Characterization of Chinese hamster ovary cell lines expressing human steroid 5 alpha-reductase isozymes
Open accessAbstract
Membrane-bound isozymes of steroid 5 alpha-reductase, designated 1 and 2, synthesize the potent androgen, dihydrotestosterone. Isozyme 1 has an alkaline pH optimum (7.0-8.5), whereas isozyme 2 has an acidic pH optimum (5.0). To gain insight into this enigmatic difference, Chinese hamster ovarian cell lines expressing the human 5 alpha-reductase isozymes were established. The half-lives of both proteins are > 30 h and are not altered by the 4-azasteroid inhibitors finasteride and 17 beta-(N,N,-diethyl)carbamoyl-4-methyl-4-aza-5 alpha-androstan-3-one. Nanomolar concentrations of finasteride block immunoprecipitation of isozyme 2 by antipeptide antibodies, which suggests that drug binding alters protein conformation. In contrast, finasteride (50 microM) has no effect on immunoprecipitation of isozyme 1. Both isozymes are localized to the endoplasmic reticulum by immunocytochemistry and have their carboxyl termini exposed to the cytoplasm. In cell lysates, isozyme 2 exhibits a Vmax at pH 5.0 but has a higher substrate affinity at neutral pH. In intact and permeabilized cells, isozyme 2 has an apparent substrate Km similar to that determined in cell lysates at neutral pH. The results suggest that isozyme 2 is more efficient at neutral pH and that the acidic pH optimum determined in lysates is a consequence of cell lysis.
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SRD5A1 catalyzes 5α-reduction of A4 more efficiently than that of testosterone.
“Indeed, the enzyme steroid 5α-reductase 1 (SRD5A1) catalyzes the 5α-reduction of A4 more efficiently than that of testosterone [56,57].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [56]
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Subcellular localization of the five members of the human steroid 5α-reductase family
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- Authors
- Thigpen, A. E., Cala, K. M., & Russell, D. W.
- Affiliations
- The University of Texas Southwestern Medical Center (US)
- ORCID
- Russell, D.W.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-08
- Volume
- 268
- Issue
- 23
- Pages
- 17404-17412
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1487396242
- Cited by
- 152
- References
- 1
- Citations by year
- 2026: 3 · 2024: 3 · 2021: 4 · 2020: 3 · 2019: 3 · 2018: 3 · 2017: 4 · 2016: 2 · 2015: 2 · 2014: 4 · 2013: 7 · 2012: 3
- FWCI
- 9.89
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01gm043753-07)
- National Institute of General Medical Sciences (GM-43753)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD 07504)
- Topics
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Prostate Cancer Treatment and Research
- Health Sciences › Medicine › Urology › Urinary Bladder and Prostate Research
- Health Sciences › Medicine › Reproductive Medicine › Sperm and Testicular Function
- Keywords
- 5α-reductase, dihydrotestosterone, pH optimum, endoplasmic reticulum localization, finasteride, protein conformation, substrate affinity, protein half-life, androgen production
- MeSH terms
- Androstenes, Animals, Azasteroids, Cell Membrane Permeability, Fluorescent Antibody Technique, Cricetinae, Humans, Hydrogen-Ion Concentration, Isoenzymes, Kinetics, Precipitin Tests, Protein Conformation, 3-Oxo-5-alpha-Steroid 4-Dehydrogenase, Transfection, CHO Cells, Finasteride, 5-alpha Reductase Inhibitors
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