Evidence that a collagen derived octapeptide inhibits fibrinogen binding to platelets stimulated by collagen and not by ADP |
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| Authors: | D Pintigny C Legrand A Karniguian Y J Legrand J P Caen |
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| Affiliation: | 1. Department of Mechanical Engineering, University of Washington, Seattle, WA, United States;2. Department of Bioengineering, University of Washington, Seattle, WA, United States;3. Bloodworks Northwest Research Institute, Seattle, WA;4. Department of Biostatistics, University of Washington, Seattle, WA, United States;5. School of Computer Science & Engineering, University of Washington, Seattle, WA, United States;6. Division of Hematology, Department of Medicine, University of Washington, Seattle, WA, United States;7. Department of Biomedical Engineering, Michigan Technological University, Houghton, MI, United States;8. Institute for Stem Cell and Regenerative Medicine, University of Washington, Seattle, WA, United States;9. Department of Laboratory Medicine & Pathology, University of Washington, Seattle, WA, United States;10. Resuscitation Engineering Science Unit (RESCU), University of Washington, Seattle, WA, United States |
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| Abstract: | A synthetic octapeptide derived from type III collagen which specifically inhibits the activation and aggregation of platelets by collagen without affecting their adhesion was assayed on the collagen and ADP dependent fibrinogen binding to platelets. With 20 micrograms/ml collagen, the octapeptide (6 mM) inhibited by 68% the fibrinogen binding: this inhibition was correlated (p less than 0.01) to a decrease in the velocity of aggregation, suggesting that the fibrinogen binding might influence this parameter. The octapeptide did not affect the ADP-induced platelet aggregation and fibrinogen binding. This indicates that the octapeptide does not inhibit the binding of fibrinogen to its receptor directly, but interferes with some step(s) preceding the collagen-induced expression of the fibrinogen receptor. |
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