Integrin alpha-V receptor (αv integrin)

Integrin alpha-V receptor is a cell-surface heterodimeric transmembrane receptor encoded by the ITGAV gene, which pairs with various beta subunits (β1, β3, β5, β6, β8) to form several integrin receptors, each mediating specific biological processes. It plays essential roles in cell adhesion, interaction with the extracellular matrix, and bidirectional signal transduction governing cell migration, proliferation, survival, and angiogenesis. As a central mediator of cancer progression and tumor angiogenesis, it acts as a major therapeutic target in oncology, particularly in tumors where αv integrins are overexpressed. Drugs such as cilengitide inhibit αv integrins, aiming to disrupt tumor growth and vascularization. However, clinical use poses safety considerations due to integrin function in normal tissues. The αvβ3 heterodimer, also known as the vitronectin receptor, is the most studied αv-containing integrin, but other pairings are also therapeutically important in cancer and fibrosis.

Other names

Integrin alpha-VITGAVαv integrinCD51Vitronectin receptor (when heterodimerized with beta 3 as αvβ3)

Inhibition of integrin–ligand interactions (e.g., blocking binding of vitronectin, fibronectin, or RGD sequence in ECM proteins) Disruption of integrin-mediated signal transduction essential for angiogenesis, tumor progression, and metastasis Blockade of integrin activation impairs cell adhesion, migration, survival, and neovascularization