Abstract
We report that the putative protein kinase C inhibitor, K252a, at concentrations of 0.2 and 1 microM, inhibited the respiratory burst induced by fluoride and formyl-methionyl-leucyl-phenyl-alanine respectively, both in human neutrophils primed with a subthreshold dose of phorbol myristate acetate and in non-primed neutrophils. In addition, K252a effectively inhibited ConA-zymosan-mediated superoxide generation in Ca2(+)-depleted neutrophils, with virtually maximal inhibition seen at 1 microM. These results suggest that protein kinase C is involved in the putative phosphatidylinositol bisphosphate-independent signal transduction mechanism of the respiratory burst as well as the pathway dependent on phosphatidylinositol bisphosphate hydrolysis.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Calcium / metabolism
-
Carbazoles / pharmacology*
-
Concanavalin A / metabolism
-
Humans
-
Indole Alkaloids
-
N-Formylmethionine Leucyl-Phenylalanine / pharmacology
-
Neutrophils / drug effects*
-
Neutrophils / enzymology
-
Oxygen Consumption / drug effects
-
Phosphatidylinositol 4,5-Diphosphate
-
Phosphatidylinositols / pharmacology*
-
Protein Kinase C / antagonists & inhibitors
-
Protein Kinase C / metabolism*
-
Superoxides / metabolism*
-
Tetradecanoylphorbol Acetate / pharmacology
-
Zymosan / metabolism
Substances
-
Carbazoles
-
Indole Alkaloids
-
Phosphatidylinositol 4,5-Diphosphate
-
Phosphatidylinositols
-
Concanavalin A
-
Superoxides
-
N-Formylmethionine Leucyl-Phenylalanine
-
Zymosan
-
staurosporine aglycone
-
Protein Kinase C
-
Tetradecanoylphorbol Acetate
-
Calcium