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Centre de Recherche en Rhumatologie-Immunologie, Centre de Recherche du Centre Hospitalier Universitaire de Québec, Pavillon CHUL (C.B., N.T., S.L., S.S.) and Departments of Anatomy-Physiology (S.G.B.) and Medicine (P.H.N.), Université Laval, Québec, Canada
Prostaglandin E2 (PGE2), originally discovered as a pro-inflammatory mediator, also inhibits several chemoattractant-elicited neutrophil functions, including adhesion, secretion of cytotoxic enzymes, production of superoxide anions, and chemotaxis. In this study, we have examined the effects of PGE2 and prostaglandin E (EP) receptor-selective agonists/antagonists on several steps of the formyl-methionyl-leucyl-phenylalanine (fMLP)-induced phospholipase D (PLD) activation pathway in human neutrophils to elucidate the PGE2 inhibitory mechanism. PGE2 and EP2 receptor agonists inhibited the stimulation of the activity of PLD induced by fMLP in a concentration-dependent manner. The fMLP-stimulated translocation to membranes of protein kinase C 
, Rho, and Arf GTPases was diminished in the presence of PGE2 or EP2 agonists. Moreover, PGE2 and EP2 agonists decreased the activation of phosphatidylinositol 3-kinase 
(PI3K) and Tec kinases as well as the tyrosine phosphorylation of proteins stimulated by fMLP. These data provide strong evidence that 1) the inhibitory effects of PGE2 on the fMLP-induced PLD activation pathway were mediated via EP2 receptors and that 2) the suppression of PI3K activity was the crucial step in the EP2-mediated inhibition of the fMLP-induced signaling cascade.
Address correspondence to: Dr. Sylvain G. Bourgoin, Centre de Recherche en Rhumatologie-Immunologie, Room T1-49, 2705 Boul Laurier, Ste Foy, Québec, Canada, G1V 4G2. E-mail: sylvain.bourgoin{at}crchul.ulaval.ca
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