sub:provenance {
  beldoc: dce:description "Approximately 61,000 statements." ;
    dce:rights "Copyright (c) 2011-2012, Selventa. All rights reserved." ;
    dce:title "BEL Framework Large Corpus Document" ;
    pav:authoredBy sub:_6 ;
    pav:version "1.4" .
  sub:_5 prov:value "The beta3 integrin is necessary for the activation of PI 3-kinase in endothelial cells stimulated by VEGF-A165  PI 3-kinase belongs to the intracellular signals triggered by VEGF-A in bovine endothelial cells, as demonstrated by the phosphorylation of its regulatory protein p85 (Guo et al., 1995). As shown in Figure 5, wortmannin used at nanomolar concentrations specific for PI 3-kinase inhibition (Arcaro and Wymann, 1993), reduced the human endothelial cells migration induced by VEGF-A165. To determine whether beta3 integrin interferes in PI 3-kinase activation occurring after VEGFR-2 stimulation, we evaluated the effect of BV4 (anti-beta3 subunit mAb) on the phosphorylation in tyrosine residues of the p85 subunit and on the catalytic activity of the enzyme. After pre-incubation with BV4 or with anti-VEGFR-2 Ab for 20 min at 4°C, cells were stimulated with VEGF-A165. Cell lysates were immunoprecipitated with anti-p85 mAb, and the separated proteins by SDS–PAGE were probed with anti-phosphotyrosine mAb. VEGF-A165 increased the tyrosine phosphorylation of p85, but it failed to phosphorylate the PI 3-kinase subunit when endothelial cells were pre-incubated with anti-beta3 or anti-VEGFR-2 antibodies (Figure 6)." ;
    prov:wasQuotedFrom pubmed:10022831 .
  sub:_6 rdfs:label "Selventa" .
  sub:assertion prov:hadPrimarySource pubmed:10022831 ;
    prov:wasDerivedFrom beldoc: , sub:_5 .
}