The effect of new potent selective inhibitors of protein kinase C on the neutrophil respiratory burst

Biochem Biophys Res Commun. 1990 Sep 28;171(3):1087-92. doi: 10.1016/0006-291x(90)90795-o.


New potent inhibitors of protein kinase C were found to inhibit protein kinase C isolated from rat brain and human neutrophils, with a large degree of selectivity over cAMP-dependent kinase and Ca2+/calmodulin-dependent kinase. These novel compounds were potent inhibitors of the fluoride, diC8- and formyl-methionyl-leucyl-phenylalanine-mediated respiratory bursts in intact neutrophils. The opsonized zymosan-stimulated burst was only marginally affected by the compounds. These results differ from those obtained in studies with H7 and CI, (which are less potent and less specific protein kinase C inhibitors) and are consistent with the hypothesis that protein kinase C has a role in the transduction mechanism for the neutrophil oxidative burst stimulated with fluoride, formyl-methionyl-leucyl-phenylalanine and diC8.

MeSH terms

  • Alkaloids / pharmacology*
  • Animals
  • Brain / enzymology
  • Carbazoles / pharmacology
  • Cattle
  • Diglycerides / pharmacology
  • Fluorides / pharmacology
  • Humans
  • Indole Alkaloids
  • Kinetics
  • Myocardium / enzymology
  • N-Formylmethionine Leucyl-Phenylalanine / pharmacology
  • Neutrophils / drug effects
  • Neutrophils / metabolism*
  • Oxygen Consumption / drug effects*
  • Protein Kinase C / antagonists & inhibitors*
  • Protein Kinase C / blood
  • Rats
  • Staurosporine
  • Superoxides / blood*
  • Zymosan / pharmacology


  • Alkaloids
  • Carbazoles
  • Diglycerides
  • Indole Alkaloids
  • 1,2-dioctanoylglycerol
  • Superoxides
  • N-Formylmethionine Leucyl-Phenylalanine
  • Zymosan
  • staurosporine aglycone
  • Protein Kinase C
  • Staurosporine
  • Fluorides