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Roles of Type 10 17β-Hydroxysteroid Dehydrogenase in Health and Disease
by
Xue-Ying He
Xue-Ying He 1,
Janusz Frackowiak
Janusz Frackowiak 2
and
Song-Yu Yang
Song-Yu Yang 1,3,*
1
Department of Molecular Biology, NYS Institute for Basic Research in Developmental Disabilities, Staten Island, NY 10314, USA
2
Department of Developmental Neurobiology, NYS Institute for Basic Research in Developmental Disabilities, Staten Island, NY 10314, USA
3
Ph.D. Program in Biology-Neuroscience, Graduate Center, The City University of New York, New York, NY 10016, USA
*
Author to whom correspondence should be addressed.
J. Pers. Med. 2025, 15(8), 346; https://doi.org/10.3390/jpm15080346 (registering DOI)
Submission received: 1 May 2025
/
Revised: 12 June 2025
/
Accepted: 13 July 2025
/
Published: 1 August 2025
Abstract
Type 10 17β-hydroxysteroid dehydrogenase (17β-HSD10) is the HSD17B10 gene product. It plays an appreciable part in the carcinogenesis and pathogenesis of neurodegeneration, such as Alzheimer’s disease and infantile neurodegeneration. This mitochondrial, homo-tetrameric protein is a central hub in various metabolic pathways, e.g., branched-chain amino acid degradation and neurosteroid metabolism. It can bind to other proteins carrying out diverse physiological functions, e.g., tRNA maturation. It has also previously been proposed to be an Aβ-binding alcohol dehydrogenase (ABAD) or endoplasmic reticulum-associated Aβ-binding protein (ERAB), although those reports are controversial due to data analyses. For example, the reported km value of some substrate of ABAD/ERAB was five times higher than its natural solubility in the assay employed to measure km. Regarding any reported “one-site competitive inhibition” of ABAD/ERAB by Aβ, the kivalue estimations were likely impacted by non-physiological concentrations of 2-octanol at high concentrations of vehicle DMSO and, therefore, are likely artefactual. Certain data associated with ABAD/ERAB were found not reproducible, and multiple experimental approaches were undertaken under non-physiological conditions. In contrast, 17β-HSD10 studies prompted a conclusion that Aβ inhibited 17β-HSD10 activity, thus harming brain cells, replacing a prior supposition that “ABAD” mediates Aβ neurotoxicity. Furthermore, it is critical to find answers to the question as to why elevated levels of 17β-HSD10, in addition to Aβ and phosphorylated Tau, are present in the brains of AD patients and mouse AD models. Addressing this question will likely prompt better approaches to develop treatments for Alzheimer’s disease.
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MDPI and ACS Style
He, X.-Y.; Frackowiak, J.; Yang, S.-Y.
Roles of Type 10 17β-Hydroxysteroid Dehydrogenase in Health and Disease. J. Pers. Med. 2025, 15, 346.
https://doi.org/10.3390/jpm15080346
AMA Style
He X-Y, Frackowiak J, Yang S-Y.
Roles of Type 10 17β-Hydroxysteroid Dehydrogenase in Health and Disease. Journal of Personalized Medicine. 2025; 15(8):346.
https://doi.org/10.3390/jpm15080346
Chicago/Turabian Style
He, Xue-Ying, Janusz Frackowiak, and Song-Yu Yang.
2025. "Roles of Type 10 17β-Hydroxysteroid Dehydrogenase in Health and Disease" Journal of Personalized Medicine 15, no. 8: 346.
https://doi.org/10.3390/jpm15080346
APA Style
He, X.-Y., Frackowiak, J., & Yang, S.-Y.
(2025). Roles of Type 10 17β-Hydroxysteroid Dehydrogenase in Health and Disease. Journal of Personalized Medicine, 15(8), 346.
https://doi.org/10.3390/jpm15080346
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