期刊
MOLECULAR AND CELLULAR ENDOCRINOLOGY
卷 265, 期 -, 页码 77-82出版社
ELSEVIER IRELAND LTD
DOI: 10.1016/j.mce.2006.12.007
关键词
aldo-keto reductase; short-chain dehydrogenase/reductase; 3 alpha-androstanediol; prostate disease
资金
- NCI NIH HHS [R01 CA090744, R01 CA-90744] Funding Source: Medline
- NIDDK NIH HHS [R01 DK047015, R01 DK47015] Funding Source: Medline
- NIEHS NIH HHS [P30 ES013508, P30-ES013508] Funding Source: Medline
Pairs of hydroxysteroid dehydrogenases (HSDs) govern ligand access to steroid receptors in target tissues and act as molecular switches. By acting as reductases or oxidases, HSDs convert potent ligands into their cognate inactive metabolites or vice versa. This pre-receptor regulation of steroid hormone action may have profound effects on hormonal response. We have identified the HSDs responsible for regulating ligand access to the androgen receptor (AR) in human prostate. Type 3 3 alpha-hydroxysteroid dehydrogenase (aldo-keto reductase 1C2) acts solely as a reductase to convert 5 alpha-dihydrotestosterone (DHT), a potent ligand for the AR (K-d = 10(-11) M for the AR), to the inactive androgen 3 alpha-androstanediol (K-d = 10(-6) M for the AR); while RoDH like 3 alpha-HSD (a short-chain dehydrogenase/reductase (SDR)) acts solely as an oxidase to convert 3 alpha-androstanediol back to 5 alpha-DHT. Our studies suggest that aldo-keto reductase (AKRs) and SDRs function as reductases and oxidases, respectively, to control ligand access to nuclear receptors. (c) 2006 Elsevier Ireland Ltd. All rights reserved.
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