Rapid Androgen-Responsive Proteome Is Involved in Prostate Cancer Progression

Androgen exerts its functions by binding with an androgen receptor (AR). It can activate many signaling pathways that are important to the progression of castration-resistant prostate cancer (CRPC). Here, we characterized the rapid proteomic changes seen at 5, 15, 30, and 60 min after the androgen t...

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Main Authors: Jong-Kwang Kim, Jae-Hun Jung, Dong-Hoon Shin, Hye-Jin You, Seho Cha, Bo-Seul Song, Jae-Young Joung, Weon-Seo Park, Kwang-Pyo Kim, Jae-Kyung Myung
Format: Article
Language:English
Published: MDPI AG 2021-12-01
Series:Biomedicines
Subjects:
Online Access:https://www.mdpi.com/2227-9059/9/12/1877
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author Jong-Kwang Kim
Jae-Hun Jung
Dong-Hoon Shin
Hye-Jin You
Seho Cha
Bo-Seul Song
Jae-Young Joung
Weon-Seo Park
Kwang-Pyo Kim
Jae-Kyung Myung
author_facet Jong-Kwang Kim
Jae-Hun Jung
Dong-Hoon Shin
Hye-Jin You
Seho Cha
Bo-Seul Song
Jae-Young Joung
Weon-Seo Park
Kwang-Pyo Kim
Jae-Kyung Myung
author_sort Jong-Kwang Kim
collection DOAJ
description Androgen exerts its functions by binding with an androgen receptor (AR). It can activate many signaling pathways that are important to the progression of castration-resistant prostate cancer (CRPC). Here, we characterized the rapid proteomic changes seen at 5, 15, 30, and 60 min after the androgen treatment of VCaP cells via the tandem mass tag (TMT) labeling strategy. A total of 5529 proteins were successfully identified and quantified. Dynamic time profiling of protein expression patterns allowed us to identify five protein clusters involved in various stages of androgen-initiated signal transmission and processing. More details of protein functions and localization patterns, and our elucidation of an AR-interacting protein network, were obtained. Finally, we validated the expression level of AR-regulated proteins known to be significantly regulated in CRPC patients using the mouse xenograft model and patient samples. Our work offers a systematic analysis of the rapid proteomic changes induced by androgen and provides a global view of the molecular mechanisms underlying CRPC progression.
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spelling doaj.art-6b7e7550bec8479da890a933ba610b2f2023-11-23T03:56:57ZengMDPI AGBiomedicines2227-90592021-12-01912187710.3390/biomedicines9121877Rapid Androgen-Responsive Proteome Is Involved in Prostate Cancer ProgressionJong-Kwang Kim0Jae-Hun Jung1Dong-Hoon Shin2Hye-Jin You3Seho Cha4Bo-Seul Song5Jae-Young Joung6Weon-Seo Park7Kwang-Pyo Kim8Jae-Kyung Myung9Research Core Center, National Cancer Center, Goyang-si 10408, KoreaDepartment of Applied Chemistry, Institute of Natural Science, Global Center for Pharmaceutical Ingredient Materials, Kyung Hee University, Yongin-si 17104, KoreaDepartment of Cancer Biomedical Science, National Cancer Center Graduate School of Cancer Science and Policy, Goyang-si 10408, KoreaDepartment of Cancer Biomedical Science, National Cancer Center Graduate School of Cancer Science and Policy, Goyang-si 10408, KoreaDepartment of Cancer Biomedical Science, National Cancer Center Graduate School of Cancer Science and Policy, Goyang-si 10408, KoreaDepartment of Cancer Biomedical Science, National Cancer Center Graduate School of Cancer Science and Policy, Goyang-si 10408, KoreaDepartment of Cancer Biomedical Science, National Cancer Center Graduate School of Cancer Science and Policy, Goyang-si 10408, KoreaDepartment of Pathology, National Cancer Center, Goyang-si 10408, KoreaDepartment of Applied Chemistry, Institute of Natural Science, Global Center for Pharmaceutical Ingredient Materials, Kyung Hee University, Yongin-si 17104, KoreaDepartment of Cancer Biomedical Science, National Cancer Center Graduate School of Cancer Science and Policy, Goyang-si 10408, KoreaAndrogen exerts its functions by binding with an androgen receptor (AR). It can activate many signaling pathways that are important to the progression of castration-resistant prostate cancer (CRPC). Here, we characterized the rapid proteomic changes seen at 5, 15, 30, and 60 min after the androgen treatment of VCaP cells via the tandem mass tag (TMT) labeling strategy. A total of 5529 proteins were successfully identified and quantified. Dynamic time profiling of protein expression patterns allowed us to identify five protein clusters involved in various stages of androgen-initiated signal transmission and processing. More details of protein functions and localization patterns, and our elucidation of an AR-interacting protein network, were obtained. Finally, we validated the expression level of AR-regulated proteins known to be significantly regulated in CRPC patients using the mouse xenograft model and patient samples. Our work offers a systematic analysis of the rapid proteomic changes induced by androgen and provides a global view of the molecular mechanisms underlying CRPC progression.https://www.mdpi.com/2227-9059/9/12/1877castration resistant prostate cancerandrogen receptorrapid signalingproteomicsmass spectrometrybioinformatics
spellingShingle Jong-Kwang Kim
Jae-Hun Jung
Dong-Hoon Shin
Hye-Jin You
Seho Cha
Bo-Seul Song
Jae-Young Joung
Weon-Seo Park
Kwang-Pyo Kim
Jae-Kyung Myung
Rapid Androgen-Responsive Proteome Is Involved in Prostate Cancer Progression
Biomedicines
castration resistant prostate cancer
androgen receptor
rapid signaling
proteomics
mass spectrometry
bioinformatics
title Rapid Androgen-Responsive Proteome Is Involved in Prostate Cancer Progression
title_full Rapid Androgen-Responsive Proteome Is Involved in Prostate Cancer Progression
title_fullStr Rapid Androgen-Responsive Proteome Is Involved in Prostate Cancer Progression
title_full_unstemmed Rapid Androgen-Responsive Proteome Is Involved in Prostate Cancer Progression
title_short Rapid Androgen-Responsive Proteome Is Involved in Prostate Cancer Progression
title_sort rapid androgen responsive proteome is involved in prostate cancer progression
topic castration resistant prostate cancer
androgen receptor
rapid signaling
proteomics
mass spectrometry
bioinformatics
url https://www.mdpi.com/2227-9059/9/12/1877
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