Integrin alpha-5 beta-1 receptor\nIntegrin alpha-V beta-3 receptor\nIntegrin alpha-V beta-5 receptor (Integrin α5β1\nIntegrin αvβ3\nIntegrin αvβ5)

Integrin alpha-5 beta-1 (α5β1), alpha-V beta-3 (αvβ3), and alpha-V beta-5 (αvβ5) are heterodimeric, transmembrane cell surface receptors that mediate cell adhesion to extracellular matrix proteins. α5β1 is the primary fibronectin receptor and plays a fundamental role in cell migration, adhesion, and cytoskeletal organization. αvβ3 and αvβ5 are vitronectin receptors, contributing to cell adhesion, migration, and angiogenesis, and are differentially expressed/distributed on the cell surface. All three integrins participate in "outside-in" and "inside-out" signaling, regulating crucial cellular processes. Their dysregulation has been implicated in cancer, inflammation, fibrosis, and other diseases, making them therapeutic targets for antibody, peptide, and small-molecule inhibitors.

Other names

α5β1 integrinαvβ3 integrinαvβ5 integrinFibronectin receptor (primarily α5β1)Vitronectin receptor (primarily αvβ3, αvβ5)

Inhibition of ligand binding (e.g., RGD sequence in fibronectin or vitronectin is blocked); Disruption of cell-ECM interaction; Inhibition of angiogenesis (blocking endothelial cell attachment/migration); Induction of apoptosis via loss of matrix attachment (anoikis)