Identification of the Major Oxidative 3α-Hydroxysteroid Dehydrogenase in Human Prostate That Converts 5α-Androstane-3α,17β-diol to 5α-Dihydrotestosterone: A Potential Therapeutic Target for Androgen-Dependent Disease
Open accessAbstract
Androgen-dependent prostate diseases initially require 5alpha-dihydrotestosterone (DHT) for growth. The DHT product 5alpha-androstane-3alpha,17beta-diol (3alpha-diol), is inactive at the androgen receptor (AR), but induces prostate growth, suggesting that an oxidative 3alpha-hydroxysteroid dehydrogenase (HSD) exists. Candidate enzymes that posses 3alpha-HSD activity are type 3 3alpha-HSD (AKR1C2), 11-cis retinol dehydrogenase (RODH 5), L-3-hydroxyacyl coenzyme A dehydrogenase , RODH like 3alpha-HSD (RL-HSD), novel type of human microsomal 3alpha-HSD, and retinol dehydrogenase 4 (RODH 4). In mammalian transfection studies all enzymes except AKR1C2 oxidized 3alpha-diol back to DHT where RODH 5, RODH 4, and RL-HSD were the most efficient. AKR1C2 catalyzed the reduction of DHT to 3alpha-diol, suggesting that its role is to eliminate DHT. Steady-state kinetic parameters indicated that RODH 4 and RL-HSD were high-affinity, low-capacity enzymes whereas RODH 5 was a low-affinity, high-capacity enzyme. AR-dependent reporter gene assays showed that RL-HSD, RODH 5, and RODH 4 shifted the dose-response curve for 3alpha-diol a 100-fold, yielding EC(50) values of 2.5 x 10(-9) M, 1.5 x 10(-9) M, and 1.0 x 10(-9) M, respectively, when compared with the empty vector (EC(50) = 1.9 x 10(-7) M). Real-time RT-PCR indicated that L-3-hydroxyacyl coenzyme A dehydrogenase and RL-HSD were expressed more than 15-fold higher compared with the other candidate oxidative enzymes in human prostate and that RL-HSD and AR were colocalized in primary prostate stromal cells. The data show that the major oxidative 3alpha-HSD in normal human prostate is RL-HSD and may be a new therapeutic target for treating prostate diseases.
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The reverse oxidation of 3α-Diol to 5α-DHT is catalyzed mainly by HSD17B6, also called SDR9C6.
“The reverse reaction, which involves oxidation of 3α-Diol to 5α-DHT is catalyzed by the SDR members, mainly HSD17B6 also designated as SDR9C6”
From Role of aldo-keto reductase family 1 (AKR1) enzymes in human steroid metabolism (2014) · cites this paper as [48]
Androsterone can be reactivated by sequential 17β-reduction and 3α-oxidase reactions.
“Androsterone, considered an inactive metabolite of DHT under normal circumstances, can then be reactivated by the sequential 17β-reduction and 3α-oxidase reactions [[63], [64], [65]].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [65]
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- Authors
- Bauman, D. R., Steckelbroeck, S., Williams, M. V., Peehl, D. M., & Penning, T. M.
- Affiliations
- University of Pennsylvania (US)
- Stanford Medicine (US)
- Corresponding author
- Penning, Trevor M.
- Venue
- Molecular Endocrinology
- Publisher
- The Endocrine Society
- Published
- 2006-02-01
- Volume
- 20
- Issue
- 2
- Pages
- 444-458
- ISSN
- 0888-8809 (ISSN-L)
- 1944-9917
- OpenAlex
- W2069335278
- Cited by
- 120
- References
- 59
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 1 · 2023: 6 · 2022: 3 · 2021: 2 · 2020: 6 · 2019: 9 · 2018: 4 · 2017: 5 · 2016: 7 · 2015: 6 · 2014: 9 · 2013: 12 · 2012: 6
- FWCI
- 4.00
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Endocrinology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Defense
- University of Pennsylvania
- National Institutes of Health
- National Cancer Institute (R01 CA 90744, 1R25-CA-10187-D1, R01CA090744)
- National Institute of Environmental Health Sciences (P30ES013508)
- Topics
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Prostate Cancer Treatment and Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Steroid Chemistry and Biochemistry
- Health Sciences › Medicine › Urology › Urinary Bladder and Prostate Research
- Keywords
- dihydrotestosterone, 5α-androstane-3α,17β-diol, 3alpha-diol, androgen receptor, prostate stromal cells, AKR1C2, enzyme kinetics, therapeutic target, enzyme colocalization
- MeSH terms
- Androgens, Animals, Cells, Cultured, Humans, Male, NADH, NADPH Oxidoreductases, Prostate, Prostatic Diseases, Receptors, Androgen, Dihydrotestosterone, Transfection, Androstane-3,17-diol, Transcriptional Activation, 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific), Fatty Acid Synthases
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