.S., Thatcher M.O., Saito R.R., Hubbard S.T., Trumbull A.M., Parker B.A., Taylor O.J., Bikman B.T. Lipopolysaccharide disrupts mitochondrial physiology in skeletal muscle via disparate effects on sphingolipid metabolisms. Shock. 2015;44:585–592. doi: 10.1097/SHK.0000000000000468. PubMed DOI PMC

Lazarou M., Sliter D.A., Kane L.A., Sarraf S.A., Wang C., Burman J.L., Sideris D.P., Fogel A.I., Youle R.J. The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy. Nature. 2015;524:309–314. doi: 10.1038/nature14893. PubMed DOI PMC

Calvani R., Joseph A.M., Adhihetty P.J., Miccheli A., Bossola M., Leeuwenburgh C., Bernabei R., Landi F., Marzetti E. Update on mitochondria and muscle aging: All wrong roads lead to sarcopenia. Biol. Chem. 2018;399:421–436. PubMed

O’Hara R., Tedone E., Ludlow A., Huang E., Arosio B., Mari D., Shay J.W. Quantitative mitochondrial copy number determination using droplet digital PCR with single-cell resolution. Genome Res. 2019;29:1878–1888. doi: 10.1101/gr.250480.119. PubMed DOI PMC

MacGarvey N.C., Suliman H.B., Bartz R.R., Fu P., Withers C.M., Welty-Wolf K.E., Piantadosi C.A. Activation of mitochondrial biogenesis by heme oxygenase-1-mediated NF-E2-related factor 2 induction rescue mice from lethal Staphylococcus aureus sepsis. Am. J. Respir. Crit. Care Med. 2012;185:851–861. doi: 10.1164/rccm.201106-1152OC. PubMed DOI PMC

Bullon P., Roman-Malo L., Marin-Aguilar F., Alvarez-Suarez J.M., Giampieri F., Battino M., Cordero M.D. Lipophilic antioxidants prevent lipopolysaccharide-induced mitochondrial dysfunction through mitochondrial biogenesis improvement. Pharmacol. Res. 2015;91:1–8. doi: 10.1016/j.phrs.2014.10.007. PubMed DOI

Hondares E., Pineda-Torra I., Iglesias R., Staels B., Villarroya F., Giralt M. PPARdelta, but not PPARalpha activates PGC-1alpha gene transcription in muscle. Biochem. Biophys. Res. Commun. 2007;354:1021–1027. doi: 10.1016/j.bbrc.2007.01.092. PubMed DOI

Dulac N., Leduc-Gaudet J.P., Cefis M., Ayoub M.B., Reynaud O., Shams A., Moamer A., Nery Fereira M.F., Hussain S.N., Gouispillou G. Regulation of muscle and mitochondrial health by the mitochondrial fission protein Drp1 in aged mice. J. Physiol. 2021;599:4045–4063. doi: 10.1113/JP281752. PubMed DOI

Yen Y.T., Yang H.R., Lo H.C., Hsieh Y.C., Tsai S.C., Hong C.W., Hsieh C.H. Enhancing autophagy with activated protein C and rapamycin protects against sepsis-induced acute lung injury. Surgery. 2013;153:689–698. doi: 10.1016/j.surg.2012.11.021. PubMed DOI

Van Zanten A.R., De Waele E., Wischmeyer P.E. Nutritional therapy and critical illness: Practical guidance for the ICU, post-ICU, and long-term convalescence phases. Crit. Care. 2019;23:368. doi: 10.1186/s13054-019-2657-5. PubMed DOI PMC

Musci R.V., Hamilton K.L., Linden M.A. Exercise-Induced Mitohormesis for the maintenance of skeletal muscle and the health span extension. Sport. 2019;7:170. doi: 10.3390/sports7070170. PubMed DOI PMC

Patterson S.D., Hughes L., Warmington S., Burr J., Scott B.R., Owens J., Abe T., Nielsen J.L., Libardi C.A., Laurentino G., et al. Blood flow restriction exercise: Consideration of methodology, application, and safety. Front. Physiol. 2019;10:533. doi: 10.3389/fphys.2019.00533. PubMed DOI PMC

Maffiuleti N.A., Roig M., Karatzanos E., Nanas S. Neuromuscular electrical stimulation for preventing skeletal-muscle weakness and wasting in critically ill patients: A systematic review. BMC Med. 2013;11:137. doi: 10.1186/1741-7015-11-137. PubMed DOI PMC

Bell R.A.V., Al-Khalaf M., Megeney L.A. The beneficial role of proteolysis in skeletal muscle growth and stress adaptation. Skelet. Muscle. 2016;6:16. doi: 10.1186/s13395-016-0086-6. PubMed DOI PMC

