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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/RAVpdB-k-K_Ql1wyAKcPssxt-tU2kfri7sBrnB7I2DJgc#_9 http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/version 1.4 http://www.tkuhn.ch/bel2nanopub/RAVpdB-k-K_Ql1wyAKcPssxt-tU2kfri7sBrnB7I2DJgc#_8 http://www.w3.org/ns/prov#value The a5b1 integrin, which binds to fibronectin, induces expression of the antiapoptotic protein Bcl-2, protecting cells from apoptosis from stresses such as the lack of growth factors (55). Other integrins, including another fibronectin receptor, avb1, do not provide this survival effect. The avb3 integrin promotes endothelial and melanoma cell survival; this effect correlates with suppression of the p53 pathway and activation of the nuclear factor kappa B transcription factor (56). The activation of Shc by a1b1, a5b1, and avb3 may also contribute to protection from apoptosis (4, 17). 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