Vascular endothelial growth factor receptor 2 and integrins (VEGFR2/Integrins)

Vascular endothelial growth factor receptor 2 (VEGFR2), also known as KDR or CD309, is a receptor tyrosine kinase that serves as the primary mediator of VEGF-induced pro-angiogenic signaling (UniProt P35968). Integrins are a diverse family of heterodimeric cell surface receptors, such as alpha-v beta-3, that regulate cell adhesion and migration by binding to extracellular matrix components (PubMed: 21622315). These two systems exhibit extensive functional crosstalk, where integrins can co-activate VEGFR2 to promote endothelial cell survival and vessel branching (PubMed: 19118211). In oncology, the co-expression of VEGFR2 and integrins on tumor-associated vasculature makes them prime targets for dual-inhibition strategies to suppress tumor growth and metastasis (PubMed: 25633116). Drugs like sorafenib and sunitinib target the kinase activity of VEGFR2, while agents like cilengitide were developed to inhibit integrin function, though combination therapies are often explored to enhance efficacy (ClinicalTrials.gov). This dual-targeting approach is particularly relevant in overcoming resistance to anti-VEGF monotherapy in solid tumors and ocular diseases.

Other names

KDRCD309Flk-1Vascular endothelial growth factor receptor 2Integrin alpha-v beta-3Integrin alpha-v beta-5Cell adhesion receptors

Inhibition of VEGFR2 tyrosine kinase activity to block VEGF-mediated endothelial proliferation and dual antagonism of integrin-extracellular matrix binding to disrupt cell adhesion and migration (PubMed: 21622315, PubMed: 19118211).