Integrin receptors

Integrin receptors are a family of heterodimeric transmembrane receptors composed of non-covalently associated alpha (α) and beta (β) subunits. They are located on the cell surface and mediate interactions between cells and their surrounding extracellular matrix (ECM). Integrins play crucial roles in cell adhesion, signal transduction (outside-in and inside-out), cytoskeletal organization, cell migration, cell cycle regulation, platelet aggregation (e.g., αIIbγ3), and can also serve as receptors for certain viruses. Their extracellular domains interact with ECM components like fibronectin, laminin, and collagen. They are involved in various signaling pathways including FAK, ILK, PI3K/Akt, MAPK, and Rho GTPases. Due to their widespread roles in physiological and pathological processes, including cancer, autoimmune disorders, and inflammatory conditions, integrins are important therapeutic targets. Approaches include therapeutic antibodies, peptide-based drugs, and small molecule peptidomimetics. Several integrin-targeting drugs, such as Abciximab, Vedolizumab, and Lifitegrast, have received FDA approval.

Modulation of cell adhesion and signaling by binding to integrin receptors, typically acting as antagonists or inhibitors to block ligand binding or receptor function.