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Integrin subunit alpha V beta 3 (αVβ3), also known as the vitronectin receptor, is a heterodimeric integral membrane protein composed of alpha V (ITGAV/CD51) and beta 3 (ITGB3/CD61) subunits. It functions primarily in cell surface adhesion and signaling by binding ligands such as vitronectin, fibronectin, fibrinogen, osteopontin, and von Willebrand factor via the RGD sequence, facilitating processes like platelet aggregation, angiogenesis, and phagocytosis in macrophages and dendritic cells. Expressed on platelets, endothelial cells, and tumor cells, αVβ3 plays a critical role in vascular remodeling and tumor progression by promoting endothelial cell migration and survival. In disease, its overexpression is linked to pathological angiogenesis in cancer, supporting tumor growth through enhanced blood supply, and it serves as an entry receptor for various pathogens including coxsackievirus, herpes virus 8, and West Nile virus. As a therapeutic target, inhibitors like the monoclonal antibody etaracizumab block αVβ3 to suppress angiogenesis in cancers and other neovascular conditions, though clinical development has faced challenges in efficacy demonstration.
Antiangiogenic inhibition of integrin signaling
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