Nanopublications

Matches in Nanopublications for { ?s ?p ?o <http://www.tkuhn.ch/bel2nanopub/RAdMwlC9OUw7nXQ-Ct-6XnNIv79Bh8j2IVKS6YNOoRhjA#provenance>. }

Showing items 1 to 11 of 11 with 100 items per page.

_6 label "Selventa" provenance.
large_corpus.bel title "BEL Framework Large Corpus Document" provenance.
large_corpus.bel description "Approximately 61,000 statements." provenance.
large_corpus.bel version "1.4" provenance.
large_corpus.bel authoredBy _6 provenance.
assertion wasDerivedFrom large_corpus.bel provenance.
assertion wasDerivedFrom _5 provenance.
assertion hadPrimarySource 10022831 provenance.
_5 wasQuotedFrom 10022831 provenance.
_5 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)." provenance.