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

The Glycoprotein Ib-IX-V (GPIb-IX-V) receptor is a specialized adhesion complex expressed on the surface of platelets and megakaryocytes, playing a pivotal role in primary hemostasis (Quach & Li, 2020, JTH). It is composed of four subunits—GPIbα, GPIbβ, GPIX, and GPV—which assemble to form a functional receptor for von Willebrand factor (vWF) (UniProt P07359). The interaction between the N-terminal domain of GPIbα and the A1 domain of vWF is essential for platelet tethering and rolling on the damaged vessel wall, especially under high-shear conditions typical of arterial flow (StatPearls, 2023). Beyond adhesion, the complex also serves as a signaling hub, interacting with various ligands like thrombin and P-selectin to promote coagulation and inflammation (PubMed, PMID: 31550395). Pathologically, the GPIb-IX-V receptor is central to the development of arterial thrombosis, which can lead to myocardial infarction and ischemic stroke. Genetic defects in the complex result in Bernard-Soulier syndrome, a severe bleeding disorder characterized by macrothrombocytopenia (NIH, GARD). Because of its unique role in the early stages of thrombus formation, the receptor is a high-interest therapeutic target for next-generation antiplatelet drugs. Inhibitors such as anfibatide and various monoclonal antibodies aim to prevent thrombosis while potentially minimizing the bleeding complications associated with broader-acting antiplatelet therapies (ClinicalTrials.gov, NCT04022538).

Other names

CD42 complexvon Willebrand factor receptorGPIb-V-IX complexGlycoprotein Ib-IX-V complex

Inhibition of the interaction between the GPIbα subunit and the A1 domain of von Willebrand factor (vWF), thereby preventing platelet adhesion and subsequent thrombus formation under high shear stress.