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Integrins are heterodimeric transmembrane receptors consisting of α and β subunits that connect cells to the extracellular matrix by binding ECM proteins such as collagen, fibronectin, and laminin. They function as structural anchors and as major signal transducers, enabling cells to sense and respond to biochemical and mechanical properties of their environment. Integrins are vital for cell survival, migration, proliferation, and tissue integrity, and play roles in normal development, wound healing, immune responses, and a wide variety of diseases including cancer, fibrosis, cardiovascular disease, and inflammation. Multiple integrin subtypes exist, and their biological effects depend on their specific α/β combinations and tissue context. Integrin-targeting drugs exploit their roles in cell migration and adhesion, but clinical use is sometimes limited by infection and bleeding risks.
Inhibition of integrin-ligand binding prevents cell adhesion, migration, or immune cell trafficking; Antagonism disrupts platelet aggregation (for anti-thrombotic drugs); Direct modulation of intracellular signaling pathways (FAK, PI3K/Akt, MAPK)
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