Integrin heterodimer

Integrin heterodimers are transmembrane receptors composed of noncovalently associated α (alpha) and β (beta) subunits that mediate cell-cell and cell-extracellular matrix (ECM) adhesion[2][5][6]. In mammals, 18 α and 8 β subunits pair to form 24 distinct integrin heterodimers, each with unique ligand specificity and tissue distribution[5][6]. Integrins facilitate bidirectional signal transduction: "outside-in" signaling influences cytoskeletal organization, cell proliferation, survival, and migration, while "inside-out" signaling modulates integrin affinity for ligands in response to intracellular cues[1][2][3]. Structurally, each subunit contains a large extracellular domain for ligand binding, a single transmembrane helix, and a short cytoplasmic tail that interacts with cytoskeletal and signaling proteins[1][2][4]. Integrins are critically involved in embryonic development, immune responses, wound healing, and hemostasis; their dysregulation is implicated in diverse diseases, including cancer, inflammation, cardiovascular disorders, and autoimmune conditions[4][5][6]. Several therapeutic agents, particularly monoclonal antibodies and small-molecule antagonists, target specific integrin heterodimers in clinical practice, but inhibition may carry risks of infection and bleeding[6].

Other names

IntegrinIntegrin receptorαβ integrinIntegrin αβ heterodimer

Inhibition of ligand binding to integrin extracellular domain; Blockade of integrin-mediated cell adhesion; Modulation of intracellular signaling pathways