Serine protease PRSS23 is upregulated by estrogen receptor α and associated with proliferation of breast cancer cells.

Serine protease PRSS23 is a newly discovered protein that has been associated with tumor progression in various types of cancers. Interestingly, PRSS23 is coexpressed with estrogen receptor α (ERα), which is a prominent biomarker and therapeutic target for human breast cancer. Estrogen signaling thr...

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Autores principales:	Hau-Shien Chan, Shing-Jyh Chang, Tao-Yeuan Wang, Hung-Ju Ko, Yu-Chih Lin, Kuan-Ting Lin, Kuo-Ming Chang, Yung-Jen Chuang
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/c41738f4d356458d979a853e3a6019be
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spelling	oai:doaj.org-article:c41738f4d356458d979a853e3a6019be2021-11-18T07:29:37ZSerine protease PRSS23 is upregulated by estrogen receptor α and associated with proliferation of breast cancer cells.1932-620310.1371/journal.pone.0030397https://doaj.org/article/c41738f4d356458d979a853e3a6019be2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22291950/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Serine protease PRSS23 is a newly discovered protein that has been associated with tumor progression in various types of cancers. Interestingly, PRSS23 is coexpressed with estrogen receptor α (ERα), which is a prominent biomarker and therapeutic target for human breast cancer. Estrogen signaling through ERα is also known to affect cell proliferation, apoptosis, and survival, which promotes tumorigenesis by regulating the production of numerous downstream effector proteins.In the present study, we aimed to clarify the correlation between and functional implication of ERα and PRSS23 in breast cancer. Analysis of published breast cancer microarray datasets revealed that the gene expression correlation between ERα and PRSS23 is highly significant among all ERα-associated proteases in breast cancer. We then assessed PRSS23 expression in 56 primary breast cancer biopsies and 8 cancer cell lines. The results further confirmed the coexpression of PRSS23 and ERα and provided clinicopathological significance. In vitro assays in MCF-7 breast cancer cells demonstrated that PRSS23 expression is induced by 17β-estradiol-activated ERα through an interaction with an upstream promoter region of PRSS23 gene. In addition, PRSS23 knockdown may suppress estrogen-driven cell proliferation of MCF-7 cells.Our findings imply that PRSS23 might be a critical component of estrogen-mediated cell proliferation of ERα-positive breast cancer cells. In conclusion, the present study highlights the potential for PRSS23 to be a novel therapeutic target in breast cancer research.Hau-Shien ChanShing-Jyh ChangTao-Yeuan WangHung-Ju KoYu-Chih LinKuan-Ting LinKuo-Ming ChangYung-Jen ChuangPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 1, p e30397 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Hau-Shien Chan Shing-Jyh Chang Tao-Yeuan Wang Hung-Ju Ko Yu-Chih Lin Kuan-Ting Lin Kuo-Ming Chang Yung-Jen Chuang Serine protease PRSS23 is upregulated by estrogen receptor α and associated with proliferation of breast cancer cells.
description	Serine protease PRSS23 is a newly discovered protein that has been associated with tumor progression in various types of cancers. Interestingly, PRSS23 is coexpressed with estrogen receptor α (ERα), which is a prominent biomarker and therapeutic target for human breast cancer. Estrogen signaling through ERα is also known to affect cell proliferation, apoptosis, and survival, which promotes tumorigenesis by regulating the production of numerous downstream effector proteins.In the present study, we aimed to clarify the correlation between and functional implication of ERα and PRSS23 in breast cancer. Analysis of published breast cancer microarray datasets revealed that the gene expression correlation between ERα and PRSS23 is highly significant among all ERα-associated proteases in breast cancer. We then assessed PRSS23 expression in 56 primary breast cancer biopsies and 8 cancer cell lines. The results further confirmed the coexpression of PRSS23 and ERα and provided clinicopathological significance. In vitro assays in MCF-7 breast cancer cells demonstrated that PRSS23 expression is induced by 17β-estradiol-activated ERα through an interaction with an upstream promoter region of PRSS23 gene. In addition, PRSS23 knockdown may suppress estrogen-driven cell proliferation of MCF-7 cells.Our findings imply that PRSS23 might be a critical component of estrogen-mediated cell proliferation of ERα-positive breast cancer cells. In conclusion, the present study highlights the potential for PRSS23 to be a novel therapeutic target in breast cancer research.
format	article
author	Hau-Shien Chan Shing-Jyh Chang Tao-Yeuan Wang Hung-Ju Ko Yu-Chih Lin Kuan-Ting Lin Kuo-Ming Chang Yung-Jen Chuang
author_facet	Hau-Shien Chan Shing-Jyh Chang Tao-Yeuan Wang Hung-Ju Ko Yu-Chih Lin Kuan-Ting Lin Kuo-Ming Chang Yung-Jen Chuang
author_sort	Hau-Shien Chan
title	Serine protease PRSS23 is upregulated by estrogen receptor α and associated with proliferation of breast cancer cells.
title_short	Serine protease PRSS23 is upregulated by estrogen receptor α and associated with proliferation of breast cancer cells.
title_full	Serine protease PRSS23 is upregulated by estrogen receptor α and associated with proliferation of breast cancer cells.
title_fullStr	Serine protease PRSS23 is upregulated by estrogen receptor α and associated with proliferation of breast cancer cells.
title_full_unstemmed	Serine protease PRSS23 is upregulated by estrogen receptor α and associated with proliferation of breast cancer cells.
title_sort	serine protease prss23 is upregulated by estrogen receptor α and associated with proliferation of breast cancer cells.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/c41738f4d356458d979a853e3a6019be
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Serine protease PRSS23 is upregulated by estrogen receptor α and associated with proliferation of breast cancer cells.

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