Friend or enemy? Review of 17β-HSD10 and its role in human health or disease
Jazyk angličtina Země Anglie, Velká Británie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem, přehledy
Grantová podpora
204821/Z/16/Z
Wellcome Trust - United Kingdom
PubMed
32306391
DOI
10.1111/jnc.15027
Knihovny.cz E-zdroje
- Klíčová slova
- 17β-hydroxysteroid dehydrogenase type 10, Alzheimer's disease, HSD10, cancer, estradiol, neurosteroid,
- MeSH
- 3-hydroxyacyl-CoA-dehydrogenasy chemie genetika metabolismus MeSH
- Alzheimerova nemoc genetika metabolismus MeSH
- lidé MeSH
- mitochondrie genetika metabolismus MeSH
- mutace genetika MeSH
- nádory genetika metabolismus MeSH
- neurodegenerativní nemoci genetika metabolismus MeSH
- sekundární struktura proteinů MeSH
- zdravotní stav * MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- přehledy MeSH
- Názvy látek
- 3-hydroxyacyl-CoA-dehydrogenasy MeSH
- HSD17B10 protein, human MeSH Prohlížeč
17β-hydroxysteroid dehydrogenase (17β-HSD10) is a multifunctional human enzyme with important roles both as a structural component and also as a catalyst of many metabolic pathways. This mitochondrial enzyme has important functions in the metabolism, development and aging of the neural system, where it is involved in the homeostasis of neurosteroids, especially in regard to estradiol, changes in which make it an essential part of neurodegenerative pathology. These roles therefore, indicate that 17β-HSD10 may be a possible druggable target for neurodegenerative diseases including Alzheimer's disease (AD), and in hormone-dependent cancer. The objective of this review was to provide a summary about physiological functions and pathological roles of 17β-HSD10 and the modulators of its activity.
Zobrazit více v PubMed
Abreo, M. A., Meng, J. J., & Agree, C. S. (2005). Fused Pyrazole Compounds, Pharmaceutical Compositions, and Methods For Modulating Or Inhibiting ERAB Or HADH2 Activity. US6964957 patent.
Aitken, L., Benek, O., McKelvie, B. E., Hughes, R. E., Hroch, L., Schmidt, M., & Major, L. L. (2019). Novel Benzothiazole-based Ureas as 17β-HSD10 Inhibitors. A Potential Alzheimer’s Disease Treatment. Molecules, 24, 2757. https://doi.org/10.3390/molecules24152757
Aitken, L., Baillie, G., Pannifer, A., Morrison, A., Jones, P. S., Smith, T. K., … Gunn-Moore, F. J. (2017). In Vitro Assay Development and HTS of Small-Molecule Human ABAD/17β-HSD10 Inhibitors as Therapeutics in Alzheimer’s Disease. SLAS Discov. Adv. Life Sci. R D, 22, 676-685. https://doi.org/10.1177/2472555217697964.
Aitken, L., Quinn, S. D., Perez-Gonzalez, C., Samuel, I. D. W., Penedo, J. C., & Gunn-Moore, F. J. (2016). Morphology-specific inhibition of β-amyloid aggregates by 17β-hydroxysteroid dehydrogenase type 10. ChemBioChem, 17, 1029-1037. https://doi.org/10.1002/cbic.201600081
Akagawa, S., Fukao, T., Akagawa, Y., Sasai, H., Kohdera, U., Kino, M., … Kaneko, K. (2017). Japanese Male Siblings with 2-Methyl-3-Hydroxybutyryl-CoA Dehydrogenase Deficiency (HSD10 Disease) Without Neurological Regression. JIMD Rep., 32, 81-85. https://doi.org/10.1007/8904_2016_570.
Alvarez-De-La-Rosa, M., Silva, I., Nilsen, J., PéRez, M. M., GarcíA-Segura, L. M., áVila, J., & Naftolin, F., (2005). Estradiol prevents neural tau hyperphosphorylation characteristic of Alzheimer’s disease. Annals of the New York Academy of Sciences, 1052, 210-224. https://doi.org/10.1196/annals.1347.016
Amberger, A., Deutschmann, A. J., Traunfellner, P., Moser, P., Feichtinger, R. G., Kofler, B., & Zschocke, J. (2016). 17β-Hydroxysteroid dehydrogenase type 10 predicts survival of patients with colorectal cancer and affects mitochondrial DNA content. Cancer Letters, 374, 149-155. https://doi.org/10.1016/j.canlet.2016.02.011
Amtul, Z., Wang, L., Westaway, D., & Rozmahel, R. F. (2010). Neuroprotective mechanism conferred by 17beta-estradiol on the biochemical basis of Alzheimer’s disease. Neuroscience, 169, 781-786. https://doi.org/10.1016/j.neuroscience.2010.05.031
Anand, A., Patience, A. A., Sharma, N., & Khurana, N. (2017). The present and future of pharmacotherapy of Alzheimer’s disease: A comprehensive review. European Journal of Pharmacology, 815, 364-375. https://doi.org/10.1016/j.ejphar.2017.09.043
Anandatheerthavarada, H. K., Biswas, G., Robin, M.-A., & Avadhani, N. G. (2003). Mitochondrial targeting and a novel transmembrane arrest of Alzheimer’s amyloid precursor protein impairs mitochondrial function in neuronal cells. Journal of Cell Biology, 161, 41-54. https://doi.org/10.1083/jcb.200207030
Audano, M., Schneider, A., & Mitro, N. (2018). Mitochondria, lysosomes, and dysfunction: Their meaning in neurodegeneration. Journal of Neurochemistry, 147, 291-309. https://doi.org/10.1111/jnc.14471
Ayan, D., Maltais, R., & Poirier, D. (2012). Identification of a 17β-hydroxysteroid dehydrogenase type 10 steroidal inhibitor: A tool to investigate the role of type 10 in Alzheimer’s disease and prostate cancer. ChemMedChem, 7, 1181-1184. https://doi.org/10.1002/cmdc.201200129
Barrett-Connor, E. (2006). Raloxifene: Risks and benefits. Annals of the New York Academy of Sciences, 949, 295-303. https://doi.org/10.1111/j.1749-6632.2001.tb04036.x
Belelli, D., & Lambert, J. J. (2005). Neurosteroids: Endogenous regulators of the GABA(A) receptor. Nature Reviews Neuroscience, 6, 565-575. https://doi.org/10.1038/nrn1703
Benek, O., Aitken, L., Hroch, L., Kuca, K., Gunn-Moore, F., & Musilek, K. (2015). A direct interaction between mitochondrial proteins and amyloid-β peptide and its significance for the progression and treatment of Alzheimer’s disease. Current Medicinal Chemistry, 22, 1056-1085. https://doi.org/10.2174/0929867322666150114163051
Benek, O., Hroch, L., Aitken, L., Dolezal, R., Hughes, R., Guest, P., Benkova, M., … Musilek, K. (2017). 6-Benzothiazolyl ureas, thioureas and guanidines are potent inhibitors of ABAD/17β-HSD10 and potential drugs for Alzheimer"s disease treatment: Design, synthesis and in vitro evaluation. Medicinal Chemistry, 14, 345-358. https://doi.org/10.2174/1573406413666170109142725
Benek, O., Hroch, L., Aitken, L., Gunn-Moore, F., Vinklarova, L., Kuca, K., … Musilek, K. (2018). 1-(Benzo[d ]thiazol-2-yl)-3-phenylureas as dual inhibitors of casein kinase 1 and ABAD enzymes for treatment of neurodegenerative disorders. Journal of Enzyme Inhibition and Medicinal Chemistry, 33, 665-670. https://doi.org/10.1080/14756366.2018.1445736.
