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HOXB13 is co-localized with androgen receptor to suppress androgen-stimulated prostate-specific antigen expression
During the prostate cancer (PCa) development and its progression into hormone independency, androgen receptor (AR) signals play a central role by triggering the regulation of target genes, including prostate-specific antigen. However, the regulation of these AR-mediated target genes is not fully und...
Autores principales: | , , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Korean Association of Anatomists
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3026180/ https://www.ncbi.nlm.nih.gov/pubmed/21267402 http://dx.doi.org/10.5115/acb.2010.43.4.284 |
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author | Kim, Sin Do Park, Ra-Young Kim, Young-Rang Kim, In-Je Kang, Taek Won Nam, Kwang Il Ahn, Kyu Youn Bae, Choon Sang Kim, Baik Youn Park, Sung Sik Jung, Chaeyong |
author_facet | Kim, Sin Do Park, Ra-Young Kim, Young-Rang Kim, In-Je Kang, Taek Won Nam, Kwang Il Ahn, Kyu Youn Bae, Choon Sang Kim, Baik Youn Park, Sung Sik Jung, Chaeyong |
author_sort | Kim, Sin Do |
collection | PubMed |
description | During the prostate cancer (PCa) development and its progression into hormone independency, androgen receptor (AR) signals play a central role by triggering the regulation of target genes, including prostate-specific antigen. However, the regulation of these AR-mediated target genes is not fully understood. We have previously demonstrated a unique role of HOXB13 homeodomain protein as an AR repressor. Expression of HOXB13 was highly restricted to the prostate and its suppression dramatically increased hormone-activated AR transactivation, suggesting that prostate-specific HOXB13 was a highly potent transcriptional regulator. In this report, we demonstrated the action mechanism of HOXB13 as an AR repressor. HOXB13 suppressed androgen-stimulated AR activity by interacting with AR. HOXB13 did neither bind to AR responsive elements nor disturb nuclear translocation of AR in response to androgen. In PCa specimen, we also observed mutual expression pattern of HOXB13 and AR. These results suggest that HOXB13 not only serve as a DNA-bound transcription factor but play an important role as an AR-interacting repressor to modulate hormone-activated androgen receptor signals. Further extensive studies will uncover a novel mechanism for regulating AR-signaling pathway to lead to expose new role of HOXB13 as a non-DNA-binding transcriptional repressor. |
format | Text |
id | pubmed-3026180 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Korean Association of Anatomists |
record_format | MEDLINE/PubMed |
spelling | pubmed-30261802011-01-25 HOXB13 is co-localized with androgen receptor to suppress androgen-stimulated prostate-specific antigen expression Kim, Sin Do Park, Ra-Young Kim, Young-Rang Kim, In-Je Kang, Taek Won Nam, Kwang Il Ahn, Kyu Youn Bae, Choon Sang Kim, Baik Youn Park, Sung Sik Jung, Chaeyong Anat Cell Biol Original Article During the prostate cancer (PCa) development and its progression into hormone independency, androgen receptor (AR) signals play a central role by triggering the regulation of target genes, including prostate-specific antigen. However, the regulation of these AR-mediated target genes is not fully understood. We have previously demonstrated a unique role of HOXB13 homeodomain protein as an AR repressor. Expression of HOXB13 was highly restricted to the prostate and its suppression dramatically increased hormone-activated AR transactivation, suggesting that prostate-specific HOXB13 was a highly potent transcriptional regulator. In this report, we demonstrated the action mechanism of HOXB13 as an AR repressor. HOXB13 suppressed androgen-stimulated AR activity by interacting with AR. HOXB13 did neither bind to AR responsive elements nor disturb nuclear translocation of AR in response to androgen. In PCa specimen, we also observed mutual expression pattern of HOXB13 and AR. These results suggest that HOXB13 not only serve as a DNA-bound transcription factor but play an important role as an AR-interacting repressor to modulate hormone-activated androgen receptor signals. Further extensive studies will uncover a novel mechanism for regulating AR-signaling pathway to lead to expose new role of HOXB13 as a non-DNA-binding transcriptional repressor. Korean Association of Anatomists 2010-12 2010-12-31 /pmc/articles/PMC3026180/ /pubmed/21267402 http://dx.doi.org/10.5115/acb.2010.43.4.284 Text en Copyright © 2010. Anatomy and Cell Biology http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Article Kim, Sin Do Park, Ra-Young Kim, Young-Rang Kim, In-Je Kang, Taek Won Nam, Kwang Il Ahn, Kyu Youn Bae, Choon Sang Kim, Baik Youn Park, Sung Sik Jung, Chaeyong HOXB13 is co-localized with androgen receptor to suppress androgen-stimulated prostate-specific antigen expression |
title | HOXB13 is co-localized with androgen receptor to suppress androgen-stimulated prostate-specific antigen expression |
title_full | HOXB13 is co-localized with androgen receptor to suppress androgen-stimulated prostate-specific antigen expression |
title_fullStr | HOXB13 is co-localized with androgen receptor to suppress androgen-stimulated prostate-specific antigen expression |
title_full_unstemmed | HOXB13 is co-localized with androgen receptor to suppress androgen-stimulated prostate-specific antigen expression |
title_short | HOXB13 is co-localized with androgen receptor to suppress androgen-stimulated prostate-specific antigen expression |
title_sort | hoxb13 is co-localized with androgen receptor to suppress androgen-stimulated prostate-specific antigen expression |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3026180/ https://www.ncbi.nlm.nih.gov/pubmed/21267402 http://dx.doi.org/10.5115/acb.2010.43.4.284 |
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