Modulation of human neutrophil LTA hydrolase activity by phorbol myristate acetate
| Autor: | Nigel P. Hurst, Shaun R. McColl, W. Henry Betts, Leslie G. Cleland |
|---|---|
| Rok vydání: | 1987 |
| Předmět: |
Leukotriene B4
Neutrophils Biophysics Arachidonic Acids Biochemistry Leukotriene-A4 hydrolase chemistry.chemical_compound Hydrolase Hydroxyeicosatetraenoic Acids Humans Drug Interactions Phosphorylation Molecular Biology Protein kinase C 5-Hydroxyeicosatetraenoic acid Calcimycin Epoxide Hydrolases Leukotriene Arachidonic Acid Leukotriene A4 hemic and immune systems Cell Biology respiratory system N-Formylmethionine Leucyl-Phenylalanine chemistry Phorbol Tetradecanoylphorbol Acetate lipids (amino acids peptides and proteins) |
| Zdroj: | Biochemical and biophysical research communications. 147(2) |
| ISSN: | 0006-291X |
| Popis: | The phorbol ester, phorbol 12-myristate 13-acetate enhanced leukotriene B4 production stimulated by formyl-methionyl-leucyl-phenylalanine and arachidonic acid and reduced the production of the all-trans isomers of LTB4 by human neutrophils. Production of 5-hydroxyeicosatetraenoic acid was unaffected. These observations are consistent with a stimulatory effect of phorbol ester on LTA hydrolase, the enzyme which catalyses the conversion of LTA4 to LTB4. We demonstrate that a protein of the same molecular weight as LTA hydrolase is phosphorylated upon stimulation of neutrophils with PMA. These data suggest that the activity of LTA hydrolase may be regulated by protein kinase C-dependent phosphorylation. |
| Databáze: | OpenAIRE |
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