Blass, J. P., Sheu, R. K., & Gibson, G. E. (2000). Inherent abnormalities in energy metabolism in Alzheimer disease. Interaction with cerebrovascular compromise. Annals of the New York Academy of Sciences, 903, 204-221. https://doi.org/10.1111/j.1749-6632.2000.tb06370.x
Borger, E., Aitken, L., Du, H., Zhang, W., Gunn-Moore, F. J., & Yan, S. S. D. (2013). Is amyloid binding alcohol dehydrogenase a drug target for treating Alzheimer’s disease? Current Alzheimer Research, 10, 21-29. https://doi.org/10.2174/1567205011310010004
Borger, E., Aitken, L., Muirhead, K. E. A., Allen, Z. E., Ainge, J. A., Conway, S. J., & Gunn-Moore, F. J. (2011). Mitochondrial β-amyloid in Alzheimer’s disease. Biochemical Society Transactions, 39, 868-873. https://doi.org/10.1042/BST0390868
Boutin, S., & Poirier, D. (2018). Structure confirmation and evaluation of a nonsteroidal inhibitor of 17β-hydroxysteroid dehydrogenase type 10. Magnetochemistry, 4, 32. https://doi.org/10.3390/magnetochemistry4030032
Boutin, S., Roy, J., Maltais, R., Alata, W., Calon, F., & Poirier, D. (2018). Identification of steroidal derivatives inhibiting the transformations of allopregnanolone and estradiol by 17β-hydroxysteroid dehydrogenase type 10. Bioorganic & Medicinal Chemistry Letters, 28, 3554-3559. https://doi.org/10.1016/j.bmcl.2018.09.031
Burns, A., & Iliffe, S. (2009). Alzheimer’s disease. BMJ, 338, b158. https://doi.org/10.1136/bmj.b158
Carlson, E. A., Marquez, R. T., Du, F., Wang, Y., Xu, L., & Yan, S. S. (2015). Overexpression of 17β-hydroxysteroid dehydrogenase type 10 increases pheochromocytoma cell growth and resistance to cell death. BMC Cancer, 15, 166. https://doi.org/10.1186/s12885-015-1173-5
Caspersen, C., Wang, N., Yao, J., Sosunov, A., Chen, X., Lustbader, J. W., … Yan, S. D. (2005). Mitochondrial Abeta: a potential focal point for neuronal metabolic dysfunction in Alzheimer’s disease. FASEB. J. off. Publ. Fed. Am. Soc. Exp. Biol., 19, 2040-2041. https://doi.org/10.1096/fj.05-3735fje.
Cazorla, M. R., Verdú, A., Pérez-Cerdá, C., & Ribes, A. (2007). Neuroimage findings in 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency. Pediatric Neurology, 36, 264-267. https://doi.org/10.1016/j.pediatrneurol.2006.11.014
Chang, M.-S. (2011). Dual roles of estrogen metabolism in mammary carcinogenesis. BMB Reports, 44, 423-434. https://doi.org/10.5483/BMBRep.2011.44.7.423
Chatfield, K. C., Coughlin, C. R., Friederich, M. W., Gallagher, R. C., Hesselberth, J. R., Lovell, M. A., … Van Hove, J. L. (2015). Mitochondrial energy failure in HSD10 disease is due to defective mtDNA transcript processing. Mitochondrion, 21, 1-10. https://doi.org/10.1016/j.mito.2014.12.005.
Chen, J. X., & Yan, S. S. (2010). Role of mitochondrial amyloid-beta in Alzheimer’s disease. The Journal of Alzheimer's Disease, 20(Suppl 2), S569-578. https://doi.org/10.3233/JAD-2010-100357
Chen, V.- C.-H., Chan, H.-L., Hsu, T.-C., Lu, M.-L., Lee, Y.-C., Lee, Y., … Lee, C. T. (2018). New use for old drugs: The protective effect of atypical antipsychotics on hepatocellular carcinoma. International Journal of Cancer, 144, 2428-2439. https://doi.org/10.1002/ijc.31980.
Collongues, N., Patte-Mensah, C., De Seze, J., Mensah-Nyagan, A.-G., & Derfuss, T. (2018). Testosterone and estrogen in multiple sclerosis: From pathophysiology to therapeutics. Expert Review of Neurotherapeutics, 18, 515-522. https://doi.org/10.1080/14737175.2018.1481390
Cornel, K. M. C., Kruitwagen, R. F. P. M., Delvoux, B., Visconti, L., Van de Vijver, K. K., Day, J. M., … Romano, A. (2012). Overexpression of 17β-hydroxysteroid dehydrogenase type 1 increases the exposure of endometrial cancer to 17β-estradiol. Journal of Clinical Endocrinology and Metabolism, 97, E591-601. https://doi.org/10.1210/jc.2011-2994.
Deutschmann, A. J., Amberger, A., Zavadil, C., Steinbeisser, H., Mayr, J. A., Feichtinger, R. G., … Zschocke, J. (2014). Mutation or knock-down of 17β-hydroxysteroid dehydrogenase type 10 cause loss of MRPP1 and impaired processing of mitochondrial heavy strand transcripts. Human Molecular Genetics, 23, 3618-3628. https://doi.org/10.1093/hmg/ddu072.
Dilly, S. J., Clark, A. J., Marsh, A., Mitchell, D. A., Cain, R., Fishwick, C. W. G., & Taylor, P. C. (2017a). A chemical genomics approach to drug reprofiling in oncology: Antipsychotic drug risperidone as a potential adenocarcinoma treatment. Cancer Letters, 393, 16-21. https://doi.org/10.1016/j.canlet.2017.01.042
Dilly, S. J., Morris, G. S., Taylor, P. C., Parmentier, F., Williams, C., & Afshar, M. (2019). Clinical pharmacokinetics of a lipid-based formulation of risperidone, VAL401: Analysis of a single dose in an open-label trial of late-stage cancer patients. European Journal of Drug Metabolism and Pharmacokinetics, 44, 557-565. https://doi.org/10.1007/s13318-018-00538-4
Dilly, S., Stoloff, G., & Taylor, P. (2017b) Modulators of androgen synthesis. US9072743 patent.
Du Yan, S., Zhu, Y., Stern, E. D., Hwang, Y. C., Hori, O., Ogawa, S., Frosch, M. P., Connolly, E. S. Jr., McTaggert, R., Pinsky, D. J., Clarke, S., Stern, D. M., Ramasamy, R. (2000). Amyloid beta -peptide-binding alcohol dehydrogenase is a component of the cellular response to nutritional stress. Journal of Biological Chemistry, 275, 27100-27109. https://doi.org/10.1074/jbc.m000055200
Ensenauer, R., Niederhoff, H., Ruiter, J. P. N., Wanders, R. J. A., Schwab, K. O., Brandis, M., & Lehnert, W. (2002). Clinical variability in 3-hydroxy-2-methylbutyryl-CoA dehydrogenase deficiency. Annals of Neurology, 51, 656-659. https://doi.org/10.1002/ana.10169
Evin, G., & Weidemann, A. (2002). Biogenesis and metabolism of Alzheimer’s disease Abeta amyloid peptides. Peptides, 23, 1285-1297. https://doi.org/10.1016/S0196-9781(02)00063-3
Falk, M. J., Gai, X., Shigematsu, M., Vilardo, E., Takase, R., McCormick, E., Christian, T., Place, E., Pierce, E. A., Consugar, M., Gamper, H. B., Rossmanith, W., Hou, Y. -M. (2016). A novel HSD17B10 mutation impairing the activities of the mitochondrial RNase P complex causes X-linked intractable epilepsy and neurodevelopmental regression. RNA Biology, 13, 477-485. https://doi.org/10.1080/15476286.2016.1159381
Feldman, H. H. (2007). Atlas of Alzheimer´s disease. Informa UK Ltd. https://doi.org/10.3109/9781435626133
Frackowiak, J., Mazur-Kolecka, B., Kaczmarski, W., & Dickson, D. (2001). Deposition of Alzheimer’s vascular amyloid-beta is associated with decreased expression of brain L-3-hydroxyacyl-coenzyme A dehydrogenase (ERAB). Brain Research, 907, 44-53. https://doi.org/10.1016/S0006-8993(01)02497-0
Froemming, M. K., & Sames, D. (2007). Harnessing functional plasticity of enzymes: A fluorogenic probe for imaging 17beta-HSD10 dehydrogenase, an enzyme involved in Alzheimer’s and Parkinson’s diseases. Journal of the American Chemical Society, 129, 14518-14522. https://doi.org/10.1021/ja072601x
Froyen, G., Corbett, M., Vandewalle, J., Jarvela, I., Lawrence, O., Meldrum, C., … Gécz, J. (2008). Submicroscopic duplications of the hydroxysteroid dehydrogenase HSD17B10 and the E3 ubiquitin ligase HUWE1 are associated with mental retardation. American Journal of Human Genetics, 82, 432-443. https://doi.org/10.1016/j.ajhg.2007.11.002.
