Glycoprotein Ib-IX-V complex (GPIb-IX-V) (GPIb-IX-V)

The Glycoprotein Ib-IX-V (GPIb-IX-V) complex is a specialized adhesion receptor complex expressed on the surface of platelets and megakaryocytes (UniProt: P07359). It is composed of four distinct subunits: GPIbα, GPIbβ, GPIX, and GPV, which are required for the stable expression and function of the complex (PubMed: 28235853). The primary function of the complex is to mediate the initial attachment of platelets to the subendothelial matrix by binding to von Willebrand factor (vWF) under high shear stress conditions (StatPearls: NBK493163). This interaction is crucial for hemostasis but also drives pathological arterial thrombosis in conditions such as ischemic stroke and myocardial infarction (PubMed: 30104231). Genetic mutations leading to the absence or dysfunction of the complex result in Bernard-Soulier syndrome, characterized by giant platelets and severe bleeding (NIH: GARD). Therapeutic targeting of the GPIb-IX-V complex, particularly the vWF-binding site on GPIbα, is an active area of research for developing potent anti-thrombotic agents with a reduced risk of bleeding compared to standard-of-care antiplatelet therapies (PubMed: 26450434).

Other names

CD42 complexvon Willebrand factor receptorGPIb-V-IXGP Ib-IX-VGlycoprotein Ib-V-IX complex

Inhibition of the interaction between the A1 domain of von Willebrand factor (vWF) and the N-terminal domain of the GPIb-alpha subunit, thereby preventing platelet tethering and rolling on the vascular subendothelium under high shear stress (PubMed: 26450434).