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Is Required for p47phox Phosphorylation and Translocation in Activated Human Monocytes1
* Department of Cell Biology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH 44195;
Division of Monoclonal Antibodies, Office of Therapeutics, Research, and Review, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892; and
Department of Medicine, University College London, London, United Kingdom
Our laboratory is interested in understanding the regulation of NADPH oxidase activity in human monocyte/macrophages. Protein kinase C (PKC) is reported to be involved in regulating the phosphorylation of NADPH oxidase components in human neutrophils; however, the regulatory roles of specific isoforms of PKC in phosphorylating particular oxidase components have not been determined. In this study calphostin C, an inhibitor for both novel PKC (including PKC 
, -
, -
, and -
) and conventional PKC (including PKC
and -
), inhibited both phosphorylation and translocation of p47phox, an essential component of the monocyte NADPH oxidase. In contrast, GF109203X, a selective inhibitor of classical PKC and PKC, did not affect the phosphorylation or translocation of p47phox, suggesting that PKC, -, or - is required. Furthermore, rottlerin (at doses that inhibit PKC activity) inhibited the phosphorylation and translocation of p47phox. Rottlerin also inhibited O 
-specific antisense oligodeoxyribonucleotides were used. PKC antisense oligodeoxyribonucleotides inhibited the phosphorylation and translocation of p47phox in activated human monocytes. We also show, using the recombinant p47phox-GST fusion protein, that p47phox can serve as a substrate for PKC in vitro. Furthermore, lysate-derived PKC from activated monocytes phosphorylated p47phox in a rottlerin-sensitive manner. Together, these data suggest that PKC plays a pivotal role in stimulating monocyte NADPH oxidase activity through its regulation of the phosphorylation and translocation of p47phox.
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