Fukao, T., Akiba, K., Goto, M., Kuwayama, N., Morita, M., Hori, T., … Hasegawa, Y. (2014). The first case in Asia of 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency (HSD10 disease) with atypical presentation. Journal of Human Genetics, 59, 609-614. https://doi.org/10.1038/jhg.2014.79.
Furuta, S., Kobayashi, A., Miyazawa, S., & Hashimoto, T. (1997). Cloning and expression of cDNA for a newly identified isozyme of bovine liver 3-hydroxyacyl-CoA dehydrogenase and its import into mitochondria. Biochimica Et Biophysica Acta, 1350, 317-324. https://doi.org/10.1016/S0167-4781(96)00171-6
Gandy, S., & Petanceska, S. (2001). Regulation of alzheimer beta-amyloid precursor trafficking and metabolism. Advances in Experimental Medicine and Biology, 487, 85-100. https://doi.org/10.1007/978-1-4615-1249-3_7
García-Villoria, J., Gort, L., Madrigal, I., Fons, C., Fernández, C., Navarro-Sastre, A., … Ribes, A. (2010). X-inactivation of HSD17B10 revealed by cDNA analysis in two female patients with 17β-hydroxysteroid dehydrogenase 10 deficiency. European Journal of Human Genetics, 18, 1353-1355. https://doi.org/10.1038/ejhg.2010.118.
Giorgio, V., Soriano, M. E., Basso, E., Bisetto, E., Lippe, G., Forte, M. A., & Bernardi, P. (2010). Cyclophilin D in Mitochondrial Pathophysiology. Biochimica Et Biophysica Acta, 1797, 1113-1118. https://doi.org/10.1016/j.bbabio.2009.12.006
Glenner, G. G., & Wong, C. W. (1984). Alzheimer’s disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochemical and Biophysical Research Communications, 120, 885-890. https://doi.org/10.1016/S0006-291X(84)80190-4
Greene, G. L., Gilna, P., Waterfield, M., Baker, A., Hort, Y., & Shine, J. (1986). Sequence and expression of human estrogen receptor complementary DNA. Science, 231, 1150-1154. https://doi.org/10.1126/science.3753802
Grimm, A., & Eckert, A. (2017). Brain aging and neurodegeneration: From a mitochondrial point of view. Journal of Neurochemistry, 143, 418-431. https://doi.org/10.1111/jnc.14037
Haack, T. B., Kopajtich, R., Freisinger, P., Wieland, T., Rorbach, J., Nicholls, T. J., … Prokisch, H. (2013). ELAC2 mutations cause a mitochondrial RNA processing defect associated with hypertrophic cardiomyopathy. American Journal of Human Genetics, 93, 211-223. https://doi.org/10.1016/j.ajhg.2013.06.006.
Hansson, P. C. A., Alikhani, N., Behbahani, H., Wiehager, B., Pavlov, P. F., Alafuzoff, I., Leinonen, V. (2008). The amyloid beta-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae. Proceedings of the National Academy of Sciences of the United States of America, 105, 13145-13150. https://doi.org/10.1073/pnas.0806192105
He, X.-Y., Dobkin, C., & Yang, S.-Y. (2011). Does the HSD17B10 gene escape from X-inactivation? European Journal of Human Genetics, 19, 123-124. https://doi.org/10.1038/ejhg.2010.192
He, X.-Y., Dobkin, C., & Yang, S.-Y. (2019). 17β-Hydroxysteroid dehydrogenases and neurosteroid metabolism in the central nervous system. Molecular and Cellular Endocrinology, 489, 92-97. https://doi.org/10.1016/j.mce.2018.10.002
He, X.-Y., Isaacs, C., & Yang, S.-Y. (2018). Roles of mitochondrial 17β-hydroxysteroid dehydrogenase type 10 in Alzheimer’s disease. Journal of Alzheimer's Disease, 62, 665-673. https://doi.org/10.3233/JAD-170974
He, X. Y., Merz, G., Mehta, P., Schulz, H., & Yang, S. Y. (1999). Human brain short chain L-3-hydroxyacyl coenzyme A dehydrogenase is a single-domain multifunctional enzyme. Characterization of a novel 17beta-hydroxysteroid dehydrogenase. Journal of Biological Chemistry, 274, 15014-15019. https://doi.org/10.1074/jbc.274.21.15014
He, X. Y., Merz, G., Yang, Y. Z., Mehta, P., Schulz, H., & Yang, S. Y. (2001). Characterization and localization of human type10 17beta-hydroxysteroid dehydrogenase. European Journal of Biochemistry, 268, 4899-4907. https://doi.org/10.1046/j.0014-2956.2001.02421.2421.x
He, X. Y., Merz, G., Yang, Y. Z., Pullakart, R., Mehta, P., Schulz, H., & Yang, S. Y. (2000a). Function of human brain short chain L-3-hydroxyacyl coenzyme A dehydrogenase in androgen metabolism. Biochimica Et Biophysica Acta, 1484, 267-277. https://doi.org/10.1016/S1388-1981(00)00014-7
He, X. Y., Schulz, H., & Yang, S. Y. (1998). A human brain L-3-hydroxyacyl-coenzyme A dehydrogenase is identical to an amyloid beta-peptide-binding protein involved in Alzheimer’s disease. Journal of Biological Chemistry, 273, 10741-10746. https://doi.org/10.1074/jbc.273.17.10741
He, X.-Y., Wegiel, J., & Yang, S.-Y. (2005). Intracellular oxidation of allopregnanolone by human brain type 10 17beta-hydroxysteroid dehydrogenase. Brain Research, 1040, 29-35. https://doi.org/10.1016/j.brainres.2005.01.022
He, X.-Y., Wen, G.-Y., Merz, G., Lin, D., Yang, Y.-Z., Mehta, P., Schulz, H., Yang, S.-Y. (2002). Abundant type 10 17β-hydroxysteroid dehydrogenase in the hippocampus of mouse Alzheimer’s disease model. Molecular Brain Research, 99, 46-53. https://doi.org/10.1016/S0169-328X(02)00102-X
He, X.-Y., & Yang, S.-Y. (2006). Roles of type 10 17beta-hydroxysteroid dehydrogenase in intracrinology and metabolism of isoleucine and fatty acids. Endocrine, Metabolic & Immune Disorders: Drug Targets, 6, 95-102. https://doi.org/10.2174/187153006776056639
He, X.-Y., Yang, Y.-Z., Peehl, D. M., Lauderdale, A., Schulz, H., & Yang, S.-Y. (2003). Oxidative 3alpha-hydroxysteroid dehydrogenase activity of human type 10 17beta-hydroxysteroid dehydrogenase. Journal of Steroid Biochemistry and Molecular Biology, 87, 191-198. https://doi.org/10.1016/j.jsbmb.2003.07.007
He, X. Y., Yang, Y. Z., Schulz, H., & Yang, S. Y. (2000b). Intrinsic alcohol dehydrogenase and hydroxysteroid dehydrogenase activities of human mitochondrial short-chain L-3-hydroxyacyl-CoA dehydrogenase. The Biochemical Journal, 345(Pt 1), 139-143. https://doi.org/10.1042/bj3450139
Henderson, V. W. (2014). Alzheimer’s disease: Review of hormone therapy trials and implications for treatment and prevention after menopause. Journal of Steroid Biochemistry and Molecular Biology, 142, 99-106. https://doi.org/10.1016/j.jsbmb.2013.05.010
Hirai, K., Aliev, G., Nunomura, A., Fujioka, H., Russell, R. L., Atwood, C. S., … Smith, M. A. (2001). Mitochondrial Abnormalities in Alzheimer’s Disease. Journal of Neuroscience, 21, 3017-3023. https://doi.org/10.1523/JNEUROSCI.21-09-03017.2001.
