Integrin alpha-V beta-5 and integrin alpha-5 beta-1 (alphaVbeta5 and alpha5beta1)

Integrins alpha-V beta-5 and alpha-5 beta-1 are heterodimeric cell surface receptors that mediate critical interactions between cells and the extracellular matrix (ECM). Both belong to the RGD-binding subfamily of integrins, recognizing the Arginine-Glycine-Aspartic acid motif in ligands such as vitronectin and fibronectin. These receptors are essential for physiological processes including angiogenesis, cell migration, and survival signaling. In pathological states, particularly cancer and fibroproliferative disorders, they are frequently overexpressed on both tumor cells and the neovasculature, where they promote tumor growth, metastasis, and resistance to therapy. Therapeutic strategies targeting these integrins include monoclonal antibodies and small molecule inhibitors designed to block ligand binding or disrupt receptor stability, thereby inhibiting pro-tumorigenic signaling pathways like FAK/Src and Rac1.

Other names

Vitronectin receptor (alphaVbeta5)Fibronectin receptor (alpha5beta1)VLA-5 (Very Late Antigen-5)CD49e/CD29ITGAV/ITGB5 and ITGA5/ITGB1

Antagonism of ligand binding (RGD-mimetic), inhibition of angiogenesis, disruption of heterodimer stability, and inhibition of downstream signaling pathways such as FAK/Src, ERK, and Rac1 to induce apoptosis in endothelial and tumor cells.