Platelet glycoprotein Ib-IX-V complex (GPIb-IX-V) (GPIb-IX-V)

The Platelet glycoprotein Ib-IX-V (GPIb-IX-V) complex is a multi-subunit adhesion receptor essential for platelet function and hemostasis (UniProt P07359). It is composed of four transmembrane polypeptides: GPIbα, GPIbβ, GPIX, and GPV, which are non-covalently associated on the platelet surface (PubMed: 15102718). The primary role of this complex is to mediate the initial attachment (tethering and rolling) of platelets to the vascular wall by binding to von Willebrand factor (vWF) immobilized on exposed subendothelial collagen, particularly under high-shear blood flow conditions (PubMed: 11781230). Beyond its role in adhesion, the complex also serves as a signaling receptor and a binding site for other ligands such as thrombin, P-selectin, and coagulation factors XI and XII (PubMed: 24553176). Genetic deficiencies or defects in the components of the GPIb-IX-V complex result in Bernard-Soulier syndrome, a severe bleeding disorder characterized by macrothrombocytopenia (StatPearls: NBK459318). Because of its critical role in arterial thrombosis, the complex is a significant target for the development of next-generation antithrombotic drugs, such as Anfibatide, designed to prevent clot formation in high-shear environments like stenosed arteries while minimizing systemic bleeding risks (PubMed: 26359251).

Other names

GPIb-V-IX complexCD42 complexvon Willebrand factor receptorGlycoprotein Ib-IX-VGPIb-IX-V complex

Inhibition of the interaction between the von Willebrand factor (vWF) A1 domain and the N-terminal domain of the GPIbα subunit to prevent platelet tethering and rolling under high shear stress.