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*
Center for Cell Biology and Cancer Research,
Department of Biochemistry,
Center for Cardiovascular Sciences, and
§
Center for Neuropharmacology and Neurosciences, Albany Medical College, Albany, NY 12208; and
¶
Department of Biology, Kobe University, Kobe, Japan
The binding of Ab (IgG)-opsonized particles by Fc
Rs on
macrophages results in phagocytosis of the particles and generation of
a respiratory burst. Both IgG-stimulated phagocytosis and respiratory
burst involve activation of protein kinase C (PKC). However, the
specific PKC isoforms required for these responses have yet to be
identified. We have studied the involvement of PKC isoforms in
IgG-mediated phagocytosis and respiratory burst in the mouse
macrophage-like cell line, RAW 264.7. Like primary
monocyte/macrophages, their IgG-mediated phagocytosis was calcium
independent and diacylglycerol sensitive, consistent with novel PKC
activation. Respiratory burst in these cells was Ca2+
dependent and inhibited by staurosporine and calphostin C as well as by
the classic PKC-selective inhibitors Gö 6976 and CGP 41251,
suggesting that classic PKC is required. In contrast, phagocytosis was
blocked by general PKC inhibitors but not by the classic PKC-specific
drugs. RAW 264.7 cells expressed PKCs 
, ßI, 
, 
, and 
.
Subcellular fractionation demonstrated that PKCs , , and
translocate to membranes during phagocytosis. In
Ca2+-depleted cells, only novel PKCs and increased
in membranes, and the time course of their translocation was consistent
with phagosome formation. Confocal microscopy of cells transfected with
green fluorescent protein-conjugated PKC or confirmed that
these isoforms translocated to the forming phagosome in Ca-replete
cells, but only PKC colocalized with phagosomes in
Ca2+-depleted cells. Taken together, these results suggest
that the classic PKC mediates IgG-stimulated respiratory burst in
macrophages, whereas the novel PKCs and/or are necessary for
phagocytosis.
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