When the blood vessel wall is damaged, platelet membrane glycoproteins interact with the extracellular matrix.
In consequence, this complex activates GPIIb / IIIa membrane glycoproteins, allowing them to bind fibrinogen.
In the absence of fibrinogen, the platelets are joined by vWF due to its ability to bind the activated GPIIb / IIIa complex.
The GPIbα subunit bears the binding site for von Willebrand factor (vWF), α-thrombin, leukocyte integrin αMβ2 and P-selectin.
The FCR pathway of GPVI activation involves γ chain (GPVI transmembrane domain associates with γ chain FCR), Src kinase FYN / LYN, and LAT adaptor protein, all participating in phospholipase C activation.
The surface expression of this complex shows high variability, particularly in relation to the polymorphism of GPIa subunit gene.
Different opinions exist on the importance of C - T point mutation at position 807, which is believed to be associated with the risk of myocardial infarction or ischemic stroke.
[3] This complex interacts with fibrinogen and thus plays an important role in platelet aggregation and adhesion to endothelial surfaces.
Thrombin binding to its receptor activates protein kinase C and increases the level of inositol triphosphate.