Glycoprotein IX
Glycoprotein IX (GP IX) is a small platelet membrane glycoprotein that forms a 1-to-1 noncovalent complex with glycoprotein Ib (GP Ib), which is a component of the GP Ib-IX-V complex. GP IX, synthesized in megakaryocytes, circulates in the plasma as part of the GP Ib-IX-V complex, which is crucial for platelet adhesion to the subendothelium.
Structure[edit | edit source]
GP IX is a single-pass type I membrane protein. It interacts with glycoprotein Ib alpha and glycoprotein Ib beta to form a complex that is critical for platelet adhesion to the vascular endothelium. The GP Ib-IX-V complex binds to von Willebrand factor, allowing platelet adhesion and aggregation at sites of vascular injury.
Function[edit | edit source]
The primary function of GP IX is to contribute to the stability of the GP Ib-IX-V complex. This complex is essential for the process of platelet aggregation, which is a crucial step in the formation of a hemostatic plug during the process of blood coagulation.
Clinical significance[edit | edit source]
Mutations in the GP IX gene can lead to Bernard-Soulier syndrome, a rare disorder characterized by thrombocytopenia, giant platelets, and a bleeding tendency.
See also[edit | edit source]
References[edit | edit source]
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