Cited by 53Hair Growth and DisordersProstate Cancer Treatment and ResearchHormonal and reproductive studies

Cations Inhibit Specifically Type I 5α-Reductase Found in Human Skin

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Sugimoto, Yasuro, López-Solache, Irma, Labrie, Fernand, Luu-The, V.a.n.·1995·Journal of Investigative Dermatology

Abstract

Steroid 5 alpha-reductase catalyzes the reduction of testosterone into the very potent androgen dihydrotestosterone. Previously, we showed that human type I 5 alpha-reductase is expressed mainly in the skin, whereas a type II 5 alpha-reductase is more specifically expressed in the prostate. To assess the possible differential effects of various cations on the two types of 5 alpha-reductase, we constructed expression vectors and transfected them into SW-13 cells, a human adrenal carcinoma cell line containing negligible endogenous 5 alpha-reductase activity. The expressed 5 alpha-reductases were analyzed for their sensitivity to Li, Ca, Cd, Cu, Mg, Mn, Ni, Zn, and Fe. The results showed that type I 5 alpha-reductase was strongly inhibited by Cd, Cu, and Zn and moderately inhibited by Ni and Fe, with 50% inhibitory concentration values of 0.9, 1.9, 2.0, 169.2, and 174.3 microM, respectively. In contrast, type II 5 alpha-reductase activity was inhibited only by Cu, with a 50% inhibitory concentration value of 19.2 microM. The data showed that cations could specifically control 5 alpha-reductase activity expression, which is more strongly inhibited in a target tissue, especially the skin.

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Crossref · 10.1111/1523-1747.ep12606985

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25 of 25 references verified0 citation errors · 0 not checkable

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  • The presence of SRD5A1 allows for local production of DHT, with the 5α-dione pathway bypassing T being the preferred route.

    “The presence of SRD5A1 allows for the local production of DHT (Luu-The et al., 1994), with the 5α-dione pathway bypassing T being the preferred route (Samson et al., 2010, Sugimoto et al., 1995) (Fig. 6).”

    From Intracrine androgen biosynthesis, metabolism and action revisited (2018) · cites this paper as Sugimoto et al., 1995

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Authors
Sugimoto, Y., López-Solache, I., Labrie, F., & Luu-The, V. A. N.
Affiliations
  • Centre de recherche du CHU de Québec-Université Laval (CA)
  • Université Laval (CA)
Venue
Journal of Investigative Dermatology
Publisher
Elsevier BV
Published
1995-05
Volume
104
Issue
5
Pages
775-778
ISSN
0022-202X (ISSN-L)
OpenAlex
W1971835761
Cited by
53
References
25
Citations by year
2026: 2 · 2025: 2 · 2022: 3 · 2021: 2 · 2020: 1 · 2019: 2 · 2018: 4 · 2017: 2 · 2016: 2 · 2015: 1 · 2014: 1 · 2013: 2
FWCI
0.96
Type
journal article
Language
en
Open access
Locations
  • Journal of Investigative Dermatology (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Urology › Hair Growth and Disorders
  • Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Prostate Cancer Treatment and Research
  • Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Hormonal and reproductive studies
Keywords
cation inhibition, dihydrotestosterone, testosterone suppression, human skin, metal ions, cadmium, copper, zinc, enzyme inhibition, SW13 cells, enzyme expression
MeSH terms
Anions, Base Sequence, Cadmium, Cations, Copper, Humans, Hydrogen-Ion Concentration, Iron, Molecular Sequence Data, Nickel, Skin, 3-Oxo-5-alpha-Steroid 4-Dehydrogenase, Transfection, Tumor Cells, Cultured, Zinc, 5-alpha Reductase Inhibitors

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