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J Biol Chem, Vol. 273, Issue 28, 17817-17823, July 10, 1998

Lipid Products of Phosphoinositide 3-Kinase and Phosphatidylinositol 4',5'-Bisphosphate Are Both Required for ADP-dependent Platelet Spreading

Jean-Michel HeraudDagger , Claire Racaud-SultanDagger , Daisy GironcelDagger , Corinne Albigès-Rizo, Thierry Giacominiparallel , Séverine RoquesDagger , Véronique Martel, Monique Breton-DouillonDagger , Bertrand PerretDagger , and Hugues ChapDagger

From the Dagger  Institut Fédératif de Recherche en Immunologie Cellulaire et Moléculaire, INSERM, Unité 326, Hôpital Purpan, F 31059 Toulouse Cedex, the  Laboratoire d'Etudes de la Différenciation et de l Adherenee Cellulaires/Unité Mixte de Recherches CNRS-Université Joseph Fourier 5538, Institut Albert Bonniot, Faculté de Médecine, F38706 La Tronche Cedex, and the parallel  Ecole Nationale Supérieure de l'Aéronautique et de l'Espace, 10 Avenue Edouard-Belin, 31055 Toulouse Cedex, France

We have shown previously that ADP released upon platelet adhesion mediated by alpha IIbbeta 3 integrin triggers accumulation of phosphatidylinositol 3',4'-bisphosphate (PtdIns-3,4-P2) (Gironcel, D., Racaud-Sultan, C., Payrastre, B., Haricot, M., Borchert, G., Kieffer, N., Breton, M., and Chap, H. (1996) FEBS Lett. 389, 253-256). ADP has also been involved in platelet spreading. Therefore, in order to study a possible role of phosphoinositide 3-kinase in platelet morphological changes following adhesion, human platelets were pretreated with specific phosphoinositide 3-kinase inhibitors LY294002 and wortmannin. Under conditions where PtdIns-3,4-P2 synthesis was totally inhibited (25 µM LY294002 or 100 nM wortmannin), platelets adhered to the fibrinogen matrix, extended pseudopodia, but did not spread. Moreover, addition of ADP to the medium did not reverse the inhibitory effects of phosphoinositide 3-kinase inhibitors on platelet spreading. Although synthetic dipalmitoyl PtdIns-3,4-P2 and dipalmitoyl phosphatidylinositol 3',4',5'-trisphosphate restored only partially platelet spreading, phosphatidylinositol 4',5'-bisphosphate (PtdIns-4,5-P2) was able to trigger full spreading of wortmannin-treated adherent platelets. Following 32P labeling of intact platelets, the recovery of [32P]PtdIns-4,5-P2 in anti-talin immunoprecipitates from adherent platelets was found to be decreased upon treatment by wortmannin. These results suggest that the lipid products of phosphoinositide 3-kinase are required but not sufficient for ADP-induced spreading of adherent platelets and that PtdIns-4,5-P2 could be a downstream messenger of this signaling pathway.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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