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α IIb β 3 ‐integrin mediated adhesion of human platelets to a fibrinogen matrix triggers phospholipase C activation and phosphatidylinositol 3′,4′‐bisphosphate accumulation
Author(s) -
Gironcel Daisy,
Racaud-Sultan Claire,
Payrastre Bernard,
Horicot Martine,
Borchert Gudrun,
Kieffer Nelly,
Breton Monique,
Chap Hugues
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00595-9
Subject(s) - phosphatidylinositol , integrin , chemistry , platelet , phospholipase c , phosphatidylinositol 4,5 bisphosphate , platelet activation , phosphatidic acid , microbiology and biotechnology , biochemistry , platelet glycoprotein gpiib iiia complex , kinase , signal transduction , receptor , biology , immunology , phospholipid , membrane
This study focused on the variations in phosphoinositide metabolism depending upon α IIb β 3 ‐integrin/fibrinogen interaction without previous activation of platelet agonist receptors. We found that adhesion of resting human platelets to immobilized fibrinogen stimulates phosphatidic acid production and a concomitant decrease in phosphatidylinositol 4′,5′‐bisphosphate. These results, and the absence of a transphosphatidylation reaction, argue in favor of the activation of a phospholipase C. Moreover, we observed the accumulation of phosphatidylinositol 3′,4′‐bisphosphate in adherent platelets as a consequence of the activation of a phosphatidylinositol 3‐kinase. This effect was inhibited by ADP scavengers. Our results demonstrate that in adherent platelets, whereas phosphatidylinositol 3‐kinase activation is controlled by both α IIb β‐integrin engagement and released ADP, phospholipase C stimulation is triggered only by α IIb β‐integrin/fibrinogen interaction.