Hass K.F., Woodruff E., Brodie K. Proteasome function is required to maintain muscle cellular architecture. Biol. Cell. 2007;99:615–626. doi: 10.1042/BC20070019. PubMed DOI PMC

Murton A.J., Constantin D., Greenhaff P.L. The involvement of the ubiquitin proteasome system in humans skeletal muscle remodeling and atrophy. Biochim. Biophys Acta. 2008;1782:730–743. doi: 10.1016/j.bbadis.2008.10.011. PubMed DOI

Larsen B.D., Rampalli S., Burns L.E., Brunette S., Dilworth F.J., Megeney L.A. Caspase 3/caspase-activated DNase promote cell differentiation by inducing DNA strand breaks. Proc. Natl. Acad. Sci. USA. 2010;107:4230–4235. doi: 10.1073/pnas.0913089107. PubMed DOI PMC

Suryawan A., Rudar M., Fioroto M.L., Davis T.A. Differential regulation of mTORC1 activation by leucine and β-hydroxy-β-methylbutyrate in skeletal muscle of neonatal pigs. J. Appl. Physiol. 2020;128:286–295. doi: 10.1152/japplphysiol.00332.2019. PubMed DOI PMC

Dzik K.P., Kaczor J.J. Mechanisms of vitamin D on skeletal muscle function: Oxidative stress, energy metabolism and anabolic state. Eur. J. Appl. Physiol. 2019;119:825–839. doi: 10.1007/s00421-019-04104-x. PubMed DOI PMC

Sinha A., Hollingsworth K.G., Ball S., Cheetham T. Improving the vitamin D status of vitamin D deficient adults is assocciated with improved mitochondrial oxidative function in skeletal muscle. J. Clin. Endocrinol. Met. 2013;98:E509–E513. doi: 10.1210/jc.2012-3592. PubMed DOI

Qin E.S., Hough C.L., Andrews J., Bunnell A.E. Intensive care unit-acquired weakness and the COVID-19 pandemic: A clinical review. PM R. 2022;14:227–238. doi: 10.1002/pmrj.12757. PubMed DOI

Hughes L., Paton B., Rosentblatt B., Gissane C., Patterson S.D. Blood flow restriction training in clinical musculoskeletal rehabilitation: A systemic review and metaanalyses. Br. J. Sports Med. 2017;51:1003–1011. doi: 10.1136/bjsports-2016-097071. PubMed DOI

Shakoory B., Carcillo J.A., Chatham W.W., Amdur R.L., Zhao H., Dinarello C.A., Cron R.Q., Opal S.M. Interleukin-1 receptor blockade is associated with reduced mortality in sepsis patients with features of macrophage activation syndrome. Crit. Care Med. 2016;44:275–281. PubMed PMC

Kooistra E.J., Waalders N.J.B., Grondman I., Janssen N.A.F., de Nooijer A.H., Netea M.G., van de Veerdonk F.L., Ewalds E., van der Hoeven J.G., Kox M., et al. Anakinra treatment in critically ill COVID-19 patients: A prospective cohort study. Crit. Care. 2020;24:688. doi: 10.1186/s13054-020-03364-w. PubMed DOI PMC

Fernández J.P., Montero A.F., Matínez A.C., Pastor D., Rodrígez A.M., Roche E. Sarcopenia: Molecular pathways and potential targets for intervention. Int. J. Mol. Sci. 2020;21:8844. doi: 10.3390/ijms21228844. PubMed DOI PMC

Kim J.S., Cross J.M., Bamman M.M. Impact of resistence loading on myostatin expression and cell cycle regulation in young and older men and women. Am. J. Physiol. Endocrinol. Metab. 2005;288:E1100–E1119. doi: 10.1152/ajpendo.00464.2004. PubMed DOI

Paproski J.J., Finelo G.C., Murillo A., Mandel E. The importance of protein intake and strength exercises for older adult. JAAPA. 2019;32:32–36. doi: 10.1097/01.JAA.0000586328.11996.c0. PubMed DOI

Abiri B., Vafa M. The role of nutrition in attenuating age-related skeletal muscle atrophy. Adv. Exp. Med. Biol. 2020;1260:297–318. PubMed

Martínez-Arnau F.M., Fonfría-Vivas R., Buigues C., Castillo Y., Molina P., Hoogland A.J., vanDoesburg F., Pruimboom L., Fernández-Garrido J., Cauli O. Effects of leucine administration in sarcopenia. A randomized and placebo-controlled clinical trial. Nutrients. 2020;12:932. doi: 10.3390/nu12040932. PubMed DOI PMC

Yoon J.H., Kwon K.S. Receptor-mediated muscle homeostasis as a target for sarcopenia therapeutics. Endocrinol. Metab. 2021;36:478–490. doi: 10.3803/EnM.2021.1081. PubMed DOI PMC

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