Integrin alpha-V beta-3 or Integrin alpha-V beta-5 (Integrin αVβ3, Integrin αVβ5)

Integrin alpha-V beta-3 and alpha-V beta-5 are transmembrane adhesion receptors—members of the integrin family—composed of non-covalently associated α (ITGAV, CD51) and β (ITGB3/CD61 or ITGB5) subunits[1][2][7][8]. They mediate cell attachment to extracellular matrix proteins, primarily vitronectin, fibronectin, osteopontin, fibrinogen, and can also act as entry receptors for certain viruses[1][2][5][6]. αVβ3 is prominent in endothelial cells, osteoclasts, and platelets, and is strongly implicated in angiogenesis, while αVβ5 is prevalent in fibroblasts and epithelial cells and has a key role in cell migration and organization during development[2][5]. Both are validated therapeutic targets in cancer, given their roles in tumor-driven angiogenesis and metastasis, and are the focus of several clinical-stage inhibitors and antibodies[7]. Their blockade disrupts integrin-mediated signaling, cell adhesion, and survival, but can affect physiological angiogenesis and normal tissue remodeling, raising notable safety considerations[7][1].

Other names

Vitronectin receptor (primarily for αVβ3)ITGAV/ITGB3/ITGB5αvβ3αvβ5CD51/CD61 (for αvβ3)VNR

Inhibition of cell adhesion to extracellular matrix via RGD motif antagonism; Blockade of angiogenesis through disruption of integrin-mediated signaling; Induction of apoptosis in targeted cells (e.g., by ProAgio via caspase-8 recruitment)[7][6]; Disruption of tumor cell migration and invasiveness