Arachidonic acid uptake by human platelets is mediated by CD36

A K DuttaRoy, Margaret Jane Gordon, Fiona Margaret Campbell, Lynn Crosbie

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

The involvement of glycoprotein (GP) IV (CD36) in arachidonic acid uptake by human platelets was investigated using an anti-CD36 monoclonal antibody (MAB). The binding of [C-14]arachidonic acid to MAB-treated platelets was significantly reduced compared with untreated platelets, The MAB also inhibited arachidonic acid-induced platelet aggregation and thromboxane Az synthesis in a dose-dependent manner. Preincubation of gel-filtered platelets with the MAB (10 mg/l) inhibited arachidonic acid-induced platelet aggregation by 50% and collagen-induced platelet aggregation by 7-8% and the lag time was increased by 200%, Although the mechanism of platelet aggregation is not fully understood yet, the inhibition of arachidonic acid-induced platelet aggregation by the MAB could be the result of a reduced uptake of exogeneously added arachidonic acid by the MAB-treated platelets, Our data clearly indicate that arachidonic acid uptake by platelets is mediated, at least in part, by CD36.

Original languageEnglish
Pages (from-to)291-295
Number of pages5
JournalPlatelets
Volume7
Issue number5-6
Publication statusPublished - 1996

Keywords

  • GLYCOPROTEIN-IV CD36
  • BINDING PROTEIN
  • ACTIVATION
  • DEFICIENCY
  • RECEPTOR
  • GPIV
  • IDENTIFICATION
  • THROMBOSPONDIN
  • PURIFICATION
  • TRANSFUSION
  • glycoprotein-IV CD36
  • binding protein
  • activation
  • deficiency
  • receptor
  • identification
  • thrombospondin
  • purification
  • transfusion

Cite this

DuttaRoy, A. K., Gordon, M. J., Campbell, F. M., & Crosbie, L. (1996). Arachidonic acid uptake by human platelets is mediated by CD36. Platelets, 7(5-6), 291-295.