The Proteolytic Profile of Human Cancer Procoagulant Suggests That It Promotes Cancer Metastasis at the Level of Activation Rather Than Degradation

作者: Nalise Low Ah Kee , Jason Krause , Gregory L. Blatch , Koji Muramoto , Kazuo Sakka

DOI: 10.1007/S10930-015-9628-8

关键词: Activator (genetics)LamininProteaseProteasesBiochemistryBiologyExtracellular matrixFibronectinProteolysisCancer procoagulant

摘要: Proteases are essential for tumour progression and many over-expressed during this time. The main focus of research was the role these proteases in degradation basement membrane extracellular matrix (ECM), thereby enabling metastasis to occur. Cancer procoagulant (CP), a protease present malignant tumours, but not normal tissue, is known activator coagulation factor X (FX). study investigated function CP cancer by focussing on its enzymatic specificity. FX cleavage confirmed using SDS-PAGE MALDI-TOF MS compared proteolytic action ECM proteins, including collagen type IV, laminin fibronectin. Contrary previous reports, cleaved at conventional activation site (between Arg-52 Ile-53). Additionally, occurred much slower rate than activators. Complete heavy chain only visible after 24 h, while RVV complete 30 min, supporting postulations that may be secondary importance progression. Of proteins tested, fibronectin cleaved. substrate specificity further screening synthetic peptide substrates novel direct assay. results indicate either cancer-associated blood or proteins. Rather, they suggest required receptors.

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