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

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

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

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

• Glycoprotein Ib
• Glycoprotein V
• Bernard-Soulier syndrome

References

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