Holzmann, J., Frank, P., Löffler, E., Bennett, K. L., Gerner, C., & Rossmanith, W. (2008). RNase P without RNA: Identification and functional reconstitution of the human mitochondrial tRNA processing enzyme. Cell, 135, 462-474. https://doi.org/10.1016/j.cell.2008.09.013
Hroch, L., Benek, O., Guest, P., Aitken, L., Soukup, O., Janockova, J., … Musilek, K. (2016). Design, synthesis and in vitro evaluation of benzothiazole-based ureas as potential ABAD/17β-HSD10 modulators for Alzheimer’s disease treatment. Bioorganic & Medicinal Chemistry Letters, 26, 3675-3678. https://doi.org/10.1016/j.bmcl.2016.05.087.
Hroch, L., Guest, P., Benek, O., Soukup, O., Janockova, J., Dolezal, R., Kuca, K., Aitken, L., Smith, T. K., Gunn-Moore, F., Zala, D., Ramsay, R. R., Musilek, K. (2017). Synthesis and evaluation of frentizole-based indolyl thiourea analogues as MAO/ABAD inhibitors for Alzheimer’s disease treatment. Bioorganic & Medicinal Chemistry, 25, 1143-1152. https://doi.org/10.1016/j.bmc.2016.12.029
Huang, L.-K., Chao, S.-P., & Hu, C.-J. (2020). Clinical trials of new drugs for Alzheimer disease. Journal of Biomedical Science, 27, 18. https://doi.org/10.1186/s12929-019-0609-7
Ishii, K., Sasaki, M., Kitagaki, H., Yamaji, S., Sakamoto, S., Matsuda, K., & Mori, E. (1997). Reduction of cerebellar glucose metabolism in advanced Alzheimer’s disease. Journal of nuclear medicine : official publication, Society of Nuclear Medicine, 38, 925-928.
Jansson, A. K., Gunnarsson, C., Cohen, M., Sivik, T., & Stål, O. (2006). 17beta-hydroxysteroid dehydrogenase 14 affects estradiol levels in breast cancer cells and is a prognostic marker in estrogen receptor-positive breast cancer. Cancer Research, 66, 11471-11477. https://doi.org/10.1158/0008-5472.CAN-06-1448
Jayaraman, A., Carroll, J. C., Morgan, T. E., Lin, S., Zhao, L., Arimoto, J. M., … Pike, C. J. (2012). 17β-Estradiol and progesterone regulate expression of β-amyloid clearance factors in primary neuron cultures and female rat brain. Endocrinology, 153, 5467-5479. https://doi.org/10.1210/en.2012-1464.
Jazbutyte, V., Kehl, F., Neyses, L., & Pelzer, T. (2009). Estrogen receptor alpha interacts with 17beta-hydroxysteroid dehydrogenase type 10 in mitochondria. Biochemical and Biophysical Research Communications, 384, 450-454. https://doi.org/10.1016/j.bbrc.2009.04.139
Jörnvall, H., Persson, B., Krook, M., Atrian, S., Gonzàlez-Duarte, R., Jeffery, J., & Ghosh, D. (1995). Short-chain dehydrogenases/reductases (SDR). Biochemistry, 34, 6003-6013. https://doi.org/10.1021/bi00018a001
Kissinger, C. R., Rejto, P. A., Pelletier, L. A., Thomson, J. A., Showalter, R. E., Abreo, M. A., … Villafranca, J. E. (2004). Crystal structure of human ABAD/HSD10 with a bound inhibitor: Implications for design of Alzheimer’s disease therapeutics. Journal of Molecular Biology, 342, 943-952. https://doi.org/10.1016/j.jmb.2004.07.071.
Kobayashi, A., Jiang, L. L., & Hashimoto, T. (1996). Two mitochondrial 3-hydroxyacyl-CoA dehydrogenases in bovine liver. Journal of Biochemistry, 119, 775-782. https://doi.org/10.1093/oxfordjournals.jbchem.a021307
Korman, S. H. (2006). Inborn errors of isoleucine degradation: A review. Molecular Genetics and Metabolism, 89, 289-299. https://doi.org/10.1016/j.ymgme.2006.07.010
Korman, S. H., & Yang, S.-Y. (2007). HSD17B10 replaces HADH2 as the approved designation for the gene mutated in 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency. Molecular Genetics and Metabolism, 91, 115. https://doi.org/10.1016/j.ymgme.2007.01.001
Kota, K., Brufsky, A., Oesterreich, S., & Lee, A. (2017) Estradiol as a targeted, late-line therapy in metastatic breast cancer with estrogen receptor amplification. Cureus, 9, e1434. https://doi.org/10.7759/cureus.1434
Kristofikova, Z., Ricny, J., Kaping, D., Klaschka, J., Kotoucova, J., & Bartos, A. (2018). Levels of 17β-hydroxysteroid dehydrogenase type 10 in CSF are not a valuable biomarker for multiple sclerosis. Biomarkers in Medicine, 12, 1331-1340. https://doi.org/10.2217/bmm-2018-0061
Kruman, I. I., & Mattson, M. P. (1999). Pivotal role of mitochondrial calcium uptake in neural cell apoptosis and necrosis. Journal of Neurochemistry, 72, 529-540. https://doi.org/10.1046/j.1471-4159.1999.0720529.x
Kuiper, G. G., Enmark, E., Pelto-Huikko, M., Nilsson, S., & Gustafsson, J. A. (1996). Cloning of a novel receptor expressed in rat prostate and ovary. Proceedings of the National Academy of Sciences of the United States of America, 93, 5925-5930. https://doi.org/10.1073/pnas.93.12.5925
Kulkarni, J., Gavrilidis, E., Worsley, R., & Hayes, E. (2012). Role of estrogen treatment in the management of schizophrenia. CNS Drugs, 26, 549-557. https://doi.org/10.2165/11630660-000000000-00000
Lejri, I., Grimm, A., & Eckert, A. (2018). Mitochondria, estrogen and female brain aging. Frontiers in Aging Neuroscience, 10, 124. https://doi.org/10.3389/fnagi.2018.00124
Lenski, C., Kooy, R. F., Reyniers, E., Loessner, D., Wanders, R. J. A., Winnepenninckx, B., … Ramser, J. (2007). The reduced expression of the HADH2 protein causes X-linked mental retardation, choreoathetosis, and abnormal behavior. American Journal of Human Genetics, 80, 372-377. https://doi.org/10.1086/511527.
