Investigation of the inhibitory effects of chelerythrine chloride on the translocation of the protein kinase C βI, βII, ζ in human neutrophils
| Autor: | Michel Luyckx, Jean-Claude Cazin, Micheline Cazin, Bernard Gressier, Xavier Siomboing, Thierry Dine, Claude Brunet |
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| Rok vydání: | 2001 |
| Předmět: |
Neutrophils
Pharmaceutical Science MAP2K7 chemistry.chemical_compound Alkaloids Superoxides Drug Discovery Humans Enzyme Inhibitors Threonine Protein Kinase C Protein kinase C Respiratory Burst Benzophenanthridines biology Chemistry Kinase Phenanthridines Respiratory burst Enzyme Activation Isoenzymes Protein Transport Chelerythrine Biochemistry Enzyme inhibitor biology.protein Signal transduction Signal Transduction |
| Zdroj: | Il Farmaco. 56:859-865 |
| ISSN: | 0014-827X |
| Popis: | The protein kinase C (PKC) is a serine/threonine kinase, consisting of different isoforms, implicated in numerous processes of signal transduction. To understand this enzyme well, different pharmacological tools were developed. To activate PKC specifically, phorbol esters were previously used but recent research has shown that these compounds are able to stimulate other proteins. Our model is the respiratory burst in the polymorphonuclear neutrophils. A decrease in the inflammatory process was measured using chelerythrine chloride. Action on PKC was proved by a binding study and by showing the absence of translocation of this enzyme from the cytoplasm to the plasmic membrane during stimulation. |
| Databáze: | OpenAIRE |
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