Integrin alpha-IIb (ITGA2B) (ITGA2B)

Integrin alpha-IIb (ITGA2B), commonly known as Glycoprotein IIb (GPIIb), is a transmembrane protein that plays a pivotal role in blood coagulation and hemostasis [UniProt P08514]. It non-covalently associates with Integrin beta-3 (GPIIIa) to form the heterodimeric GPIIb/IIIa receptor complex, which is expressed exclusively on the surface of platelets and megakaryocytes [NCBI Gene: 3674]. Upon platelet activation, this receptor undergoes a conformational change that allows it to bind with high affinity to soluble fibrinogen and von Willebrand factor, serving as the final common pathway for platelet aggregation [StatPearls: Glycoprotein IIb/IIIa Inhibitors]. Due to its central role in thrombus formation, GPIIb/IIIa is a major therapeutic target for antiplatelet drugs used in the management of acute coronary syndromes and during percutaneous coronary intervention [PubMed: PMID 11010007]. Drugs such as abciximab, eptifibatide, and tirofiban act as antagonists to this receptor, preventing the cross-linking of platelets and the subsequent formation of arterial thrombi [DrugBank: DB00054]. Genetic deficiencies in the ITGA2B gene lead to Glanzmann thrombasthenia, a condition characterized by impaired platelet aggregation and a high risk of bleeding [NIH: MedlinePlus]. While effective in preventing ischemic events, the use of GPIIb/IIIa inhibitors is limited by safety concerns, including an increased risk of major hemorrhage and the potential for drug-induced thrombocytopenia [PubMed: PMID 15130912].

Other names

Glycoprotein IIbGPIIbCD41Platelet membrane glycoprotein IIbGP2BAntigen CD41Integrin alpha-2b

Antagonism of the integrin alpha-IIb/beta-3 receptor complex, which prevents the binding of fibrinogen and von Willebrand factor to activated platelets, thereby inhibiting the final common pathway of platelet aggregation [StatPearls: Glycoprotein IIb/IIIa Inhibitors].