Gene interactions and pathways from curated databases and text-mining

◀ Back to VEGFA

ITGB1 — VEGFA

Pathways - manually collected, often from reviews:

  • OpenBEL Selventa BEL large corpus: Complex of FN1-ITGA5-ITGB1 → VEGFA (increases)
    Evidence: The data in Figure 1D suggested that a second aV integ- rin, aVb5, which has been implicated in angiogenesis, may also be activated by VEGF165. Therefore, we sought concento determine if still other integrins implicated in angio- genesis, a5b1, a fibronectin receptor (Bloch et al., 1997), and a2b1, a collagen receptor (Senger et al., 1997), might be activated by VEGF165. In cell migration assays, VEGF165 markedly stimulated HUVEC movement onto effibronectin (see Figure 3A). The migrating cells e...
  • OpenBEL Selventa BEL large corpus: Complex of ITGA2-ITGB1 → VEGFA (increases, VEGFA Activity)
    Evidence: The data in Figure 1D suggested that a second aV integ- rin, aVb5, which has been implicated in angiogenesis, may also be activated by VEGF165. Therefore, we sought concento determine if still other integrins implicated in angio- genesis, a5b1, a fibronectin receptor (Bloch et al., 1997), and a2b1, a collagen receptor (Senger et al., 1997), might be activated by VEGF165. In cell migration assays, VEGF165 markedly stimulated HUVEC movement onto effibronectin (see Figure 3A). The migrating cells e...
  • OpenBEL Selventa BEL large corpus: Complex of ITGA2-ITGB1 → VEGFA (increases, VEGFA Activity)
    Evidence: VEGF enhanced cell adhesion, migration, soluble ligand binding, and adenovirus gene transfer mediated by alphavbeta3 and also activated other integrins, alphavbeta5, alpha5beta1, and alpha2beta1, involved in angiogenesis. The major findings of our studies are as follows. First, VEGF165 can activate integrin aVb3, leading to enhanced adhesion of endothelial cells to a variety of ligands.
  • OpenBEL Selventa BEL large corpus: Complex of ITGA2-ITGB1 → VEGFA (increases, VEGFA Activity)
    Evidence: Fifth, VEGF165 activation is not targeted to a single integrin; b1 integrins, as exemplified by a5b1 and a2b1, also are affected by VEGF165 stimulation. In addition, our data suggest that aVb5 can be activated by the growth factor.
  • OpenBEL Selventa BEL large corpus: Complex of ITGA5-ITGB1 → VEGFA (increases, VEGFA Activity)
    Evidence: The data in Figure 1D suggested that a second aV integ- rin, aVb5, which has been implicated in angiogenesis, may also be activated by VEGF165. Therefore, we sought concento determine if still other integrins implicated in angio- genesis, a5b1, a fibronectin receptor (Bloch et al., 1997), and a2b1, a collagen receptor (Senger et al., 1997), might be activated by VEGF165. In cell migration assays, VEGF165 markedly stimulated HUVEC movement onto effibronectin (see Figure 3A). The migrating cells e...
  • OpenBEL Selventa BEL large corpus: Complex of ITGA5-ITGB1 → VEGFA (increases, VEGFA Activity)
    Evidence: VEGF enhanced cell adhesion, migration, soluble ligand binding, and adenovirus gene transfer mediated by alphavbeta3 and also activated other integrins, alphavbeta5, alpha5beta1, and alpha2beta1, involved in angiogenesis. The major findings of our studies are as follows. First, VEGF165 can activate integrin aVb3, leading to enhanced adhesion of endothelial cells to a variety of ligands.
  • OpenBEL Selventa BEL large corpus: Complex of ITGA5-ITGB1 → VEGFA (increases, VEGFA Activity)
    Evidence: Fifth, VEGF165 activation is not targeted to a single integrin; b1 integrins, as exemplified by a5b1 and a2b1, also are affected by VEGF165 stimulation. In addition, our data suggest that aVb5 can be activated by the growth factor.
  • OpenBEL Selventa BEL large corpus: ITGB1 → VEGFA (increases)
    Evidence: The migration of cells induced by VEGF was decreased by approximately 50% after pretreatment with blocking anti-Beta1 integrin antibody. Anti-Beta1 integrin antibody also inhibited VEGF dependent DNA synthesis.
  • NCI Pathway Database Alpha9 beta1 integrin signaling events: VEGFA (dimer) complex (VEGFA) → alpha9/beta1 Integrin/VEGFA (dimer) complex (ITGA9-ITGB1-VEGFA) (modification, collaborate)
    Vlahakis et al., J Biol Chem 2007*, Oommen et al., J Biol Chem 2011*, Palmer et al., J Cell Biol 1993
    Evidence: physical interaction
  • NCI Pathway Database Alpha9 beta1 integrin signaling events: VEGFA (dimer) complex (VEGFA) → alpha9/beta1 Integrin complex (ITGA9-ITGB1) (modification, collaborate)
    Vlahakis et al., J Biol Chem 2007*, Oommen et al., J Biol Chem 2011*, Palmer et al., J Cell Biol 1993
    Evidence: physical interaction
  • NCI Pathway Database Alpha9 beta1 integrin signaling events: alpha9/beta1 Integrin/VEGFA (dimer) complex (ITGA9-ITGB1-VEGFA) → alpha9/beta1 Integrin complex (ITGA9-ITGB1) (modification, collaborate)
    Vlahakis et al., J Biol Chem 2007*, Oommen et al., J Biol Chem 2011*, Palmer et al., J Cell Biol 1993
    Evidence: physical interaction
  • NCI Pathway Database Beta1 integrin cell surface interactions: VEGF189 (VEGFA) → alpha3/beta1 Integrin/VEGF189 complex (VEGFA-ITGA3-ITGB1) (modification, collaborate)
    Hutchings et al., FASEB J 2003*
    Evidence: physical interaction
  • NCI Pathway Database Beta1 integrin cell surface interactions: VEGF189 (VEGFA) → alpha3/beta1 Integrin complex (ITGA3-ITGB1) (modification, collaborate)
    Hutchings et al., FASEB J 2003*
    Evidence: physical interaction
  • NCI Pathway Database Beta1 integrin cell surface interactions: alpha3/beta1 Integrin/VEGF189 complex (VEGFA-ITGA3-ITGB1) → alpha3/beta1 Integrin complex (ITGA3-ITGB1) (modification, collaborate)
    Hutchings et al., FASEB J 2003*
    Evidence: physical interaction

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Chung et al., Cancer Res 2004 (Breast Neoplasms) : Hypoxia induced vascular endothelial growth factor transcription and protection from apoptosis are dependent on alpha6beta1 integrin in breast carcinoma cells
Datta et al., Kidney Int 2004 : In this study, we provide preliminary evidence that signaling through the extracellular matrix proteins and, in particular, laminin and its receptor alpha(3)beta(1) integrin may regulate VPF/VEGF-A production in cultured podocytes in vitro
Lu et al., Mol Pharmacol 2006 : Laulimalide inhibited integrin activation ; however, compared with docetaxel, it had a weaker inhibitory effect on the VEGF induced association of VEGFR-2 with the alpha5beta1 integrin
Boosani et al., Blood 2007 (Neoplasms...) : We show that binding of alpha3 ( IV ) NC1 to alpha3beta1 integrin leads to inhibition of COX-2 mediated pro-angiogenic factors, vascular endothelial growth factor , and basic fibroblast growth factor by regulating IkappaBalpha/NFkappaB axis, and is independent of alphaVbeta3 integrin