The rate of superoxide generation of guinea pig intraperitoneal neutrophils by a chemotactic peptide or 12-O-tetradecanoylphorbol-13-acetate (TPA) was increased by 2-bromo-2-chloro-l,l,l,-trifluoroethane (halothane), an inhalation anesthetic. This increase was inhibited by l-(5-isoquinolinesulfonyl)methylpiperazine dihydrochloride (H-7), a specific inhibitor of Ca 2+-and phospholipid-dependent protein ldnase C (PKC). Halothane was found to significantly activate partially purified PKC. The activation required phosphatidylserine (IS) and Ca 2+. Dioleoylglycerol-or TPA-activated PKC activity was further increased by halothane. The cytoplasmic proteins of guinea pig neutrophils phosphorylated by halothaneactivated PKC were similar to those phosphorylated by PMA-activated PKC. The phosphorylation of a 48 kDa protein, a phosphorylated protein required for NADPH oxidase activation, was also increased by halothane. These data suggest that the increase of superoxide production by halothane is correlated with its activation of PKC.
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