Abstract
The protein kinase C inhibitor C-I reduced superoxide production by human neutrophils in response to phorbol myristate acetate by > 50%. In contrast to its effects in oxidative metabolism, 100 uM C-I caused minimal inhibition (5–18%) of lysozyme release in response to phorbol myristate acetate. Enzyme release produced by the formylated oligopeptide FMLP was enhanced by 23–54% in neutrophils pretreated with 100 uM C-I. These findings suggest that protein kinase C activation is not required for phorbol myristate acetate induced enzyme release. Enhancement of FMLP stimulated degranulation by C-I suggests that protein kinase C activation may have inhibitory effects on the release of granule enzymes by human neutrophils.
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More From: Biochemical and Biophysical Research Communications
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