Inhibition of collagen-induced platelet reactivity by DGEA peptide

• Autorzy: Luzak B. , Golanski J. , Rozalski M. , Boncler M.A. , Watala C.
• Języki publikacji: EN

Abstrakty

EN

Direct interactions between collagen, the most thrombogenic component of the extracellular matrix, and platelet surface membrane receptors mediate platelet adhe­sion and induce platelet activation and aggregation. In this process two glyco- proteins are crucial: integrin a2β1, an adhesive receptor, and GPVI, which is espe­cially responsible for signal transduction. Specific antagonists of the collagen recep­tors 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 a2β1, 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, aggrega­tion and release reaction of collagen activated blood platelets. The inhibitory effect of DGEA on static platelet adhesion reached sub-maximal values at millimolar inhibi­tor concentrations, whereas the specific blocker of a2β1 — 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 is specific, we conclude that DGEA is a strong antagonist interfering with a variety of collagen-platelet inter­actions, and it can be recognised not only by the primary platelet adhesion receptor but also by other collagen receptors.

Słowa kluczowe

EN

platelet adhesion; collagen receptor; aggregation; platelet reactivity; platelet receptor antagonist; collagen; induce platelet activation

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2003
• Tom: 50
• Numer: 4
• Opis fizyczny: p.1119-1128,fig.,ref.

Twórcy

autor

Luzak B.

• Medical University of Lodz, Zeromskiego 113, 90-549 Lodz, Poland

autor

Golanski J.

autor

Rozalski M.

autor

Boncler M.A.

autor

Watala C.

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