Vascular endothelial growth factor receptor 2 and Integrin αvβ3 (VEGFR2 and Integrin αvβ3)

Vascular endothelial growth factor receptor 2 (VEGFR2) is a receptor tyrosine kinase primarily expressed on endothelial cells and is the dominant mediator of vascular endothelial growth factor (VEGF)-induced angiogenesis, vascular permeability, and endothelial cell proliferation. Integrin αvβ3 is a cell surface adhesion receptor that binds to extracellular matrix proteins containing an RGD motif, such as vitronectin, and plays critical roles in cell adhesion, migration, survival, and also in angiogenesis. Both VEGFR2 and integrin αvβ3 are extensively studied therapeutic targets in cancer, cardiovascular, and ocular diseases due to their role in pathological angiogenesis. Importantly, these two receptor classes engage in biochemical cross-talk—activation of integrin αvβ3 enhances VEGFR2 phosphorylation and downstream signaling, and direct complexes between these proteins occur in the context of endothelial cell migration and vessel formation[1][2][3]. Numerous drugs, especially kinase inhibitors, monoclonal antibodies, and synthetic peptides, have been developed to target these pathways individually or in combination, though translational challenges have emerged in both efficacy and safety[1][4][5].

Other names

Kinase insert domain receptor (KDR)Flk-1 (murine)Fetal liver kinase 1CD309vitronectin receptorCD51/CD61

VEGFR2: Inhibition of receptor tyrosine kinase activity, blockade of VEGF ligand binding, inhibition of downstream angiogenic signaling, suppression of endothelial proliferation | Integrin αvβ3: Blockade of cell adhesion to extracellular matrix, inhibition of angiogenesis, interference with integrin-mediated signaling pathways, disruption of cell migration