Integrin alpha-4 beta-1 and Integrin alpha-V beta-3 (α4β1 integrin and αVβ3 integrin)

Integrin alpha-4 beta-1 and Integrin alpha-V beta-3 are members of the integrin superfamily of cell adhesion receptors, composed of non-covalently linked α and β subunits (encoded by ITGA4/ITGB1 and ITGAV/ITGB3, respectively)[4][5][6][7]. These receptors mediate cell-extracellular matrix and cell-cell adhesion, which are essential for cell migration, immune cell trafficking, and angiogenesis. The α4β1 integrin is particularly important in lymphocyte homing and inflammatory responses, whereas αVβ3 is critical in angiogenesis and tumor cell invasion. Both are actively pursued as therapeutic targets in cancer, autoimmune, and cardiovascular diseases, with several clinical agents developed to modulate their function. Their structure includes an extracellular domain that binds ligands (such as fibronectin, VCAM-1, vitronectin, and others), a single transmembrane helix per subunit, and short cytoplasmic tails that connect to the cytoskeleton and trigger intracellular signaling upon activation[1][2][3][4][6][7].

Other names

Integrin α4β1: Very late antigen-4 (VLA-4)CD49d/CD29Integrin αVβ3: Vitronectin receptorCD51/CD61

Antagonists block integrin-ligand binding, inhibiting cell adhesion and migration - Inhibition of signal transduction pathways downstream of integrin engagement - Suppression of angiogenesis and/or immune cell infiltration depending on disease context