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Article type: Research Article
Authors: He, Xue-Yinga | Isaacs, Charlesa | Yang, Song-Yua; b; *
Affiliations: [a] Department of Developmental Biochemistry, NYS Institute for Basic Research in Developmental Disabilities, Staten Island, NY, USA | [b] PhD Program in Biology–Neuroscience, Graduate Center of the City University of New York, New York, NY, USA
Correspondence: [*] Correspondence to: Song-Yu Yang, MD, PhD, Department of Developmental Biochemistry, NYS Institute for Basic Research in Developmental Disabilities, Staten Island, NY 10314, USA. Tel.: +1 718 494 5317; Fax: +1 718 698 7916; E-mail: [email protected].
Abstract: 17β-Hydroxysteroid dehydrogenase type 10 is a multifunctional, homotetrameric, mitochondrial protein encoded by the HSD17B10 gene at Xp 11.2. This protein, 17β-HSD10, is overexpressed in brain cells of Alzheimer’s disease (AD) patients. It was reported to be involved in AD pathogenesis as the endoplasmic reticulum-associated amyloid-β binding protein (ERAB) and as amyloid-β binding alcohol dehydrogenase (ABAD). However, the exaggerated catalytic efficiencies for ERAB/ABAD in these reports necessitated the re-characterization of the catalytic functions of this brain enzyme. In addition to isoleucine metabolism, 17β-HSD10 is also responsible for the mitochondrial metabolism of neurosteroids such as 5α-androstane-3α,17β-diol and 17β-estradiol. These neurosteroids are inactivated by the oxidation catalyzed by 17β-HSD10. Since neurosteroid homeostasis is presumably essential for cognitive function, analysis of the impact of 17β-HSD10 and its inhibitor, amyloid-β peptide (Aβ), on the metabolism of neuroactive steroids offers a new approach to AD pathogenesis.
Keywords: Data integrity, mitochondria, neurosteroid, short chain 3-hydroxyacyl-CoA dehydrogenase, steroidogenesis
DOI: 10.3233/JAD-170974
Journal: Journal of Alzheimer's Disease, vol. 62, no. 2, pp. 665-673, 2018
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