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Inhibition of collagen-induced platelet reactivity by DGEA peptide

Inhibition of collagen-induced platelet reactivity by DGEA peptide,Boguslawa Luzak,Jacek Golanski,Marcin Rozalski,Magdalena A. Boncler,Cezary Watala

Inhibition of collagen-induced platelet reactivity by DGEA peptide   (Citations: 8)
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Direct interactions between collagen, the most thrombogenic component of the extracellular matrix, and platelet surface membrane receptors mediate platelet adhe- sion and induce platelet activation and aggregation. In this process two glyco- proteins are crucial: integrin 21, an adhesive receptor, and GPVI, which is espe- cially responsible for signal transduction. Specific antagonists of the collagen recep- tors are useful tools for investigating the complexity of platelet-collagen interactions. In this work we assessed the usefulness of DGEA peptide (Asp-Gly-Glu-Ala), the shortest collagen type I-derived motif recognised by the collagen-binding integrin 21, as a potential antagonist of collagen receptors. We examined platelet function using several methods including platelet adhesion under static conditions, platelet function analyser PFA-100™, whole blood electric impedance aggregometry (WBEA) and flow cytometry. We found that DGEA significantly inhibited adhesion, aggrega- tion and release reaction of collagen activated blood platelets. The inhibitory effect of DGEA on static platelet adhesion reached sub-maximal values at millimolar inhibi- tor concentrations, whereas the specific blocker of 21 — monoclonal antibodies Gi9, when used at saturating concentrations, had only a moderate inhibitory effect on platelet adhesion. Considering that 25-30% of total collagen binding to 21 is specific, we conclude that DGEA is a strong antagonist interfering with a variety of collagen-platelet inter- actions, and it can be recognised not only by the primary platelet adhesion receptor 21 but also by other collagen receptors.
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