| Literature DB >> 12757754 |
R K Andrews1, E E Gardiner, Y Shen, J C Whisstock, M C Berndt.
Abstract
Glycoprotein (GP) Ib-IX-V is a remarkable platelet adhesion receptor of the leucine-rich repeat family. It has evolved to fulfil its major function of initiating platelet aggregation (thrombus formation) at high-shear stress in flowing blood. In addition to binding von Willebrand factor (vWF) in subendothelial matrix or plasma to trigger platelet aggregation, GPIb-IX-V also binds counter-receptors, alphaMbeta2 (Mac-1) on neutrophils or P-selectin on activated platelets or endothelial cells. GPIb-IX-V ligands also include alpha-thrombin, clotting factors XI/XIIa, and high-molecular-weight kininogen. Interactions involving GPIb-IX-V are therefore central to vascular processes of thrombosis and inflammation, and the receptor is under intense scrutiny as a potential therapeutic target.Entities:
Mesh：
Substances：
Year: 2003 PMID： 12757754 DOI： 10.1016/s1357-2725(02)00280-7
Source DB: PubMed Journal: Int J Biochem Cell Biol ISSN： 1357-2725 Impact factor: 5.085