Integrin (cell surface receptor for extracellular matrix proteins) (Integrin)

Integrins are heterodimeric transmembrane receptors that anchor cells to the extracellular matrix and mediate mechanical and chemical signaling between the ECM and the cell interior[1][2][4][5]. Each integrin consists of one α and one β subunit[3]. They recognize and bind to ECM proteins such as collagen, fibronectin, and laminin, and their activation leads to clustering, formation of adhesion complexes, and initiation of intracellular signaling cascades controlling survival, proliferation, migration, and differentiation[1][2][3][4][5]. Integrins are central regulators of tissue architecture, gene expression, and disease pathogenesis, and are targeted by multiple therapeutic agents in cancer, thrombosis, and chronic inflammatory conditions[3][5]. The phrase "Extracellular matrix proteins / Cell surface integrins" lacks canonical specificity, as the target for therapeutic intervention is almost always an integrin, not the whole ECM protein class[1][3][6].

Other names

Cell adhesion receptorsECM receptorsIntegrin receptorsHeterodimeric cell surface receptorsβ1-integrin

Antagonism/blockade of integrin-ligand binding (prevents cell adhesion, migration, thrombosis); Modulation of integrin signaling pathways (alters cell survival, proliferation, cytokine release); Inhibition of integrin-mediated activation of intracellular kinases (e.g., Src, FAK); Induction of apoptosis or detachment (in cancer therapy)