Title
Down-Regulation Of Prostasin Serine Protease: A Potential Invasion Suppressor In Prostate Cancer
Keywords
Cell line; Gene expression; Immunohistochemistry; Prostatectomy; Transfection
Abstract
BACKGROUND. Prostasin is a serine protease predominantly expressed in normal prostate epithelial cells. The biological function of prostasin has not been determined. METHODS. Western blot and RT-PCR analyses were used to examine the expression of prostasin in prostate cancer cell lines. Immunohistochemistry was used to evaluate prostasin protein expression in human prostate cancer. An in vitro Matrigel invasion assay was used to test the invasiveness of prostate cancer cell lines forced to express recombinant prostasin. RESULTS. Both prostasin protein and mRNA were found to be expressed in normal human prostate epithelial cells and a non-invasive human prostate cancer cell line, the LNCaP, but neither was found in invasive human prostate cancer cell lines DU-145 and PC-3. Prostasin mRNA expression was absent in invasive prostate cancer cell lines of a transgenic mouse model. Immunohistochemistry analysis showed that prostasin protein expression is down-regulated in high-grade prostate cancer. Transfection of DU-145 and PC-3 cells with a full-length human prostasin cDNA restored prostasin expression and reduced the in vitro invasiveness by 68 and 42%, respectively. CONCLUSIONS. Our data indicate that prostasin may be implicated in normal prostate biology and is able to suppress prostate cancer invasion in vitro. © 2001 Wiley-Liss, Inc.
Publication Date
7-1-2001
Publication Title
Prostate
Volume
48
Issue
2
Number of Pages
93-103
Document Type
Article
Personal Identifier
scopus
DOI Link
https://doi.org/10.1002/pros.1085
Copyright Status
Unknown
Socpus ID
0035399691 (Scopus)
Source API URL
https://api.elsevier.com/content/abstract/scopus_id/0035399691
STARS Citation
Chen, Li Mei; Byron Hodge, G.; and Guarda, Luis A., "Down-Regulation Of Prostasin Serine Protease: A Potential Invasion Suppressor In Prostate Cancer" (2001). Scopus Export 2000s. 219.
https://stars.library.ucf.edu/scopus2000/219