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statements. http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/rights Copyright (c) 2011-2012, Selventa. All rights reserved. http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RAr15TUSgysMy0DiIzpKXryHvZDfpIFc3_RCxaC0-plEI#_9 http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/version 1.4 http://www.tkuhn.ch/bel2nanopub/RAr15TUSgysMy0DiIzpKXryHvZDfpIFc3_RCxaC0-plEI#_8 http://www.w3.org/ns/prov#value Based on the realization of a direct MMP/integrin interaction, the following chain of events can be postulated. (i) Tissue injury exposes epithelial cells to proximally located fibrillar collagen and triggers integrin ligation. (ii) The newly formed adhesive contact between collagen and integrins induces transcriptional upregulation of MMP1 in the cell. (iii) By a so far unknown mechanism, pro-MMP1 is locally secreted and binds to a subset of I domains in the alpha2beta1 integrin. (iv) Formation of this ternary complex converts pro-MMP1 into its active form. This activation occurs either by another protease or by a conformational reorganization of the catalytic domain. Activated MMP1 then cleaves type I collagen at a single site. (v) Cleaved collagen rapidly denatures, which reduces its integrin-binding affinity. (vi) Consequently, the focal adhesion complex disassembles and allows the reorganization of the cytoskeleton. (vii) The cell can then move forward and form novel cell/matrix contacts. This chain of events is supported from data studying migration of VSMC on collagen, where MMP1 activity was localized only to discrete zones underneath the leading edge and the cell tail [102]. 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