UDP-glucuronosyltransferase 2B15 (UGT2B15) and UGT2B17 enzymes are major determinants of the androgen response in prostate cancer LNCaP cells
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Uridine diphosphate-glucuronosyltransferase 2 (UGT2)B15 and B17 enzymes conjugate dihydrotestosterone (DHT) and its metabolites androstane-3alpha, 17beta-diol (3alpha-DIOL) and androsterone (ADT). The presence of UGT2B15/B17 in the epithelial cells of the human prostate has been clearly demonstrated, and significant 3alpha-DIOL glucuronide and ADT-glucuronide concentrations have been detected in this tissue. The human androgen-dependent cancer cell line, LNCaP, expresses UGT2B15 and -B17 and is also capable of conjugating androgens. To assess the impact of these two genes in the inactivation of androgens in LNCaP cells, their expression was inhibited using RNA interference. The efficient inhibitory effects of a UGT2B15/B17 small interfering RNA (siRNA) probe was established by the 70% reduction of these UGT mRNA levels, which was further confirmed at the protein levels. The glucuronidation of dihydrotestosterone (DHT), 3alpha-DIOL, and ADT by LNCaP cell homogenates was reduced by more than 75% in UGT2B15/B17 siRNA-transfected LNCaP cells when compared with cells transfected with a non-target probe. In UGT2B15/B17-deficient LNCaP cells, we observe a stronger response to DHT than in control cells, as determined by cell proliferation and expression of eight known androgen-sensitive genes. As expected, the amounts of DHT in cell culture media from control cells were significantly lower than that from UGT2B15/B17 siRNA-treated cells, which was caused by a higher conversion to its corresponding glucuronide derivative. Taken together these data support the idea that UGT2B15 and -B17 are critical enzymes for the local inactivation of androgens and that glucuronidation is a major determinant of androgen action in prostate cells.
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Glucuronidation of 3α-adiol is of particular importance for androgen inactivation and regulation of cancer progression because prostate cancer cells can convert 3α-adiol back to DHT.
“Because of the ability of prostate cancer cells to convert 3α-adiol back to DHT its glucuronidation is of particular importance for androgen inactivation and the regulation of cancer progression (Chouinard et al., 2007).”
From Intracrine androgen biosynthesis, metabolism and action revisited (2018) · cites this paper as Chouinard et al., 2007
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- Authors
- Chouinard, S., Barbier, O., & Bélanger, A.
- Affiliations
- Centre hospitalier de l'Université Laval (CA)
- Corresponding author
- Bélanger, Alain
- ORCID
- Barbier, Olivier
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2007-11
- Volume
- 282
- Issue
- 46
- Pages
- 33466-33474
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2126040395
- Cited by
- 109
- References
- 55
- Citations by year
- 2026: 3 · 2024: 4 · 2023: 9 · 2022: 4 · 2021: 3 · 2020: 5 · 2019: 5 · 2018: 8 · 2017: 9 · 2016: 9 · 2015: 4 · 2014: 4 · 2013: 11 · 2012: 7
- FWCI
- 5.76
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Canadian Institutes of Health Research
- Topics
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Prostate Cancer Treatment and Research
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Keywords
- androgen metabolism, dihydrotestosterone, glucuronidation, prostate cancer, LNCaP cells, androstanediol, androstanediol glucuronide, androgen response, gene silencing
- MeSH terms
- Androgens, Humans, Male, Models, Biological, Prostatic Neoplasms, Time Factors, Transfection, Glucuronosyltransferase, Minor Histocompatibility Antigens, Gene Expression Regulation, Neoplastic, RNA, Small Interfering, Cell Line, Tumor, Cell Proliferation
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