Endothelial cell surface integrins and vascular endothelial growth factor (VEGF) pathway proteins (Integrin-VEGF axis)

This target group comprises a complex network of cell surface receptors and signaling ligands that cooperatively regulate angiogenesis, the physiological process of new blood vessel formation. Endothelial cell surface integrins, particularly the alpha-v beta-3 and alpha-v beta-5 heterodimers, mediate the attachment of endothelial cells to the extracellular matrix, providing essential mechanical and biochemical signals for survival and migration (Desgrosellier & Cheresh, 2010, Nature Reviews Cancer). The Vascular Endothelial Growth Factor (VEGF) pathway, centered on the interaction between VEGF-A and its primary receptor VEGFR2, acts as the dominant driver of endothelial cell proliferation and vascular permeability (Apte et al., 2019, JAMA). Functional synergy and physical crosstalk between integrins and VEGF receptors are well-documented, where integrins can serve as co-receptors that amplify VEGFR2 signaling (Soldi et al., 1999, EMBO Journal). In pathological conditions such as solid tumor growth and neovascular age-related macular degeneration, this axis is frequently overactivated, leading to the development of leaky, disorganized vasculature. Therapeutic interventions targeting these proteins, including monoclonal antibodies like bevacizumab and various tyrosine kinase inhibitors, aim to inhibit these pathways to suppress tumor growth or prevent vision loss (Ferrara & Adamis, 2016, Nature Reviews Drug Discovery).

Other names

Angiogenic receptorsVEGF-Integrin signaling complexEndothelial adhesion and growth factor receptors

Inhibition of VEGF ligand binding to VEGFR, blockade of VEGFR tyrosine kinase activity, and antagonism of integrin-mediated cell adhesion to the extracellular matrix.