Int J Biochem Cell Biol. 2003 Aug;35(8):1170-4.

Glycoprotein Ib-IX-V.

Andrews RK, Gardiner EE, Shen Y, Whisstock JC, Berndt MC.

Source

Vascular Biology Laboratory, Department of Biochemistry and Molecular Biology, Monash University, Clayton, Vic. 3168, Australia. rob.andrews@med.monash.edu.au

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.

PMID:: 12757754; [PubMed - indexed for MEDLINE]

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