CD51/Integrin alpha V

CD51, the integrin alpha V chain, dimerizes with beta subunits (beta 1, beta 3, beta 5, beta 6 or beta 8) to form receptors for RGD motif-containing matrix proteins including vitronectin, fibronectin, osteopontin and latent TGF-beta. Expressed on endothelial cells, osteoclasts, fibroblasts, platelets and subsets of leukocytes, alpha V integrins govern angiogenesis, bone resorption, wound repair and phagocytosis of apoptotic cells. The alpha V beta 6 and alpha V beta 8 receptors activate latent transforming growth factor beta, linking matrix contact to fibrosis and immune regulation. Integrin alpha V antagonists have been pursued as anti-angiogenic therapeutics in oncology.