Year-end Sale % OFF 
Abstract
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.
Highlights
Bioinformatics approaches have shown that the serine protease 23 gene (PRSS23) is highly conserved in vertebrates and is predicted to encode a novel protease on chromosome 11q14.1 in humans [1,2,3]
Histopathological assays and surveys of cancer cell lines further confirmed PRSS23 expression was significantly increased in estrogen receptor a (ERa)-positive breast cancers, and PRSS23 expression was upregulated by ERa-mediated transcriptional regulation
We investigated the functional role of PRSS23 and found that PRSS23 may regulate DNA replication during cancer cell proliferation, which highlights PRSS23’s potential as a novel target for breast cancer therapy
Summary
Bioinformatics approaches have shown that the serine protease 23 gene (PRSS23) is highly conserved in vertebrates and is predicted to encode a novel protease on chromosome 11q14.1 in humans [1,2,3]. Estrogen, which are well conserved in vertebrates, represents a group of sex steroid hormones that include estradiol, estrone, and estriol [11]. Ample evidence has shown that estrogen and anti-estrogen agents, such as tamoxifen and fulvestrant, can bind to the ligand binding domain of estrogen receptor a (ERa) to modulate differential expression of downstream transcriptional targets of ERa in breast cancer cells. These findings suggest that ERa could be a vital prognostic biomarker in breast cancer [12,13,14,15,16,17]
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
