The influence of matriptase-2 on prostate cancer in vitro: A possible role for β-catenin
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 rol...
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Veröffentlicht in: | Oncology reports 2012-10, Vol.28 (4), p.1491-1497 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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 |
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ISSN: | 1021-335X 1791-2431 |
DOI: | 10.3892/or.2012.1945 |