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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 640))

Abstract

Glycoprotein VI (GPVI) is a membrane glycoprotein unique to platelets and has been identified as a physiological receptor for collagen. Damage to a vessel wall exposes the subendothelial component collagen to platelets in the blood flow. Interaction of platelets with collagen via the receptor GPVI results in platelet activation and adhesion-the processes that are essential for thrombus formation. On the platelet surface, GPVI is present as a complex with the homodimeric Fc receptor γ-chain (FcRγ with a possible stoichiometry of two GPVI molecules and one FcRγ dimer). When collagen binds to GPVI, a platelet activation cascade is initiated by tyrosine phosphorylation of the immunoreceptor tyrosine-based activation motif of FcRγ and this phosphorylation induces the formation of a large complex composed from many signal-transducing proteins. In flow adhesion experiments that closely approximate physiological conditions, GPVI is essential for the formation of large platelet aggregates on collagen. However, GPVI-deficient patients or mice do not show any severe bleeding tendency. This suggests that a GPVI inhibitor would be able to inhibit thrombus formation but still not cause a significant bleeding tendency. Such an inhibitor would show promise as an anti-thrombotic agent for clinical use.

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Jung, S.M., Moroi, M. (2008). Platelet Glycoprotein VI. In: Sigalov, A.B. (eds) Multichain Immune Recognition Receptor Signaling. Advances in Experimental Medicine and Biology, vol 640. Springer, New York, NY. https://doi.org/10.1007/978-0-387-09789-3_5

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