| The influence of matriptase-2 on prostate cancer in vitro: A possible role for β-catenin. | |
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MedLine Citation:
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PMID: 22858929 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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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. |
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Authors:
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Siobhan L Webb; Andrew J Sanders; Malcolm D Mason; Wen G Jiang |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-8-02 |
Journal Detail:
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Title: Oncology reports Volume: - ISSN: 1791-2431 ISO Abbreviation: Oncol. Rep. Publication Date: 2012 Aug |
Date Detail:
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Created Date: 2012-8-3 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9422756 Medline TA: Oncol Rep Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Metastasis and Angiogenesis Research Group, Institute of Cancer and Genetics, Cardiff University School of Medicine, Cardiff, UK. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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