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Integrin alpha-V beta-3 receptor and Integrin alpha-V beta-5 receptor are transmembrane receptors composed of an alpha and beta chain, classified within the integrin family. They mediate cell adhesion by binding to extracellular matrix proteins such as vitronectin and fibronectin, and facilitate processes including cell migration, signal transduction, and angiogenesis. Both receptors are widely expressed on endothelial cells, fibroblasts, epithelial cells, immune cells, and certain tumor cells. Their abnormal expression and function have been implicated in cancer progression, pathological angiogenesis, fibrosis, and inflammatory diseases. Therapeutically, these integrins are targeted to inhibit vascularization in tumors and modulate inflammation. Drugs targeting these receptors block ECM ligand binding or induce apoptosis, and have been studied as anti-cancer and anti-fibrotic agents. Safety concerns include the potential for delayed wound healing and immunological side effects due to their important roles in normal tissue homeostasis[2][3][4][5][6][7][9].
Blockade of ligand binding (especially inhibition of vitronectin/fibronectin interactions); Inhibition of angiogenesis; Induction of apoptosis (ProAgio recruits caspase 8 after binding); Interference with signal transduction required for cell migration, survival, proliferation.
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