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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/RAdN0jzrVDJxL5YAUdQ7TXxpD3MRW5RwtgnGySFiL8Ehs#_8 http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/version 1.4 http://www.tkuhn.ch/bel2nanopub/RAdN0jzrVDJxL5YAUdQ7TXxpD3MRW5RwtgnGySFiL8Ehs#_7 http://www.w3.org/ns/prov#value Our results show that VEGF can induce activation of the key integrins involved in angiogenesis, thereby establishing a mechanism by which the VEGF/VEGFR system can regulate cellular adhesive and migratory responses. Prothrombin, recently identified as an activation- dependent ligand of aVb3 (Byzova and Plow, 1998), supported limited adhesion of nonstimulated HUVECs; however, when these cells were stimulated with as little as 10 ng/ml VEGF165, adhesion to prothrombin increased by more than 10-fold. 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