Glycoprotein Ib (GP Ib), or CD42b, is a platelet surface membrane glycoprotein composed of a heterodimer, an alpha chain and a beta chain, that is linked by disulfide bonds. CD42b functions as a receptor for von Willebrand factor (VWF). The complete receptor complex includes noncovalent association of the alpha and beta subunits with platelet glycoprotein IX and platelet glycoprotein V. The binding of the GP Ib-IX-V complex to VWF facilitates initial platelet adhesion to vascular subendothelium after vascular injury, and it also initiates signaling events within the platelet that lead to enhanced platelet activation, thrombosis, and hemostasis. Several mutations have been described in CD42b, some of which are the cause of Bernard-Soulier syndromes and platelet-type von Willebrand disease (1).
Hematopoietic cell lineage
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