Cited by 235Pharmacogenetics and Drug MetabolismProstate Cancer Treatment and ResearchDrug Transport and Resistance Mechanisms

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Inactivation of androgens by UDP-glucuronosyltransferase enzymes in humans

Bélanger, Alain, Pelletier, Georges, Labrie, Fernand, Barbier, Olivier, Chouinard, Sarah·2003·Trends in Endocrinology & Metabolism

DOI 10.1016/j.tem.2003.10.005

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Abstract

In humans, 3beta-hydroxysteroid dehydrogenase (3beta-HSD), 17beta-HSD and 5alpha-reductase activities in androgen target tissues, such as the prostate and skin, convert dehydroepiandrosterone, androstenedione and testosterone into the most potent natural androgen dihydrotestosterone (DHT). This androgen is converted mainly in situ into two phase I metabolites, androsterone (ADT) and androstane-3alpha,17beta-diol (3alpha-DIOL), which might be back converted to DHT. Here, we discuss the recent findings regarding the characterization of specific UDP-glucuronosyltransferases (UGTs), UGT2B7, B15 and B17, responsible for the glucuronidation of these metabolites. The tissue distribution and cellular localization of the UGT2B transcripts and proteins in humans clearly indicate that these enzymes are synthesized in androgen-sensitive tissues. It is postulated that the conjugating activity of UGT enzymes is the main mechanism for modulating the action of steroids and protecting the androgen-sensitive tissues from deleteriously high concentrations of DHT, ADT and 3alpha-DIOL.

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Turgeon, 2001, Relative enzymatic activity, protein stability and tissue distribution of human steroid metabolizing UGT2B subfamily members, Endocrinology, 142, 778, 10.1210/en.142.2.778 · DOI · Paper page

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Authors: Bélanger, A., Pelletier, G., Labrie, F., Barbier, O., & Chouinard, S.
Affiliations: Centre hospitalier de l'Université Laval (CA)
Corresponding author: Bélanger, Alain
ORCID: Barbier, Olivier
Venue: Trends in Endocrinology & Metabolism
Publisher: Elsevier BV
Published: 2003-12
Volume: 14
Issue: 10
Pages: 473-479
ISSN: 1043-2760 (ISSN-L)
DOI: 10.1016/j.tem.2003.10.005
OpenAlex: W1988871942
Cited by: 235
References: 74
Citations by year: 2026: 2 · 2025: 5 · 2024: 8 · 2023: 5 · 2022: 12 · 2021: 9 · 2020: 8 · 2019: 8 · 2018: 8 · 2017: 17 · 2016: 11 · 2015: 13 · 2014: 11 · 2013: 18 · 2012: 8
FWCI: 0.66
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Trends in Endocrinology and Metabolism (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Prostate Cancer Treatment and Research
Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
Keywords: androgen metabolism, UDP-glucuronosyltransferase, UGT2B7, UGT2B15, UGT2B17, dihydrotestosterone, androstanediol, androstanediol glucuronide, glucuronidation, 3β-hydroxysteroid dehydrogenase, 17β-hydroxysteroid dehydrogenase, 5α-reductase, prostate, skin
MeSH terms: Androgens, Humans, Isoenzymes, Male, Prostate, Prostatic Neoplasms, Skin, Glucuronosyltransferase

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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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Inactivation of androgens by UDP-glucuronosyltransferase enzymes in humans

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks