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December 5, 2017Journal of Thrombosis and HaemostasisOpen Access

GPVI-Fc2 exhibited specific, saturable binding to both D-fragment and D-dimer, which was inhibited by mFab-F and abrogated by collagenous substrates, while GPVI ex did not bind to any fibrinogen substrate.

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Population

Recombinant GPVI monomeric extracellular domain, dimeric Fc-fusion protein, normal platelets, and Glanzmann…

Design

Preclinical

Authors

IIIsuru InduruwaMMMasaaki MoroiABArkadiusz Bonna

Discussion

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Overview

May guide GPVI-targeted antithrombotic development; hypothesis-generating from animal data and should not yet change practice.

Structured PICO

P
Population
Recombinant GPVI monomeric extracellular domain (GPVI ex), dimeric Fc-fusion protein (GPVI-Fc2), normal platelets, and Glanzmann thrombasthenic (GT) platelets
I
Intervention
Exposure to immobilized fibrinogen derivatives (D-fragment, D-dimer, fibrinogen, fibrin) and various inhibitors (mFab-F, Eptifibatide, collagenous substrates)
O
Outcome
Binding of GPVI to fibrinogen substrates and platelet adhesion under static and flow conditionssurrogate

Only dimeric GPVI interacts with the fibrinogen D-domain to support platelet adhesion and activation, providing mechanistic insight into thrombus formation.

Cite This Study

Induruwa et al. (2017) studied this question.

synapsesocial.com/papers/6a7f173dd81da9b9ca9c4e95https://doi.org/10.1111/jth.13919
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Also Consider

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  4. 4Platelet Glycoprotein VI Dimerization, an Active Process Inducing Receptor Competence, Is an Indicator of Platelet Reactivity2011 · 101 citations
  5. 5Structure-function relationship of the platelet glycoprotein VI (GPVI) receptor: does it matter if it is a dimer or monomer?2021 · 21 citations