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Phosphorylates a Subset of Selective Sites of the NADPH Oxidase Component p47phox and Participates in Formyl Peptide-Mediated Neutrophil Respiratory Burst
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Institut National de la Santé et de la Recherche Médicale Unité 479, Centre Hospitalier Universitaire Xavier Bichat, Paris, France; and
Centre National de la Recherche Scientifique Unité Propre de la Recherche et des Études Scientifiques A 8068, Institut Cochin de Génétique Moléculaire, Département de Biologie Cellulaire, Hôpital Cochin, Paris, France
Generation of superoxide anion by the multiprotein complex NADPH
phagocyte oxidase is accompanied by extensive phosphorylation of its
47-kDa protein component, p47phox, a major
cytosolic component of this oxidase. Protein kinase C 
(PKC ), an
atypical PKC isoform expressed abundantly in human polymorphonuclear
leukocytes (PMN), translocates to the PMN plasma membrane upon
stimulation by the chemoattractant fMLP. We investigated the role of
PKC in p47phox phosphorylation and in
superoxide anion production by human PMN. In vitro incubation of
recombinant p47phox with recombinant PKC
induced a time- and concentration-dependent phosphorylation of
p47phox with an apparent
Km value of 2 µM. Phosphopeptide mapping
analysis of p47phox showed that PKC
phosphorylated fewer selective sites in comparison to
"conventional" PKCs. Serine 303/304 and serine 315 were identified
as targets of PKC by site-directed mutagenesis. Stimulation of PMN
by fMLP induced a rapid and sustained plasma membrane translocation of
PKC that correlated to that of p47phox. A
cell-permeant-specific peptide antagonist of PKC inhibited both
fMLP-induced phosphorylation of p47phox and its
membrane translocation. The antagonist also inhibited the fMLP-induced
production of oxidant (IC50 of 10 µM), but not that
induced by PMA. The inhibition of PKC expression in HL-60
neutrophil-like cells using antisense oligonucleotides (5 and 10 µM)
inhibited fMLP-promoted oxidant production (27 and 50%, respectively),
but not that induced by PMA. In conclusion,
p47phox is a substrate for PKC and
participates in the signaling cascade between fMLP receptors and NADPH
oxidase activation.
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