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The influence of matriptase-2 on prostate cancer in vitro: a possible role for β-catenin.

Abstract
The type II transmembrane serine proteases (TTSPs) are a family of cell surface proteolytic enzymes contributing to a number of processes, such as tumour invasion and metastasis. Within the TTSPs, matriptase-2 is a relatively newly identified member and this protease has been shown to play a key role in cancer progression. β-catenin has long been regarded as an oncogene. The deregulation of the β-catenin signalling pathway plays a significant role in the progression and possibly the development of cancer. However, little is known about the role of matriptase-2 in prostate cancer. This study aimed to examine the correlation between matriptase-2 and β-catenin. Matriptase-2 was knocked down in the normal prostate cells, PZHPV7 and PNT2C2, using a ribozyme transgene targeting matriptase-2. The altered cells were used in a number of in vitro experiments designed to investigate the involvement of matriptase-2 with β-catenin and to further characterise its function. The knockdown of matriptase-2 had no effect on cell growth or adhesion but significantly reduced cell motility (PZHPV7 cells, p<0.001; PNT2C2 cells, p=0.001 vs. respective control cells) and invasive capability (PZHPV7 cells, p=0.001; PNT2C2 cells, p=0.007). The knockdown also caused a large increase in β-catenin protein expression at the cell membrane in PZHPV7 and PNT2C2 cells and a decrease in PC3 cells overexpressing matriptase-2, but did not affect the mRNA levels. Matriptase-2 may have an important impact on prostate cancer progression. The data gained from this study suggest that matriptase-2 protects against the development and progression of prostate cancer by regulating the motility and invasive capabilities of prostate cancer cells. Matriptase-2 also reduces the levels of β-catenin at the cell membrane. As β-catenin is highly involved in the regulation of cellular processes, including motility and invasion, the reduction of β-catenin expression by matriptase-2 may be a possible mechanism by which matriptase-2 functions.
AuthorsSiobhan L Webb, Andrew J Sanders, Malcolm D Mason, Wen G Jiang
JournalOncology reports (Oncol Rep) Vol. 28 Issue 4 Pg. 1491-7 (Oct 2012) ISSN: 1791-2431 [Electronic] Greece
PMID22858929 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Membrane Proteins
  • beta Catenin
  • Serine Endopeptidases
  • matriptase 2
Topics
  • Base Sequence
  • Cell Adhesion (genetics)
  • Cell Line, Tumor
  • Cell Membrane (metabolism)
  • Cell Movement (genetics)
  • Gene Knockdown Techniques
  • Humans
  • Male
  • Membrane Proteins (genetics, metabolism)
  • Molecular Sequence Data
  • Prostate (cytology, metabolism)
  • Prostatic Neoplasms (genetics, metabolism, pathology)
  • Serine Endopeptidases (genetics, metabolism)
  • Transgenes
  • beta Catenin (metabolism)

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