Membrane type-1 matrix metalloproteinase activity is regulated by the endocytic collagen receptor Endo180.
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ABSTRACT: The molecular interactions leading to organised, controlled extracellular matrix degradation are of central importance during growth, development and tissue repair, and when deregulated contribute to disease processes including cancer cell invasion. There are two major pathways for collagen degradation: one dependent on secreted and membrane-bound collagenases, the other on receptor-mediated collagen internalisation and intracellular processing. Despite the established importance of both pathways, the functional interaction between them is largely unknown. We demonstrate here, that the collagen internalisation receptor Endo180 (also known as CD280, uPARAP, MRC2) is a novel regulator of membrane-bound matrix metalloproteinase (MT1-MMP) activity, MT1-MMP-dependent MMP-2 activation and urokin
SUBMITTER: Messaritou G
PROVIDER: S-EPMC2776499 | biostudies-literature | 2009 Nov
REPOSITORIES: biostudies-literature
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