Protein kinase C activity is not involved in N-formylmethionyl-leucyl-phenylalanine-induced phospholipase D activation in human neutrophils, but is essential for concomitant NADPH oxidase activation: studies with a staurosporine analogue with improved selectivity for protein kinase C
ContributorsKessels, G. C.; Krause, Karl-Heinz; Verhoeven, A. J.
Published inBiochemical journal, vol. 292 ( Pt 3), p. 781-785
Publication date1993
Abstract
Keywords
- Alkaloids/ pharmacology
- Bucladesine/pharmacology
- Enzyme Activation
- Humans
- Isoquinolines/ pharmacology
- Kinetics
- N-Formylmethionine Leucyl-Phenylalanine/ pharmacology
- NADH, NADPH Oxidoreductases/ blood
- NADPH Oxidase
- Neutrophils/drug effects/ enzymology
- Phospholipase D/antagonists & inhibitors/ blood
- Protein Kinase C/antagonists & inhibitors/ blood
- Staurosporine
- Sulfonamides
- Superoxides/blood
- Tetradecanoylphorbol Acetate/pharmacology
Affiliation Not a UNIGE publication
Citation (ISO format)
KESSELS, G. C., KRAUSE, Karl-Heinz, VERHOEVEN, A. J. Protein kinase C activity is not involved in N-formylmethionyl-leucyl-phenylalanine-induced phospholipase D activation in human neutrophils, but is essential for concomitant NADPH oxidase activation: studies with a staurosporine analogue with improved selectivity for protein kinase C. In: Biochemical journal, 1993, vol. 292 ( Pt 3), p. 781–785. doi: 10.1042/bj2920781
Main files (1)
Article
Identifiers
- PID : unige:11155
- DOI : 10.1042/bj2920781
- PMID : 8391255
ISSN of the journal0264-6021