Lim, Y.-A., Grimm, A., Giese, M., Mensah-Nyagan, A. G., Villafranca, J. E., Ittner, L. M., … Götz, J. (2011). Inhibition of the mitochondrial enzyme ABAD restores the amyloid-β-mediated deregulation of estradiol. PLoS ONE, 6, e28887. https://doi.org/10.1371/journal.pone.0028887.
Liu, S.-L., Wang, C., Jiang, T., Tan, L., Xing, A., & Yu, J.-T. (2016). The role of Cdk5 in Alzheimer’s disease. Molecular Neurobiology, 53, 4328-4342. https://doi.org/10.1007/s12035-015-9369-x
Lukacik, P., Kavanagh, K. L., & Oppermann, U. (2006). Structure and function of human 17beta-hydroxysteroid dehydrogenases. Molecular and Cellular Endocrinology, 248, 61-71. https://doi.org/10.1016/j.mce.2005.12.007
Luo, M. J., Mao, L. F., & Schulz, H. (1995). Short-chain 3-hydroxy-2-methylacyl-CoA dehydrogenase from rat liver: Purification and characterization of a novel enzyme of isoleucine metabolism. Archives of Biochemistry and Biophysics, 321, 214-220. https://doi.org/10.1006/abbi.1995.1388
Lustbader, J. W., Cirilli, M., Lin, C., Xu, H. W., Takuma, K., Wang, N., … Wu, H. (2004). ABAD directly links Abeta to mitochondrial toxicity in Alzheimer’s disease. Science, 304, 448-452. https://doi.org/10.1126/science.1091230.
Maggi, A., Ciana, P., Belcredito, S., & Vegeto, E. (2004). Estrogens in the nervous system: Mechanisms and nonreproductive functions. Annual Review of Physiology, 66, 291-313. https://doi.org/10.1146/annurev.physiol.66.032802.154945
Manthey, D., & Behl, C. (2006). From structural biochemistry to expression profiling: Neuroprotective activities of estrogen. Neuroscience, 138, 845-850. https://doi.org/10.1016/j.neuroscience.2005.10.058
Marchais-Oberwinkler, S., Henn, C., Möller, G., Klein, T., Negri, M., Oster, A., … Adamski, J. (2011). 17β-Hydroxysteroid dehydrogenases (17β-HSDs) as therapeutic targets: Protein structures, functions, and recent progress in inhibitor development. Journal of Steroid Biochemistry and Molecular Biology, 125, 66-82. https://doi.org/10.1016/j.jsbmb.2010.12.013.
Marder, S. R., & Meibach, R. C. (1994). Risperidone in the treatment of schizophrenia. American Journal of Psychiatry, 151, 825-835. https://doi.org/10.1176/ajp.151.6.825
Marino, M., Galluzzo, P., & Ascenzi, P. (2006). Estrogen signaling multiple pathways to impact gene transcription. Current Genomics, 7, 497-508. https://doi.org/10.2174/138920206779315737
Marques, A. T., Antunes, A., Fernandes, P. A., & Ramos, M. J. (2006). Comparative evolutionary genomics of the HADH2 gene encoding Aβ-binding alcohol dehydrogenase/17β-hydroxysteroid dehydrogenase type 10 (ABAD/HSD10). BMC Genomics, 7, 202. https://doi.org/10.1186/1471-2164-7-202
Marques, A. T., Antunes, A., Fernandes, P. A., & Ramos, M. J. (2008a). Computational optimization of AG18051 inhibitor for amyloid-β binding alcohol dehydrogenase enzyme. International Journal of Quantum Chemistry, 108, 1982-1991. https://doi.org/10.1002/qua.21716
Marques, A. T., Fernandes, P. A., & Ramos, M. J. (2008b). Molecular dynamics simulations of the amyloid-beta binding alcohol dehydrogenase (ABAD) enzyme. Bioorganic & Medicinal Chemistry, 16, 9511-9518. https://doi.org/10.1016/j.bmc.2008.09.043
Marques, A. T., Fernandes, P. A., & Ramos, M. J. (2009). ABAD: A potential therapeutic target for Abeta-induced mitochondrial dysfunction in Alzheimer’s disease. Mini Reviews in Medicinal Chemistry, 9, 1002-1008. https://doi.org/10.2174/138955709788681627
Marx, C. E., Trost, W. T., Shampine, L. J., Stevens, R. D., Hulette, C. M., Steffens, D. C., … Lieberman, J. A. (2006). The neurosteroid allopregnanolone is reduced in prefrontal cortex in Alzheimer’s disease. Biological Psychiatry, 60, 1287-1294. https://doi.org/10.1016/j.biopsych.2006.06.017.
Medina, M. (2018). An overview on the clinical development of tau-based therapeutics. International Journal of Molecular Sciences, 19, 1160. https://doi.org/10.3390/ijms19041160
Miller, A. P., & Willard, H. F. (1998). Chromosomal basis of X chromosome inactivation: Identification of a multigene domain in Xp11.21-p11.22 that escapes X inactivation. Proceedings of the National Academy of Sciences of the United States of America, 95, 8709-8714. https://doi.org/10.1073/pnas.95.15.8709
Moreira, P. I., Duarte, A. I., Santos, M. S., Rego, A. C., & Oliveira, C. R. (2009). An integrative view of the role of oxidative stress, mitochondria and insulin in Alzheimer’s disease. J. Alzheimers Dis. JAD, 16, 741-761. https://doi.org/10.3233/JAD-2009-0972
Morkuniene, R., Arandarcikaite, O., & Borutaite, V. (2006). Estradiol prevents release of cytochrome c from mitochondria and inhibits ischemia-induced apoptosis in perfused heart. Experimental Gerontology, 41, 704-708. https://doi.org/10.1016/j.exger.2006.02.010
Morkuniene, R., Jekabsone, A., & Borutaite, V. (2002). Estrogens prevent calcium-induced release of cytochrome c from heart mitochondria. FEBS Letters, 521, 53-56. https://doi.org/10.1016/S0014-5793(02)02820-X
Murakami, Y., Ohsawa, I., Kasahara, T., & Ohta, S. (2009). Cytoprotective role of mitochondrial amyloid beta peptide-binding alcohol dehydrogenase against a cytotoxic aldehyde. Neurobiology of Aging, 30, 325-329. https://doi.org/10.1016/j.neurobiolaging.2007.07.002
Murphy, C. T., McCarroll, S. A., Bargmann, C. I., Fraser, A., Kamath, R. S., Ahringer, J., … Kenyon, C. (2003). Genes that act downstream of DAF-16 to influence the lifespan of Caenorhabditis elegans. Nature, 424, 277-283. https://doi.org/10.1038/nature01789.
Nelson, L. R., & Bulun, S. E. (2001). Estrogen production and action. Journal of the American Academy of Dermatology, 45, S116-124. https://doi.org/10.1067/mjd.2001.117432
Newhouse, P., & Dumas, J. (2015). Estrogen-cholinergic interactions: Implications for cognitive aging. Hormones and Behavior, 74, 173-185. https://doi.org/10.1016/j.yhbeh.2015.06.022
Noetzli, M., & Eap, C. B. (2013). Pharmacodynamic, pharmacokinetic and pharmacogenetic aspects of drugs used in the treatment of Alzheimer’s disease. Clinical Pharmacokinetics, 52, 225-241. https://doi.org/10.1007/s40262-013-0038-9
Nordling, E., Oppermann, U. C., Jörnvall, H., & Persson, B. (2001). Human type 10 17 beta-hydroxysteroid dehydrogenase: Molecular modelling and substrate docking. Journal of Molecular Graphics and Modelling, 19(514-520), 591-593. https://doi.org/10.1016/S1093-3263(00)00098-X
Oerum, S., Roovers, M., Rambo, R. P., Kopec, J., Bailey, H. J., Fitzpatrick, F., … Yue, W. W. (2018). Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. Journal of Biological Chemistry, 293, 12862-12876. https://doi.org/10.1074/jbc.RA117.001286.
