@prefix this: . @prefix sub: . @prefix beldoc: . @prefix rdfs: . @prefix rdf: . @prefix xsd: . @prefix dct: . @prefix dce: . @prefix pav: . @prefix np: . @prefix belv: . @prefix prov: . @prefix go: . @prefix Protein: . @prefix hgnc: . @prefix geneProductOf: . @prefix hasAgent: . @prefix nch: . @prefix ProteinComplex: . @prefix species: . @prefix occursIn: . @prefix mesh: . @prefix pubmed: . @prefix orcid: . sub:Head { this: np:hasAssertion sub:assertion; np:hasProvenance sub:provenance; np:hasPublicationInfo sub:pubinfo; a np:Nanopublication . } sub:assertion { nch:p85%2Fp110%20PI3Kinase%20Complex a ProteinComplex: . sub:_1 hasAgent: sub:_2; a go:0016301 . sub:_2 geneProductOf: hgnc:6307; a Protein: . sub:_3 hasAgent: nch:p85%2Fp110%20PI3Kinase%20Complex; a go:0016301 . sub:_4 occursIn: mesh:D004730, mesh:D042783, species:9606; rdf:object sub:_3; rdf:predicate belv:increases; rdf:subject sub:_1; a rdf:Statement . sub:assertion rdfs:label "kin(p(HGNC:KDR)) -> kin(complex(NCH:\"p85/p110 PI3Kinase Complex\"))" . } 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 . } sub:pubinfo { this: dct:created "2014-07-03T14:29:45.737+02:00"^^xsd:dateTime; pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 . }