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J. Biol. Chem., Vol. 279, Issue 26, 27059-27068, June 25, 2004
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Distinct Ligand-dependent Roles for p38 MAPK in Priming and Activation of the Neutrophil NADPH Oxidase*
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From the
Department of Surgery, Beth Israel Deaconess Medical Center, Boston, Massachusetts 02130 and the Department of Biology and ¶Division of Biological Engineering, Center for Cancer Research, Massachusetts Institute of Technology, E18-580, Cambridge, Massachusetts 02139
In response to certain cytokines and inflammatory mediators, the activity of the neutrophil NADPH oxidase enzyme is primed for enhanced superoxide production when the cells receive a subsequent oxidase-activating stimulus. The relative role of p38 MAPK in the priming and activation processes is incompletely understood. We have developed a 2-step assay that allows the relative contributions of p38 MAPK activity in priming to be distinguished from those involved in oxidase activation. Using this assay, together with in vitro kinase assays and immunochemical studies, we report that p38 MAPK plays a critical role in TNF
priming of the human and porcine NADPH oxidase for superoxide production in response to complement-opsonized zymosan (OpZ), but little, if any, role in neutrophil priming by platelet-activating factor (PAF) for OpZ-dependent responses. The OpZ-mediated activation process per se is independent of p38 MAPK activity, in contrast to oxidase activation by fMLP, where 70% of the response is eliminated by p38 MAPK inhibitors regardless of the priming agent. We further report that incubation of neutrophils with TNF results in the p38 MAPK-dependent phosphorylation of a subpopulation of p47phox and p67phox molecules, whereas PAF priming results in phosphorylation only of p67phox. Despite these phosphorylations, TNF priming does not result in significant association of either of these oxidase subunits with neutrophil membranes, demonstrating that the molecular basis for priming does not appear to involve preassembly of the NADPH oxidase holoenzyme/cytochrome complex prior to oxidase activation.
Received for publication, December 29, 2003 , and in revised form, April 8, 2004.
* This work was supported by National Institutes of Health Grant GM98059 and a Burroughs-Wellcome Career Development Award (to M. B. Y.). 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.
|| To whom correspondence should be addressed. Tel.: 617-452-2103; Fax: 617-452-4978; E-mail: myaffe{at}mit.edu.
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