A role of p44/42 mitogen-activated protein kinases in formyl-peptide receptor-mediated phospholipase D activity and oxidant production Sylvain Paruch * , Jamel El-Benna † , Bahia Djerdjouri * , Stéfano Marullo * and Axel Périanin * ,1 * Département de Biologie Cellulaire de l’Institut Cochin, The Institut National de la Recherche Médicale (INSERM U567), The Centre National de la Recherche Scientifique (UMR 8104), and the Université René Descartes, Paris France; and † INSERM U683, Paris, France 1 Correspondence: Département de Biologie Cellulaire, Institut Cochin, Hôpital Cochin, Pavillon G. Roussy 5 Etage, 27 rue du Faubourg St. Jacques, Paris 75014, France. E-mail: perianin@cochin.inserm.fr <h3>SPECIFIC AIMS</h3> Chemoattractant receptors play a key role in cell trafficking and pathological processes (inflammation, metastasis). Chemoattractant-induced inflammatory cell responses are mediated through the activation of various intracellular signaling effectors. Among these, phosphatidylcholine-specific phospholipase D (PLD) is a major source of second messengers (phosphatidic acid, diglycerides, phosphocholine) that regulates various physiological processes including phagocyte defense activities, as well as neoplastic transformation. The biochemical regulation of PLD activity involves protein phosphorylation. So far, a role of mitogen-activated (MAP) kinases in chemoattractant-mediated PLD phosphorylation and activation remains unknown. In this study, we have used pharmacological, biochemical, and molecular biology
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