ArticleBMC cancer2009
Expression of prostasin and its inhibitors during colorectal cancer carcinogenesis.
Article in BMC cancer, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Membrane-Anchored Serine Protease Inhibitors: Physiological Functions, Mechanisms, and Roles in Cancer.International journal of molecular sciences · 2026Review
- Prediction of the treatment response in ovarian cancer: a ctDNA approach.Journal of ovarian research · 2020Review
- The cell-surface anchored serine protease TMPRSS13 promotes breast cancer progression and resistance to chemotherapy.Oncogene · 2020Article
- Cell surface-anchored serine proteases in cancer progression and metastasis.Cancer metastasis reviews · 2019Review
- Membrane-Anchored Serine Proteases and Protease-Activated Receptor-2-Mediated Signaling: Co-Conspirators in Cancer Progression.Cancer research · 2019Review
- Expression pattern of humanOncology letters · 2018Article
- Article
- Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis.The Journal of biological chemistry · 2017Article
- The serine protease prostasin (PRSS8) is a potential biomarker for early detection of ovarian cancer.Journal of ovarian research · 2016Article
- Prognostic significance of SERPINE2 in gastric cancer and its biological function in SGC7901 cells.Journal of cancer research and clinical oncology · 2015Article
- High ABCC2 and low ABCG2 gene expression are early events in the colorectal adenoma-carcinoma sequence.PloS one · 2015Article
- Intestinal PTGS2 mRNA levels, PTGS2 gene polymorphisms, and colorectal carcinogenesis.PloS one · 2014Article
- Down-regulation of HAI-1 is associated with poor-differentiation status of colorectal cancer.Human cell · 2013Article
- Prostasin: An Epithelial Sodium Channel Regulator.Journal of biomarkers · 2013Review
- Genes regulated in metastatic osteosarcoma: evaluation by microarray analysis in four human and two mouse cell line systems.Sarcoma · 2012Article
- Spatiotemporal expression of SERPINE2 in the human placenta and its role in extravillous trophoblast migration and invasion.Reproductive biology and endocrinology : RB&E · 2011Article
- DNA Methylation Profiles of Protease Nexin 1 (SERPINE2) Gene in Human Cell Lines.Chinese journal of cancer research = Chung-kuo yen cheng yen chiu · 2011Article
- Transport via the transcytotic pathway makes prostasin available as a substrate for matriptase.The Journal of biological chemistry · 2011Article
- Article
- Membrane-anchored serine proteases in health and disease.Progress in molecular biology and translational science · 2011Review
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9 authors.
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Abstract
backgroundClinical trials where cancer patients were treated with protease inhibitors have suggested that the serine protease, prostasin, may act as a tumour suppressor. Prostasin is proteolytically activated by the serine protease, matriptase, which has a very high oncogenic potential. Prostasin is inhibited by protease nexin-1 (PN-1) and the two isoforms encoded by the mRNA splice variants of hepatocyte growth factor activator inhibitor-1 (HAI-1), HAI-1A, and HAI-1B.
methodsUsing quantitative RT-PCR, we have determined the mRNA levels for prostasin and PN-1 in colorectal cancer tissue (n = 116), severe dysplasia (n = 13), mild/moderate dysplasia (n = 93), and in normal tissue from the same individuals. In addition, corresponding tissues were examined from healthy volunteers (n = 23). A part of the cohort was further analysed for the mRNA levels of the two variants of HAI-1, here denoted HAI-1A and HAI-1B. mRNA levels were normalised to beta-actin. Immunohistochemical analysis of prostasin and HAI-1 was performed on normal and cancer tissue.
resultsThe mRNA level of prostasin was slightly but significantly decreased in both mild/moderate dysplasia (p < 0.001) and severe dysplasia (p < 0.01) and in carcinomas (p < 0.05) compared to normal tissue from the same individual. The mRNA level of PN-1 was more that two-fold elevated in colorectal cancer tissue as compared to healthy individuals (p < 0.001) and elevated in both mild/moderate dysplasia (p < 0.01), severe dysplasia (p < 0.05) and in colorectal cancer tissue (p < 0.001) as compared to normal tissue from the same individual. The mRNA levels of HAI-1A and HAI-1B mRNAs showed the same patterns of expression. Immunohistochemistry showed that prostasin is located mainly on the apical plasma membrane in normal colorectal tissue. A large variation was found in the degree of polarization of prostasin in colorectal cancer tissue.
conclusionThese results show that the mRNA level of PN-1 is significantly elevated in colorectal cancer tissue. Future studies are required to clarify whether down-regulation of prostasin activity via up regulation of PN-1 is causing the malignant progression or if it is a consequence of it.
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