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I Protein Kinase C during Fc
R-Mediated Phagocytosis in Microglia1
* Laboratory of Molecular Pharmacology, Biosignal Research Center, Kobe University, Kobe, Japan;
Center for Cell Biology and Cancer Research, Albany Medical College, Albany, NY 12208;
Department of Anatomy and Cell Biology, Kochi Medical School, Kochi, Japan;
Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan;
¶ Graduate School of Biomedical Sciences, Hiroshima University, Hiroshima, Japan;
|| Institute for Comprehensive Medical Science, Fujita Health University, Toyoake, Japan; and
# CREST JST (Japan Science and Technology)
Protein kinase C (PKC) plays a prominent role in immune signaling. To elucidate the signal transduction in a respiratory burst and isoform-specific function of PKC during Fc
R-mediated phagocytosis, we used live, digital fluorescence imaging of mouse microglial cells expressing GFP-tagged molecules. 
I PKC, 
PKC, and diacylglycerol kinase (DGK) dynamically and transiently accumulated around IgG-opsonized beads (BIgG). Moreover, the accumulation of p47phox, an essential cytosolic component of NADPH oxidase and a substrate for I PKC, at the phagosomal cup/phagosome was apparent during BIgG ingestion. Superoxide (O2–) production was profoundly inhibited by Gö6976, a cPKC inhibitor, and dramatically increased by the DGK inhibitor, R59949. Ultrastructural analysis revealed that BIgG induced O2– production at the phagosome but not at the intracellular granules. We conclude that activation/accumulation of I PKC is involved in O2– production, and that O2– production is primarily initiated at the phagosomal cup/phagosome. This study also suggests that DGK plays a prominent role in regulation of O2– production during FcR-mediated phagocytosis.
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