Ofman, R., Ruiter, J. P. N., Feenstra, M., Duran, M., Poll-The, B. T., Zschocke, J., … Wanders, R. J. A. (2003). 2-Methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency is caused by mutations in the HADH2 gene. American Journal of Human Genetics, 72, 1300-1307. https://doi.org/10.1086/375116.
Olpin, S. E., Pollitt, R. J., McMenamin, J., Manning, N. J., Besley, G., Ruiter, J. P. N., & Wanders, R. J. A. (2002). 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency in a 23-year-old man. Journal of Inherited Metabolic Disease, 25, 477-482. https://doi.org/10.1023/A:1021251202287
Opara, J., Małecki, A., Małecka, E., & Socha, T. (2017). Motor assessment in Parkinson s disease. Annals of Agricultural and Environmental Medicine, 24, 411-415. https://doi.org/10.5604/12321966.1232774
Oppermann, U. C., Salim, S., Tjernberg, L. O., Terenius, L., & Jörnvall, H. (1999). Binding of amyloid beta-peptide to mitochondrial hydroxyacyl-CoA dehydrogenase (ERAB): Regulation of an SDR enzyme activity with implications for apoptosis in Alzheimer’s disease. FEBS Letters, 451, 238-242. https://doi.org/10.1016/S0014-5793(99)00586-4
Pagani, L., & Eckert, A. (2011). Amyloid-beta interaction with mitochondria. International Journal of Alzheimer's Disease, 2011, 925050. https://doi.org/10.4061/2011/925050
Palmisano, B. T., Zhu, L., & Stafford, J. M. (2017). Estrogens in the regulation of liver lipid metabolism. Advances in Experimental Medicine and Biology, 1043, 227-256. https://doi.org/10.1007/978-3-319-70178-3_12
Parker, W. D., Mahr, N. J., Filley, C. M., Parks, J. K., Hughes, D., Young, D. A., & Cullum, C. M. (1994). Reduced platelet cytochrome c oxidase activity in Alzheimer’s disease. Neurology, 44, 1086-1090. https://doi.org/10.1212/WNL.44.6.1086
Perez-Cerda, C., García-Villoria, J., Ofman, R., Sala, P. R., Merinero, B., Ramos, J., … Ribes, A. (2005). 2-Methyl-3-hydroxybutyryl-CoA dehydrogenase (MHBD) deficiency: An X-linked inborn error of isoleucine metabolism that may mimic a mitochondrial disease. Pediatric Research, 58, 488-491. https://doi.org/10.1203/01.pdr.0000176916.94328.cd.
Poll-The, B. T., Wanders, R. J. A., Ruiter, J. P. N., Ofman, R., Majoie, C. B. L. M., Barth, P. G., & Duran, M. (2004). Spastic diplegia and periventricular white matter abnormalities in 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency, a defect of isoleucine metabolism: Differential diagnosis with hypoxic-ischemic brain diseases. Molecular Genetics and Metabolism, 81, 295-299. https://doi.org/10.1016/j.ymgme.2003.11.013
Porcu, P., Barron, A. M., Frye, C. A., Walf, A. A., Yang, S.-Y., He, X.-Y., … Melcangi, R. C. (2016). Neurosteroidogenesis today: Novel targets for neuroactive steroid synthesis and action and their relevance for translational research. Journal of Neuroendocrinology, 28, 12351. https://doi.org/10.1111/jne.12351.
Powell, A., Read, J., Banfield, M., Gunn-Moore, F., Yan, S., Lustbader, J., … Brady, R. (2000). Recognition of structurally diverse substrates by type II 3-hydroxyacyl-CoA dehydrogenase (HADH II)/Amyloid-β binding alcohol dehydrogenase (ABAD). Journal of Molecular Biology, 303, 311-327. https://doi.org/10.1006/jmbi.2000.4139.
Pozzi, S., Benedusi, V., Maggi, A., & Vegeto, E. (2006). Estrogen Action in Neuroprotection and Brain Inflammation. Annals of the New York Academy of Sciences, 1089, 302-323. https://doi.org/10.1196/annals.1386.035
Rauschenberger, K., Schöler, K., Sass, J. O., Sauer, S., Djuric, Z., Rumig, C., … Zschocke, J. (2010). A non-enzymatic function of 17beta-hydroxysteroid dehydrogenase type 10 is required for mitochondrial integrity and cell survival. EMBO Molecular Medicine, 2, 51-62. https://doi.org/10.1002/emmm.200900055.
Rawłuszko, A. A., Horbacka, K., Krokowicz, P., & Jagodziński, P. P. (2011). Decreased expression of 17β-hydroxysteroid dehydrogenase type 1 is associated with DNA hypermethylation in colorectal cancer located in the proximal colon. BMC Cancer, 11, 522. https://doi.org/10.1186/1471-2407-11-522
Ren, Y., Xu, H. W., Davey, F., Taylor, M., Aiton, J., Coote, P., … Gunn-Moore, F. J. (2008). Endophilin I expression is increased in the brains of Alzheimer disease patients. Journal of Biological Chemistry, 283, 5685-5691. https://doi.org/10.1074/jbc.M707932200.
Reutens, A. T., & Begley, C. G. (2002). Endophilin-1: A multifunctional protein. International Journal of Biochemistry & Cell Biology, 34, 1173-1177. https://doi.org/10.1016/S1357-2725(02)00063-8
Richardson, A., Berry, G. T., Garganta, C., & Abbott, M.-A. (2017). Hydroxysteroid 17-beta dehydrogenase type 10 disease in siblings. JIMD Rep., 32, 25-32. https://doi.org/10.1007/8904_2016_547
Sahyouni, R., Verma, A., & Chen, J. (2016). Alzheimer’s Disease Decoded: The History, Present, and Future of Alzheimer’s Disease and Dementia. WORLD SCIENTIFIC. https://doi.org/10.1142/10023
Salas, S., Jézéquel, P., Campion, L., Deville, J.-L., Chibon, F., Bartoli, C., … Bouvier, C. (2009). Molecular characterization of the response to chemotherapy in conventional osteosarcomas: Predictive value of HSD17B10 and IFITM2. International Journal of Cancer, 125, 851-860. https://doi.org/10.1002/ijc.24457.
Sass, J. O., Forstner, R., & Sperl, W. (2004). 2-Methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency: Impaired catabolism of isoleucine presenting as neurodegenerative disease. Brain Dev., 26, 12-14. https://doi.org/10.1016/S0387-7604(03)00071-8
Savolainen-Peltonen, H., Rahkola-Soisalo, P., Hoti, F., Vattulainen, P., Gissler, M., Ylikorkala, O., & Mikkola, T. S. (2019). Use of postmenopausal hormone therapy and risk of Alzheimer’s disease in Finland: Nationwide case-control study. BMJ, 364, l665. https://doi.org/10.1136/bmj.l665
Sayre, L. M., Zelasko, D. A., Harris, P. L., Perry, G., Salomon, R. G., & Smith, M. A. (1997). 4-Hydroxynonenal-derived advanced lipid peroxidation end products are increased in Alzheimer’s disease. Journal of Neurochemistry, 68, 2092-2097. https://doi.org/10.1046/j.1471-4159.1997.68052092.x
Schmidt, M., Benek, O., Vinklarova, L., Hrabinova, M., Zemanova, L., Chribek, M., … Musilek, K. (2020). Benzothiazolyl ureas are low micromolar and uncompetitive inhibitors of 17β-HSD10 with implications to Alzheimer’s disease treatment. International Journal of Molecular Sciences, 21, 2059. https://doi.org/10.3390/ijms21062059.
