Integrin alpha-V beta-5 receptor (Integrin αVβ5)

Integrin alpha-V beta 5 is a heterodimeric transmembrane glycoprotein composed of an alpha V subunit (encoded by ITGAV) and a beta 5 subunit (encoded by ITGB5). It belongs to the large family of integrins—cell surface receptors that mediate attachment between cells and components of the extracellular matrix. The primary ligand for this receptor is vitronectin, but it can also bind other RGD-motif-containing proteins.\n\nIntegrin alpha-V beta 5 plays essential roles in mediating cell adhesion, signal transduction from the extracellular environment into cells ("outside-in" signaling), regulation of cell migration/invasion during development or disease progression, phagocytosis in retinal pigment epithelial cells critical for vision maintenance, angiogenesis, tissue repair, immune response modulation, and fibrosis.\n\nIt is widely expressed on fibroblasts, epithelial cells—including those lining blood vessels—and certain cancer types such as hepatomas and carcinomas. Overexpression has been linked to poor prognosis in glioblastoma multiforme due to its involvement in tumor progression pathways including immune response regulation and neovascularization.\n\nThe receptor also serves as an entry point for certain viruses including adenovirus type C.\n\nTherapeutically targeting this molecule remains under investigation primarily within oncology—for antiangiogenic strategies—and fibrotic diseases.

Other names

Integrin αVβ5ITGAV:ITGB5Vitronectin receptor (less commonly for this specific dimer, more often for αVβ3)CD51/CD105 (CD51 is the alpha-V subunit)

Drugs or biologics targeting integrin alpha-V beta 5 typically act by inhibiting its interaction with ligands such as vitronectin, thereby blocking downstream signaling involved in angiogenesis, tumor cell migration/invasion, or fibrosis. Some agents may also block viral entry mediated by this receptor.