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Protein kinase C mediates human neutrophil cytotoxicity.

Abstract
Human neutrophils stimulated with phorbol myristate acetate were able to damage human erythroleukemic K562 cells, in the absence of specific antibody, as assessed by a two hour 51Cr release assay. Neutrophils treated with formyl-peptide fMet-Leu-Phe did not display tumoricidal response, but the addition of diacylglycerol kinase inhibitor R59022 together with formyl-peptide induced the cytotoxic capacity against tumor target cells. Phorbol ester is a potent activator of certain functions of neutrophils because of its ability to directly and irreversibly stimulate protein kinase C; formyl-peptide, on the contrary, activates protein kinase C by inducing a rapid and transient production of diacylglycerol, that is quickly metabolized. The addition of an inhibitor of diacylglycerol kinase, R59022, however potentiated the action of formyl-peptide. These results indicate that protein kinase C is involved in the tumoricidal activity of neutrophils against K562 cells, and that maximal activation of the enzyme is required to achieve the cytotoxic response.
AuthorsR Gavioli, S Spisani, A Giuliani, S Traniello
JournalBiochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 148 Issue 3 Pg. 1290-4 (Nov 13 1987) ISSN: 0006-291X [Print] UNITED STATES
PMID2825682 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Pyrimidinones
  • Thiazoles
  • N-Formylmethionine Leucyl-Phenylalanine
  • R 59022
  • Phosphotransferases
  • Diacylglycerol Kinase
  • Protein Kinase C
  • Tetradecanoylphorbol Acetate
Topics
  • Cytotoxicity, Immunologic (drug effects)
  • Diacylglycerol Kinase
  • Humans
  • N-Formylmethionine Leucyl-Phenylalanine (pharmacology)
  • Neutrophils (physiology)
  • Phosphotransferases (antagonists & inhibitors)
  • Protein Kinase C (physiology)
  • Pyrimidinones (pharmacology)
  • Tetradecanoylphorbol Acetate (pharmacology)
  • Thiazoles (pharmacology)

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