Salzer W, Gerard C, McCall C
Department of Medicine, Wake Forest University Medical Center, Bowman Gray School of Medicine, Winston-Salem, North Carolina 27103.
Biochem Biophys Res Commun. 1987 Oct 29;148(2):747-54. doi: 10.1016/0006-291x(87)90939-9.
The protein kinase C inhibitor C-I reduced superoxide production by human neutrophils in response to phorbol myristate acetate by greater than 50%. In contrast to its effects in oxidative metabolism, 100 microM 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 microM 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.
