Matrix metalloproteinase-2 activation modulates glioma cell migration
作者： Alex Strongin , Elena I. Deryugina , Ralph A. Reisfeld , Mario A. Bourdon , Guang-Xiang Luo
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摘要: Stable transfection of U251.3 glioma cells with cDNA encoding MT-MMP-1 resulted in increased cell surface expression and TIMP-2, constitutive activation MMP-2 proenzyme collagen degradation. In tumor spheroid outgrowth assays, migration transfectants relative to control was enhanced on decreased vitronectin fibronectin. These effects were reversed by TIMP-2 not associated any substantial changes adhesion. Binding the C-terminal domain specifically inhibited anti-(alpha)vss3 integrin blocking antibody indicating that interacts (alpha)vss3 through enzyme's portion at or near integrin's matrix adhesion sites. We propose these mechanisms could govern directed degradation cells' microenvironment sequestration active surface. Our data suggest its proteolytic activity localized differentially modulate response particular proteins altering both composition extracellular receptors
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