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Departments of
*
Biochemistry and
Medicine, Division of Infectious Diseases, Wake Forest University School of Medicine, Winston-Salem, NC 27157
The responses of human neutrophils (PMN) involve reorganization and
phosphorylation of cytoskeletal components. We investigated the
translocation of protein kinase C (PKC) isoforms to PMN cytoskeletal
(Triton-insoluble) fractions, in conjunction with activation of the
respiratory burst enzyme NADPH oxidase. In resting PMN, PKC-
(29%)
and small amounts of PKC-
(0.6%), but not PKC-ßII, were present
in cytoskeletal fractions. Upon stimulation with the PKC agonist PMA,
the levels of PKC-, PKC-ßII, and PKC- increased in the
cytoskeletal fraction, concomitant with a decrease in the
noncytoskeletal (Triton-soluble) fractions. PKC- maximally
associated with cytoskeletal fractions at 160 nM PMA and then declined,
while PKC- and PKC-ßII plateaued at 300 nM PMA. Translocation of
PKC- was maximal by 2 min and sustained for at least 10 min.
Translocation of PKC- and PKC-ßII was biphasic, plateauing at 2–3
min and then increasing up to 10 min. Under maximal stimulation
conditions, PKC isoforms were entirely cytoskeletal associated.
Translocation of the NADPH oxidase component
p47phox to the cytoskeletal fraction correlated
with translocation of PKC- and PKC-ßII, but not with translocation
of PKC-. Oxidase activity in cytoskeletal fractions paralleled
translocation of PKC-, PKC-ßII, and
p47phox. Stimulation with
1,2-dioctanoylglycerol resulted in little translocation of PKC isoforms
or p47phox, and in minimal oxidase activity. We
conclude that conventional PKC isoforms (PKC- and/or PKC-ßII) may
regulate PMA-stimulated cytoskeletal association and activation of
NADPH oxidase. PKC- may modulate other PMN responses that involve
cytoskeletal components.
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