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Originally published In Press as doi:10.1074/jbc.M004703200 on July 12, 2000

J. Biol. Chem., Vol. 275, Issue 37, 28406-28412, September 15, 2000
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Phosphorylation of p22phox Is Mediated by Phospholipase D-dependent and -independent Mechanisms
CORRELATION OF NADPH OXIDASE ACTIVITY AND p22phox PHOSPHORYLATION*

Debra S. RegierDagger §, Dianne G. GreeneDagger , Susan SergeantDagger , Algirdas J. Jesaitis, and Linda C. McPhailDagger ||**

From the Departments of Dagger  Biochemistry and || Medicine, Division of Infectious Diseases, Wake Forest University School of Medicine, Winston-Salem, North Carolina 27157 and the  Department of Microbiology, Montana State University, Bozeman, Montana 59717

Human neutrophils participate in the host innate immune response, partly mediated by the multicomponent superoxide-generating enzyme NADPH oxidase. A correlation between phosphorylation of cytosolic NADPH oxidase components and enzyme activation has been identified but is not well understood. We previously showed that p22phox, the small subunit of the membrane-bound oxidase component flavocytochrome b558, is an in vitro substrate for both a phosphatidic acid-activated kinase and conventional protein kinase C isoforms (Regier, D. S., Waite, K. A., Wallin, R., and McPhail, L. C. (1999) J. Biol. Chem. 274, 36601-36608). Here we show that several neutrophil agonists (phorbol myristate acetate, opsonized zymosan, and N-formyl-methionyl-leucyl-phenylalanine) induce p22phox phosphorylation in intact neutrophils. To determine if phospholipase D (PLD) is needed for p22phox phosphorylation, cells were pretreated with ethanol, which reduces phosphatidic acid production by PLD in stimulated cells. Phorbol myristate acetate-induced phosphorylation of p22phox and NADPH oxidase activity were not reduced by ethanol. In contrast, ethanol reduced both activities when cells were stimulated by N-formyl-methionyl-leucyl-phenylalanine or opsonized zymosan. Varying the time of stimulation with opsonized zymosan showed that the phosphorylation of p22phox coincides with NADPH oxidase activation. GF109203X, an inhibitor of protein kinase C and the phosphatidic acid-activated protein kinase, decreased both p22phox phosphorylation and NADPH oxidase activity in parallel in opsonized zymosan-stimulated cells. Stimulus-induced phosphorylation of p22phox was on Thr residue(s), in agreement with in vitro results. Overall, these data show that NADPH oxidase activity and p22phox phosphorylation are correlated and suggest two mechanisms (PLD-dependent and -independent) by which p22phox phosphorylation occurs.

* This work was supported by National Institutes of Health (NIH) Grant R01-AI22564 (to L. C. M.); March of Dimes Birth Defects Foundation Grants FY97-0443, FY98-0638, and FY99-0561 (to L. C. M.); and NIH Grant RO1-AI26711 (to A. J. J.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported by the Signal Transduction Mechanisms and Cell Function training program, NIH, Grant CA-09422.

** To whom correspondence should be addressed: Dept. of Biochemistry, Wake Forest University School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157. Tel.: 336-716-2621; Fax: 336-716-7671; E-mail: lmcphail@wfubmc.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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