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Platelet glycoprotein VI: its structure and function.

Masaaki Moroi·Stephanie M Jung
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Abstract

Glycoprotein (GP) VI is a platelet membrane protein with a molecular weight of 62 kDa that was identified as a physiological collagen receptor from studies of patients deficient in this protein. GPVI-deficient platelets lacked specifically collagen-induced aggregation and the ability to form thrombi on a collagen surface under flow conditions, suggesting that GPVI makes an indispensable contribution to collagen-induced platelet activation. On the platelet surface, GPVI is present as a complex with the Fc receptor (FcR) gamma-chain, probably composed of two GPVI molecules and one FcR gamma-chain dimer. GPVI must form such a dimeric complex to exhibit high affinity binding to collagen. The GPVI-induced activation mechanism is initiated by tyrosine phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of the FcR gamma-chain, and then this signal is transduced to many related proteins, mainly by tyrosine phosphorylation. GPVI is widely recognized as a requisite factor for the formation of platelet aggregates on a collagen surface under blood flow. However, individuals with GPVI-deficient or null platelets do not exhibit any strong bleeding tendency. Analyzing this apparent dichotomy should provide us with a more precise understanding of the mechanism of thrombus formation.

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AnimalsCollagenHemorrhageHumansPlatelet ActivationPlatelet Membrane GlycoproteinsSignal TransductionJournal ArticleReview

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BibTeXRIS

Masaaki Moroi, Stephanie M Jung. 2004. Platelet glycoprotein VI: its structure and function.. https://doi.org/10.1016/j.thromres.2004.06.046

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