Glycoprotein Ib-IX-V.
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.
Andrews
R K
RK
Vascular Biology Laboratory, Department of Biochemistry and Molecular Biology, Monash University, Clayton, Vic. 3168, Australia. rob.andrews@med.monash.edu.au
Gardiner
E E
EE
Shen
Y
Y
Whisstock
J C
JC
Berndt
M C
MC
D000818:Animals; D001665:Binding Sites; D006801:Humans; D010974:Platelet Aggregation; D019038:Platelet Glycoprotein GPIb-IX Complex / Q000737:chemistry / Q000378:metabolism*; D020836:Protein Structure, Quaternary; D013927:Thrombosis / Q000097:blood; D014841:von Willebrand Factor / Q000378:metabolism
D019038:Platelet Glycoprotein GPIb-IX Complex; D014841:von Willebrand Factor