Integrin alpha-V beta-3 (αvβ3) and Integrin alpha-V beta-5 (αvβ5) receptor (αvβ3 and αvβ5)

Integrin alpha-V beta-3 and alpha-V beta-5 receptors are type I transmembrane heterodimers consisting of the αv subunit paired with β3 or β5, respectively. They mediate cell adhesion by binding to RGD-containing extracellular matrix proteins such as vitronectin, fibronectin, and others, and are crucial for cell migration, tissue invasion, and angiogenesis. Their distribution and function on the cell surface differ: αvβ3 is enriched at focal contacts involved in cytoskeletal attachment, while αvβ5 is found in different membrane domains. Both integrins are upregulated in proliferating endothelial cells, some cancers, and during tissue remodeling; they participate in signal transduction pathways leading to changes in cell survival, proliferation, differentiation, and immune responses. Drug development is focused on exploiting their role in angiogenesis and tumor growth, but therapeutic targeting is challenged by essential functions in normal tissue homeostasis and repair.

Other names

Vitronectin receptor (primarily for αvβ3)αvβ3 integrin, αvβ5 integrinITGAV/ITGB3 (αvβ3), ITGAV/ITGB5 (αvβ5) (gene-based aliases)

Ligand mimicry: competitive inhibition of binding to extracellular matrix proteins (e.g., vitronectin, fibronectin) by mimicking the RGD motif; Blocking integrin-mediated signal transduction and cell adhesion; Inhibition of angiogenesis and tumor cell migration