Anti-GPVI antibody [EPR8347]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

GPVI or glycoprotein VI functions mechanically as a collagen receptor on the surface of platelets. With a molecular mass around 62 kDa it is expressed mainly on megakaryocytes and platelets. GPVI plays an important role in platelet adhesion and activation by binding to collagen exposed at sites of vascular injury. This interaction initiates a cascade of platelet activation essential for normal hemostasis.

Biological function summary

The target participates in the formation of platelet activation complexes. GPVI partners with the Fc receptor γ-chain to transmit activation signals upon collagen binding. This process results in platelet shape change granule secretion and aggregation which are all critical steps for clot formation. By interacting with collagen GPVI ensures that platelets can effectively respond to vascular damage particularly in arterial vessels where high shear forces prevail.

Pathways

The glycoprotein VI contributes significantly to the immune and coagulation pathways. It activates the enzyme Syk kinase following collagen binding which further triggers the downstream signaling pathways like the MAPK pathway leading to platelet activation. GPVI works closely with other receptors like integrin α2β1 and the glycoprotein Ib/V/IX complex reinforcing platelet-collagen interactions and stabilizing the platelet plug formation during thrombus growth.

Associated diseases and disorders

Glycoprotein VI shows relevance in cardiovascular diseases and immune thrombocytopenia. Abnormal GPVI function or expression can exacerbate conditions such as myocardial infarction by promoting excessive platelet activation and thrombosis. Conversely reduced GPVI levels relate to bleeding disorders due to impaired platelet function. Studies have also linked GPVI to autoimmune conditions where antibodies may target it similar to responses in immune thrombocytopenia.