Integrin alpha-2 (ITGA2) (ITGA2)

Integrin alpha-2 (ITGA2), also known as CD49b, is a transmembrane glycoprotein that non-covalently pairs with the integrin beta-1 subunit to form the alpha-2-beta-1 (α2β1) heterodimer (UniProt: P17301). This complex serves as a primary receptor for collagen and laminin, playing a critical role in cell-extracellular matrix (ECM) adhesion, platelet aggregation, and tissue remodeling (NCBI Gene: 3673). In the vascular system, α2β1 is essential for platelet adhesion to injured vessel walls, while in other tissues, it regulates cell migration and survival (PubMed: 22535016). Pathologically, ITGA2 is implicated in cancer progression, where its overexpression facilitates tumor cell invasion and metastasis, and in inflammatory diseases (PubMed: 25650541). Therapeutic strategies targeting ITGA2 focus on inhibiting its collagen-binding domain to treat thrombotic disorders or prevent cancer spread, though such interventions must balance efficacy with the risk of impaired hemostasis (ClinicalTrials.gov: NCT01450449).

Other names

CD49bVLA-2 alpha subunitPlatelet membrane glycoprotein IaGPIaBRALLHPA-5Very late activation protein 2

Inhibition of the alpha-2-beta-1 integrin complex to block binding to collagen and other extracellular matrix ligands, thereby preventing platelet adhesion and tumor cell migration.