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Androgen Regulation of 5α-Reductase Isoenzymes in Prostate Cancer: Implications for Prostate Cancer Prevention (Androgen Regulation of 5α-Reductase Isoenzymes)

The enzyme 5α-reductase, which converts testosterone to dihydrotestosterone (DHT), performs key functions in the androgen receptor (AR) signaling pathway. The three isoenzymes of 5α-reductase identified to date are encoded by different genes: SRD5A1 , SRD5A2 , and SRD5A3 . In this study, we investig... Full description

Journal Title: PLoS ONE 2011, Vol.6(12), p.e28840
Main Author: Li, Jin
Other Authors: Ding, Zhiyong , Wang, Zhengxin , Lu, Jing-Fang , Maity, Sankar N , Navone, Nora M , Logothetis, Christopher J , Mills, Gordon B , Kim, Jeri
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0028840
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recordid: plos10.1371/journal.pone.0028840
title: Androgen Regulation of 5α-Reductase Isoenzymes in Prostate Cancer: Implications for Prostate Cancer Prevention (Androgen Regulation of 5α-Reductase Isoenzymes)
format: Article
creator:
  • Li, Jin
  • Ding, Zhiyong
  • Wang, Zhengxin
  • Lu, Jing-Fang
  • Maity, Sankar N
  • Navone, Nora M
  • Logothetis, Christopher J
  • Mills, Gordon B
  • Kim, Jeri
subjects:
  • Research Article
  • Biology
  • Medicine
  • Urology
  • Oncology
  • Biochemistry
ispartof: PLoS ONE, 2011, Vol.6(12), p.e28840
description: The enzyme 5α-reductase, which converts testosterone to dihydrotestosterone (DHT), performs key functions in the androgen receptor (AR) signaling pathway. The three isoenzymes of 5α-reductase identified to date are encoded by different genes: SRD5A1 , SRD5A2 , and SRD5A3 . In this study, we investigated mechanisms underlying androgen regulation of 5α-reductase isoenzyme expression in human prostate cells. We found that androgen regulates the mRNA level of 5α-reductase isoenzymes in a cell type–specific manner, that such regulation occurs at the transcriptional level, and that AR is necessary for this regulation. In addition, our results suggest that AR is recruited to a negative androgen response element (nARE) on the promoter of SRD5A3 in vivo and directly binds to the nARE in vitro . The different expression levels of 5α-reductase isoenzymes may confer response or resistance to 5α-reductase inhibitors and thus may have importance in prostate cancer prevention.
language: eng
source:
identifier: E-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0028840
fulltext: fulltext
issn:
  • 1932-6203
  • 19326203
url: Link


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titleAndrogen Regulation of 5α-Reductase Isoenzymes in Prostate Cancer: Implications for Prostate Cancer Prevention (Androgen Regulation of 5α-Reductase Isoenzymes)
creatorLi, Jin ; Ding, Zhiyong ; Wang, Zhengxin ; Lu, Jing-Fang ; Maity, Sankar N ; Navone, Nora M ; Logothetis, Christopher J ; Mills, Gordon B ; Kim, Jeri
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identifierE-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0028840
subjectResearch Article ; Biology ; Medicine ; Urology ; Oncology ; Biochemistry
descriptionThe enzyme 5α-reductase, which converts testosterone to dihydrotestosterone (DHT), performs key functions in the androgen receptor (AR) signaling pathway. The three isoenzymes of 5α-reductase identified to date are encoded by different genes: SRD5A1 , SRD5A2 , and SRD5A3 . In this study, we investigated mechanisms underlying androgen regulation of 5α-reductase isoenzyme expression in human prostate cells. We found that androgen regulates the mRNA level of 5α-reductase isoenzymes in a cell type–specific manner, that such regulation occurs at the transcriptional level, and that AR is necessary for this regulation. In addition, our results suggest that AR is recruited to a negative androgen response element (nARE) on the promoter of SRD5A3 in vivo and directly binds to the nARE in vitro . The different expression levels of 5α-reductase isoenzymes may confer response or resistance to 5α-reductase inhibitors and thus may have importance in prostate cancer prevention.
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titleAndrogen Regulation of 5α-Reductase Isoenzymes in Prostate Cancer: Implications for Prostate Cancer Prevention (Androgen Regulation of 5α-Reductase Isoenzymes)
descriptionThe enzyme 5α-reductase, which converts testosterone to dihydrotestosterone (DHT), performs key functions in the androgen receptor (AR) signaling pathway. The three isoenzymes of 5α-reductase identified to date are encoded by different genes: SRD5A1 , SRD5A2 , and SRD5A3 . In this study, we investigated mechanisms underlying androgen regulation of 5α-reductase isoenzyme expression in human prostate cells. We found that androgen regulates the mRNA level of 5α-reductase isoenzymes in a cell type–specific manner, that such regulation occurs at the transcriptional level, and that AR is necessary for this regulation. In addition, our results suggest that AR is recruited to a negative androgen response element (nARE) on the promoter of SRD5A3 in vivo and directly binds to the nARE in vitro . The different expression levels of 5α-reductase isoenzymes may confer response or resistance to 5α-reductase inhibitors and thus may have importance in prostate cancer prevention.
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abstractThe enzyme 5α-reductase, which converts testosterone to dihydrotestosterone (DHT), performs key functions in the androgen receptor (AR) signaling pathway. The three isoenzymes of 5α-reductase identified to date are encoded by different genes: SRD5A1 , SRD5A2 , and SRD5A3 . In this study, we investigated mechanisms underlying androgen regulation of 5α-reductase isoenzyme expression in human prostate cells. We found that androgen regulates the mRNA level of 5α-reductase isoenzymes in a cell type–specific manner, that such regulation occurs at the transcriptional level, and that AR is necessary for this regulation. In addition, our results suggest that AR is recruited to a negative androgen response element (nARE) on the promoter of SRD5A3 in vivo and directly binds to the nARE in vitro . The different expression levels of 5α-reductase isoenzymes may confer response or resistance to 5α-reductase inhibitors and thus may have importance in prostate cancer prevention.
copSan Francisco, USA
pubPublic Library of Science
doi10.1371/journal.pone.0028840
oafree_for_read
date2011-12-14