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Integrin alpha-V beta-1 (αVβ1) is a heterodimeric transmembrane receptor composed of αV (ITGAV) and β1 (ITGB1) subunits. Integrins mediate cell adhesion by linking the extracellular matrix to the cytoskeleton and participating in bidirectional signal transduction[6]. Although αVβ1 can bind fibronectin (an important extracellular matrix component), its affinity and capacity to promote fibronectin matrix assembly and cell migration are substantially lower than those of α5β1 integrin[6][8]. In cell models, αVβ1 does not localize to focal adhesions and fails to support robust cell migration or fibronectin matrix assembly as α5β1 does, highlighting functional differences between integrin heterodimers with similar ligand specificities[8]. As a result, αVβ1 is not as well recognized as a distinct functional or therapeutic target compared to more widely studied integrins such as αVβ3, α5β1, or αIIbβ3[6][8]. *Note:* If your intent was to refer to integrin αVβ3, αVβ5, or α5β1, which are all major fibronectin or vitronectin receptors and important drug targets, then "integrin αV/β1" may be an error[6][8]. For rigor and utility, future queries should specify the individual well-characterized heterodimeric integrin, e.g., α5β1 receptor or αVβ3 receptor.
Inhibition of integrin-ligand binding (general for integrin-targeting drugs) Blockade of extracellular matrix interaction
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