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Updated: Feb 14, 2026

Turbidimetry on Human Washed Platelets: The Effect of the Pannexin1-inhibitor Brilliant Blue FCF on Collagen-induced Aggregation
Published on: April 6, 2017
Immobilized fibrinogen activates human platelets through glycoprotein VI
Pierre H Mangin1, Marie-Blanche Onselaer2, Nicolas Receveur3
1Université de Strasbourg, INSERM, EFS Grand-Est, BPPS UMR-S 1255, FMTS, France pierre.mangin@efs.sante.fr s.p.watson@bham.ac.uk.
Glycoprotein VI (GPVI) binds fibrinogen, a key interaction for platelet activation and aggregation. This finding reveals GPVI as a potential target for developing novel antithrombotic therapies.
Area of Science:
- Hematology
- Immunology
- Biochemistry
Background:
- Glycoprotein VI (GPVI) is a primary platelet receptor for collagen and fibrin.
- GPVI is recognized as a safe and promising target for antithrombotic drug development.
Purpose of the Study:
- To investigate the role of GPVI in platelet activation and adhesion mediated by fibrinogen.
- To explore the potential of GPVI as an antithrombotic target.
Main Methods:
- Studied human platelet adhesion and spreading on fibrinogen.
- Utilized GPVI-deficient patients' platelets and GPVI-transgenic mouse models.
- Employed surface plasmon resonance and cell adhesion assays.
- Investigated platelet aggregation under flow conditions using monoclonal antibody blockade.
Main Results:
- Human platelets lacking GPVI showed abolished spreading on fibrinogen, indicating GPVI mediates fibrinogen-induced platelet activation.
- GPVI-transgenic mouse platelets exhibited enhanced spreading and calcium signaling on fibrinogen.
- Direct binding of fibrinogen to GPVI was confirmed.
- Blockade of GPVI impaired platelet aggregation in flowing blood.
Conclusions:
- Human GPVI directly binds to immobilized fibrinogen.
- This interaction contributes significantly to platelet spreading and aggregation under flow conditions.
- GPVI represents a viable target for antithrombotic strategies.
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