Interaction between integrin avb3 and extracellular matrix is crucial for endothelial cells sprouting from capillaries and for angiogenesis.
Tyrosine-phosphorylated VEGFR2 co-immunoprecipitated with b3 integrin subunit, but not with b1 or b5, from cells stimulated with VEGFA (165 amino acid isoform)
VEGFR2 phosphorylation and mitogenicity induced by VEGFA were enhanced in cells plated on the avb3 ligand, vitronectin, compared with cells plated on the a5b1 ligand, fibronectin or the a2b1 ligand, collagen.
A new role for avb3 integrin in the activation of an in vitro angiogenic program in endothelial cells:
Besides being the most important survival system for nascent vessels by regulating cell adhesion to matrix, avb3 integrin participates in the full activation of VEGFR2 triggered by VEGFA.