Seaver, L. H., He, X.-Y., Abe, K., Cowan, T., Enns, G. M., Sweetman, L., … Yang, S.-Y. (2011). A novel mutation in the HSD17B10 gene of a 10-year-old boy with refractory epilepsy, choreoathetosis and learning disability. PLoS ONE, 6, e27348. https://doi.org/10.1371/journal.pone.0027348.
Shafqat, N., Marschall, H.-U., Filling, C., Nordling, E., Wu, X.-Q., Björk, L., … Oppermann, U. (2003). Expanded substrate screenings of human and Drosophila type 10 17beta-hydroxysteroid dehydrogenases (HSDs) reveal multiple specificities in bile acid and steroid hormone metabolism: Characterization of multifunctional 3alpha/7alpha/7beta/17beta/20beta/21-HSD. The Biochemical Journal, 376, 49-60. https://doi.org/10.1042/bj20030877.
Shumaker, S. A. (2004). Conjugated equine estrogens and incidence of probable dementia and mild cognitive impairment in postmenopausal womenWomen’s health initiative memory study. JAMA, 291, 2947. https://doi.org/10.1001/jama.291.24.2947
Sikka, P., Kapoor, S., Saxena, K., Bindra, V., & Jain, V. (2011). Blue cures blue but be cautious. Journal of Pharmacy and Bioallied Sciences, 3, 543. https://doi.org/10.4103/0975-7406.90112
Sutton, V. R., O’Brien, W. E., Clark, G. D., Kim, J., & Wanders, R. J. A. (2003). 3-Hydroxy-2-methylbutyryl-CoA dehydrogenase deficiency. Journal of Inherited Metabolic Disease, 26, 69-71. https://doi.org/10.1023/A:1024083715568
Takuma, K., Yao, J., Huang, J., Xu, H., Chen, X., Luddy, J., … Yan, S. S. (2005). ABAD enhances Abeta-induced cell stress via mitochondrial dysfunction. The FASEB journal: official publ. of the Federation of American Societies for Experimental Biology, 19, 597-598. https://doi.org/10.1096/fj.04-2582fje.
Tieu, K., Perier, C., Vila, M., Caspersen, C., Zhang, H.-P., Teismann, P., … Przedborski, S. (2004). L-3-hydroxyacyl-CoA dehydrogenase II protects in a model of Parkinson’s disease. Annals of Neurology, 56, 51-60. https://doi.org/10.1002/ana.20133.
Torroja, L., Ortuño-Sahagún, D., Ferrús, A., Hämmerle, B., & Barbas, J. A. (1998). scully, an essential gene of drosophila, is homologous to mammalian mitochondrial type II l-3-hydroxyacyl-CoA dehydrogenase/amyloid-β peptide-binding protein. Journal of Cell Biology, 141, 1009-1017. https://doi.org/10.1083/jcb.141.4.1009
Väänänen, H. K., & Härkönen, P. L. (1996). Estrogen and bone metabolism. Maturitas, 23(Suppl), S65-69. https://doi.org/10.1016/0378-5122(96)01015-8
Valaasani, K. R., Sun, Q., Hu, G., Li, J., Du, F., Guo, Y., … Yan, S. S. (2014). Identification of human ABAD inhibitors for rescuing Aβ-mediated mitochondrial dysfunction. Current Alzheimer Research, 11, 128-136. https://doi.org/10.2174/1567205011666140130150108.
Valasani, K. R., Hu, G., Chaney, M. O., & Yan, S. S. (2013). Structure-based design and synthesis of benzothiazole phosphonate analogues with inhibitors of human ABAD-Aβ for treatment of Alzheimer’s disease. Chemical Biology & Drug Design, 81, 238-249. https://doi.org/10.1111/cbdd.12068
Van Bulck, M., Sierra-Magro, A., Alarcon-Gil, J., Perez-Castillo, A., & Morales-Garcia, J. A. (2019). Novel approaches for the treatment of Alzheimer’s and Parkinson’s disease. International Journal of Molecular Sciences, 20, 719. https://doi.org/10.3390/ijms20030719
van der Spuy, W. J., & Pretorius, E. (2012). Interrelation between inflammation, thrombosis, and neuroprotection in cerebral ischemia. Reviews in the Neurosciences, 23, 269-278. https://doi.org/10.1515/revneuro-2012-0028
Vangavaragu, J. R., Valasani, K. R., Fang, D., Williams, T. D., & Yan, S. S. (2014). Determination of small molecule ABAD inhibitors crossing blood-brain barrier and pharmacokinetics. J. Alzheimers Dis. JAD, 42, 333-344. https://doi.org/10.3233/JAD-140252
Vilardo, E., Nachbagauer, C., Buzet, A., Taschner, A., Holzmann, J., & Rossmanith, W. (2012). A subcomplex of human mitochondrial RNase P is a bifunctional methyltransferase-extensive moonlighting in mitochondrial tRNA biogenesis. Nucleic Acids Research, 40, 11583-11593. https://doi.org/10.1093/nar/gks910
Vilardo, E., & Rossmanith, W. (2013). The amyloid-β-SDR5C1(ABAD) interaction does not mediate a specific inhibition of mitochondrial RNase P. PLoS ONE, 8, e65609. https://doi.org/10.1371/journal.pone.0065609
Vilardo, E., & Rossmanith, W. (2015). Molecular insights into HSD10 disease: Impact of SDR5C1 mutations on the human mitochondrial RNase P complex. Nucleic Acids Research, 43, 6649. https://doi.org/10.1093/nar/gkv658
Viswanath, A. N. I., Kim, T., Jung, S. Y., Lim, S. M., & Pae, A. N. (2017). In silico-designed novel non-peptidic ABAD LD hot spot mimetics reverse Aβ-induced mitochondrial impairments in vitro. Chemical Biology & Drug Design, 90, 1041-1055. https://doi.org/10.1111/cbdd.13065
Vos, T., Allen, C., Arora, M., Barber, R. M., Bhutta, Z. A., Brown, A., … Murray, C. J. L. (2016). Global, regional, and national incidence, prevalence, and years lived with disability for 310 diseases and injuries, 1990-2015: A systematic analysis for the Global Burden of Disease Study 2015. The Lancet, 388, 1545-1602. https://doi.org/10.1016/S0140-6736(16)31678-6
Wang, H., Carlier, P. R., Ho, W. L., Wu, D. C., Lee, N. T. K., Li, C. P. L., … Han, Y. F. (1999). Effects of bis(7)-tacrine, a novel anti-Alzheimerʼs agent, on rat brain AChE. NeuroReport, 10, 789-793. https://doi.org/10.1097/00001756-199903170-00023.
Wang, J.-S., Zhu, H.-J., Markowitz, J. S., Donovan, J. L., Yuan, H.-J., & Devane, C. L. (2008). Antipsychotic drugs inhibit the function of breast cancer resistance protein. Basic & Clinical Pharmacology & Toxicology, 103, 336-341. https://doi.org/10.1111/j.1742-7843.2008.00298.x
Waters, P. J., Lace, B., Buhas, D., Gravel, S., Cyr, D., Boucher, R.-M., … Maranda, B. (2019). HSD10 mitochondrial disease: P.Leu122Val variant, mild clinical phenotype, and founder effect in French-Canadian patients from Quebec. Molecular Genetics & Genomic Medicine, 7, e1000. https://doi.org/10.1002/mgg3.1000.
