Journal article

Identification of a Functional Site on CD36 Involved in the Interaction Between Platelets and Collagen.

N Mercier, B Catimel, MP Reck, D Pellecchia, JL McGregor

Platelets | Published : 1995

Abstract

Adhesion of platelets to collagen, exposed on the subendothelium as a result of vessel wall injury, is a vital step in the formation of a haemostatic plug. Glycoprotein CD36, also known as GPIIIb/GPIV, is one of the platelet glycoproteins known to interact with collagen. The aim of this work was to identify structural/functional sites on CD36 interacting with collagen. Eight peptides, corresponding to sites presumed to be hydrophylic, were synthesized by Fmoc (Fluorenylmethoxycarbonyl) chemistry. Peptides were tested for their ability to inhibit platelet aggregation induced by type I collagen. Peptide E5 (WLNETGTIGDEKA; 415-427), but not the other peptides, inhibited aggregation and secretio..

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University of Melbourne Researchers

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