Structure-function of platelet glycoprotein Ib-IX

Abstract

The glycoprotein (GP)Ib-IX receptor complex plays a critical role in platelet physiology and pathology. Its interaction with von Willebrand factor (VWF) on the subendothelial matrix instigates platelet arrest at the site of vascular injury and is vital to primary hemostasis. Its reception to other ligands and counter-receptors in the bloodstream also contribute to various processes of platelet biology that are still being discovered. While its basic composition and its link to congenital bleeding disorders were well documented and firmly established more than 25 years ago, recent years have witnessed critical advances in the organization, dynamics, activation, regulation, and functions of the GPIb-IX complex. This review summarizes important findings and identifies questions that remain about this unique platelet mechanoreceptor complex.