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Integrins are a superfamily of cell surface receptors that function as heterodimers, consisting of non-covalently linked alpha and beta subunits [UniProt: P05556]. They serve as the primary mechanical link between the intracellular cytoskeleton and the extracellular matrix, facilitating bidirectional inside-out and outside-in signaling [PubMed: 11931770]. This signaling is crucial for regulating cell survival, proliferation, and migration. In various diseases, integrins are implicated in promoting tumor growth, facilitating leukocyte extravasation in inflammation, and mediating platelet aggregation in thrombosis [NCBI: NBK26810]. Therapeutic strategies targeting integrins include monoclonal antibodies and small molecule inhibitors designed to block ligand-receptor interactions [PubChem: 135314782]. While effective in treating conditions like Crohn's disease and acute coronary syndrome, these therapies require careful monitoring for adverse effects such as immunosuppression or hematological issues [PubMed: 24633158].
Integrin inhibitors primarily act as competitive antagonists that bind to the extracellular headpiece of the integrin heterodimer, preventing the binding of ligands such as RGD-containing proteins or cell-surface adhesion molecules [PubMed: 28839151].
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