GP1BB Human

Glycoprotein Ib Platelet Subunit Beta (GPIbβ) is a crucial component of the GPIb-IX-V complex, which plays a significant role in the process of hemostasis and thrombosis. This complex is found on the surface of platelets and is essential for the initial adhesion of platelets to the site of vascular injury.

The GPIb-IX-V complex is composed of four subunits: GPIbα, GPIbβ, GPIX, and GPV. GPIbβ, specifically, is a transmembrane protein that forms a disulfide bond with GPIbα. This bond is critical for the stability and function of the entire complex .

The primary function of the GPIb-IX-V complex is to mediate the initial interaction between platelets and the subendothelial von Willebrand factor (VWF) at sites of vascular injury. This interaction is crucial for platelet adhesion, which is the first step in the formation of a blood clot . The binding of VWF to the GPIb-IX-V complex not only facilitates platelet adhesion but also initiates intracellular signaling pathways that lead to platelet activation and aggregation .

Mutations or deficiencies in the GPIbβ subunit can lead to bleeding disorders such as Bernard-Soulier syndrome (BSS). BSS is characterized by a deficiency in the GPIb-IX-V complex, leading to impaired platelet adhesion and prolonged bleeding times . Additionally, the GPIb-IX-V complex has been implicated in various physiological and pathophysiological processes, including immune surveillance, hepatic thrombopoietin generation, and platelet clearance .

Human recombinant GPIbβ is produced using recombinant DNA technology, which allows for the expression of the protein in various host systems. This recombinant protein is used in research to study the structure and function of the GPIb-IX-V complex, as well as in the development of therapeutic agents for bleeding disorders .