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J. Biol. Chem., Vol. 280, Issue 44, 37021-37032, November 4, 2005

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Interleukin-8-induced Priming of Neutrophil Oxidative Burst Requires Sequential Recruitment of NADPH Oxidase Components into Lipid Rafts^*

Cécile Guichard1, Eric Pedruzzi, Cédric Dewas, Michèle Fay, Cécile Pouzet, Marcelle Bens¶, Alain Vandewalle¶, Eric Ogier-Denis, Marie-Anne Gougerot-Pocidalo, and Carole Elbim

From the Unité INSERM 683, ^¶Unité INSERM 478, IFR02, BP 416, Facultédemédecine Xavier BICHAT, BP 416, 75870 Paris Cedex 18, France

The superoxide-producing phagocyte NADPH oxidase consists of a membrane-bound flavocytochrome b₅₅₈, the cytosol factors p47^phox, p67^phox, p40^phox, and the small GTPase Rac2, which translocate to the membrane to assemble the active complex following neutrophil activation. Interleukin-8 (IL-8) does not activate NADPH oxidase, but potentiates the oxidative burst induced by stimuli such as formyl-methionyl-leucyl-phenylalanine (fMLP) via a priming mechanism. The effect of IL-8 on the components of NADPH oxidase during the priming process has never been investigated in human neutrophils. Here we showed that within 3 min, IL-8 treatment enhanced the Btk- and ERK1/2-dependent phosphorylation of p47^phox, as well as the recruitment of flavocytochrome b₅₅₈, p47^phox, and Rac2 into cholesterol-enriched detergent-resistant microdomains (or lipid rafts). Conversely, IL-8 treatment lasting 15 min failed to recruit flavocytochrome b₅₅₈, p47^phox, or Rac2, but did enhance the Btk- and p38 MAPK-dependent phosphorylation and the translocation of p67^phox into detergent-resistant microdomains. Moreover, methyl--cyclodextrin, which disrupts lipid rafts, inhibited IL-8-induced priming in response to fMLP. Our findings indicate that IL-8-induced priming of the oxidative burst in response to fMLP involves a sequential assembly of the NADPH oxidase components in the lipid rafts of neutrophils.

Received for publication, June 17, 2005 , and in revised form, August 12, 2005.

^* This work was supported by the Institut National de la Santé et de la Recherche Médicale (INSERM) and a Ministère de l'enseignement et de la recherche grant (to C. G.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. 1.

¹ To whom correspondence should be addressed. Tel.: 33-1-44-85-62-09; Fax: 33-1-44-85-62-07; E-mail: guichard{at}bichat.inserm.fr.

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