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The type II transmembrane serine proteases (TTSPs) are a family of cellsurface proteolytic enzymes contributing to a number of processes, such as tumourinvasion and metastasis. Within the TTSPs, matriptase-2 is a relatively newlyidentified member and this protease has been shown to play a key role in cancerprogression. β-catenin has long been regarded as an oncogene. The deregulationof the β-catenin signalling pathway plays a significant role in the progressionand possibly the development of cancer. However, little is known about the roleof matriptase-2 in prostate cancer. This study aimed to examine the correlationbetween matriptase-2 and β-catenin. Matriptase-2 was knocked down in the normalprostate 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 investigatethe involvement of matriptase-2 with β-catenin and to further characterise itsfunction. The knockdown of matriptase-2 had no effect on cell growth or adhesionbut significantly reduced cell motility (PZHPV7 cells, p&lt;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-cateninprotein expression at the cell membrane in PZHPV7 and PNT2C2 cells and a decreasein PC3 cells overexpressing matriptase-2, but did not affect the mRNA levels.Matriptase-2 may have an important impact on prostate cancer progression. Thedata gained from this study suggest that matriptase-2 protects against the developmentand progression of prostate cancer by regulating the motility and invasive capabilitiesof prostate cancer cells. Matriptase-2 also reduces the levels of β-catenin atthe cell membrane. As β-catenin is highly involved in the regulation of cellularprocesses, including motility and invasion, the reduction of β-catenin expressionby matriptase-2 may be a possible mechanism by which matriptase-2 functions.

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