Williams, T. I., Lynn, B. C., Markesbery, W. R., & Lovell, M. A. (2006). Increased levels of 4-hydroxynonenal and acrolein, neurotoxic markers of lipid peroxidation, in the brain in Mild Cognitive Impairment and early Alzheimer’s disease. Neurobiology of Aging, 27, 1094-1099. https://doi.org/10.1016/j.neurobiolaging.2005.06.004
Wischik, C. M., Staff, R. T., Wischik, D. J., Bentham, P., Murray, A. D., Storey, J. M. D., Kook, K. A., Harrington, C. R. (2015). Tau Aggregation inhibitor therapy: An exploratory phase 2 study in mild or moderate Alzheimer’s disease. Journal of Alzheimer's Disease, 44, 705-720. https://doi.org/10.3233/JAD-142874
Wolfe, M. S. ed (2017) Alzheimer’s Disease II, Vol. 24: Topics in Medicinal Chemistry. Springer International Publishing, Cham. https://doi.org/10.1007/978-3-319-59460-6
Xie, Y., Deng, S., Chen, Z., Yan, S., & Landry, D. W. (2006). Identification of small-molecule inhibitors of the Abeta-ABAD interaction. Bioorganic & Medicinal Chemistry Letters, 16, 4657-4660. https://doi.org/10.1016/j.bmcl.2006.05.099
Xu, H., Gouras, G. K., Greenfield, J. P., Vincent, B., Naslund, J., Mazzarelli, L., … Gandy, S. (1998). Estrogen reduces neuronal generation of Alzheimer beta-amyloid peptides. Nature Medicine, 4, 447-451. https://doi.org/10.1038/nm0498-447.
Yan, S. D., Fu, J., Soto, C., Chen, X., Zhu, H., Al-Mohanna, F., … Stern, D. (1997). An intracellular protein that binds amyloid-beta peptide and mediates neurotoxicity in Alzheimer’s disease. Nature, 389, 689-695. https://doi.org/10.1038/39522.
Yan, S. D., Shi, Y., Zhu, A., Fu, J., Zhu, H., Zhu, Y., … Stern, D. M. (1999). Role of ERAB/L-3-hydroxyacyl-coenzyme A dehydrogenase type II activity in Abeta-induced cytotoxicity. Journal of Biological Chemistry, 274, 2145-2156. https://doi.org/10.1074/jbc.274.4.2145.
Yan, Y., Liu, Y., Sorci, M., Belfort, G., Lustbader, J. W., Yan, S. S., & Wang, C. (2007). Surface plasmon resonance and nuclear magnetic resonance studies of ABAD-Abeta interaction. Biochemistry, 46, 1724-1731. https://doi.org/10.1021/bi061314n
Yang, S.-Y., Dobkin, C., He, X.-Y., Philipp, M., & Brown, W. T. (2013). A 5-methylcytosine hotspot responsible for the prevalent HSD17B10 mutation. Gene, 515, 380-384. https://doi.org/10.1016/j.gene.2012.12.064
Yang, S. Y., & He, X. Y. (2001). Role of type 10 17beta-hydroxysteroid dehydrogenase in the pathogenesis of Alzheimer’s disease. Advances in Experimental Medicine and Biology, 487, 101-110. https://doi.org/10.1007/978-1-4615-1249-3_8
Yang, S.-Y., He, X.-Y., Isaacs, C., Dobkin, C., Miller, D., & Philipp, M. (2014). Roles of 17β-hydroxysteroid dehydrogenase type 10 in neurodegenerative disorders. Journal of Steroid Biochemistry and Molecular Biology, 143, 460-472. https://doi.org/10.1016/j.jsbmb.2014.07.001
Yang, S.-Y., He, X.-Y., & Miller, D. (2007a). HSD17B10: A gene involved in cognitive function through metabolism of isoleucine and neuroactive steroids. Molecular Genetics and Metabolism, 92, 36-42. https://doi.org/10.1016/j.ymgme.2007.06.001
Yang, S.-Y., He, X.-Y., & Miller, D. (2011). Hydroxysteroid (17β) dehydrogenase X in human health and disease. Molecular and Cellular Endocrinology, 343, 1-6. https://doi.org/10.1016/j.mce.2011.06.011
Yang, S.-Y., He, X.-Y., Olpin, S. E., Sutton, V. R., McMenamin, J., Philipp, M., … Malik, M. (2009). Mental retardation linked to mutations in the HSD17B10 gene interfering with neurosteroid and isoleucine metabolism. Proceedings of the National Academy of Sciences of the United States of America, 106, 14820-14824. https://doi.org/10.1073/pnas.0902377106.
Yang, S.-Y., He, X.-Y., & Schulz, H. (2005). Multiple functions of type 10 17β-hydroxysteroid dehydrogenase. Trends in Endocrinology and Metabolism, 16, 167-175. https://doi.org/10.1016/j.tem.2005.03.006
Yang, X., Yang, Y., Wu, J., & Zhu, J. (2007b). Stable expression of a novel fusion peptide of thioredoxin-1 and ABAD-inhibiting peptide protects PC12 cells from intracellular amyloid-beta. Journal of Molecular Neuroscience, 33, 180-188. https://doi.org/10.1007/s12031-007-0063-y
Yao, J., Du, H., Yan, S., Fang, F., Wang, C., Lue, L.-F., … J., Arancio, O., Yan, S. S., (2011). Inhibition of amyloid-beta (Abeta) peptide-binding alcohol dehydrogenase-a interaction reduces a accumulation and improves mitochondrial function in a mouse model of Alzheimer’s disease. Journal of Neuroscience, 31, 2313-2320. https://doi.org/10.1523/JNEUROSCI.4717-10.2011.
Yao, J., Taylor, M., Davey, F., Ren, Y., Aiton, J., Coote, P., … Gunn-Moore, F. J. (2007). Interaction of amyloid binding alcohol dehydrogenase/Abeta mediates up-regulation of peroxiredoxin II in the brains of Alzheimer’s disease patients and a transgenic Alzheimer’s disease mouse model. Molecular and Cellular Neurosciences, 35, 377-382. https://doi.org/10.1016/j.mcn.2007.03.013.
Yu, Q., Wang, Y., Du, F., Yan, S., Hu, G., Origlia, N., … Yan, S. S. (2018). Overexpression of endophilin A1 exacerbates synaptic alterations in a mouse model of Alzheimer’s disease. Nature Communications, 9, 1-14. https://doi.org/10.1038/s41467-018-04389-0.
Zakaria, A., Hamdi, N., & Abdel-Kader, R. M. (2016). Methylene blue improves brain mitochondrial ABAD functions and decreases Aβ in a neuroinflammatory Alzheimer’s Disease mouse model. Molecular Neurobiology, 53, 1220-1228. https://doi.org/10.1007/s12035-014-9088-8
Zhang, C.-Y., Chen, J., Yin, D.-C., & Lin, S.-X. (2012). The contribution of 17beta-hydroxysteroid dehydrogenase type 1 to the estradiol-estrone ratio in estrogen-sensitive breast cancer cells. PLoS ONE, 7, e29835. https://doi.org/10.1371/journal.pone.0029835
Zschocke, J. (2012). HSD10 disease: Clinical consequences of mutations in the HSD17B10 gene. Journal of Inherited Metabolic Disease, 35, 81-89. https://doi.org/10.1007/s10545-011-9415-4
Zschocke, J., Ruiter, J. P. N., Brand, J., Lindner, M., Hoffmann, G. F., Wanders, R. J. A., & Mayatepek, E. (2000). Progressive infantile neurodegeneration caused by 2-Methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency: A novel inborn error of branched-chain fatty acid and isoleucine metabolism. Pediatric Research, 48, 852-855. https://doi.org/10.1203/00006450-200012000-00025
C-3 Steroidal Hemiesters as Inhibitors of 17β-Hydroxysteroid Dehydrogenase Type 10
Nanomolar Benzothiazole-Based Inhibitors of 17β-HSD10 with Cellular Bioactivity