Integrin alpha-V beta-3 and Integrin alpha-5 beta-1 (Integrin αVβ3 and Integrin α5β1)

Integrin alpha-V beta-3 and Integrin alpha-5 beta-1 are heterodimeric transmembrane receptors of the integrin family, composed of α and β subunits (αV with β3; α5 with β1), that mediate cell adhesion to extracellular matrix proteins and transduce signals to regulate cell migration, survival, and proliferation[3][5][6][7]. Integrin αVβ3, often called the vitronectin receptor, binds vitronectin, fibronectin, fibrinogen, osteopontin, and other ligands, and is prominently involved in angiogenesis and metastasis, especially in tumor and activated endothelial cells[5][6][2]. Integrin α5β1 is the primary fibronectin receptor and plays a central role in cell adhesion, migration, development, and wound healing by specifically recognizing the RGD motif in fibronectin[4][7][9]. Both integrins regulate not only physical cell-matrix adhesion but also intracellular signaling pathways, influencing cytoskeletal remodeling and cell fate decisions[4][6]. They are validated therapeutic targets in oncology (anti-angiogenic and anti-metastatic therapies) and other diseases with pathological tissue remodeling, but safety issues, including effects on normal cell survival and bleeding risk, have limited clinical success[3][6].

Other names

Vitronectin receptorαVβ3 integrinITGAV-ITGB3Fibronectin receptorα5β1 integrinITGA5-ITGB1

Antagonists/blockers inhibit integrin-ligand binding, disrupting cell adhesion, migration, angiogenesis, and metastasis. Some drugs induce conformational change to interfere with receptor activation.