Evidence that cytochrome P450 2E1 is involved in the (omega-1)-hydroxylation of lauric acid in rat liver microsomes
| Autor: | T. Goasduff, F. Berthou, L. Lebreton, Y. Amet, J.F. Menez, Jean-Pierre Salaün |
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| Rok vydání: | 1994 |
| Předmět: |
Male
Pyridines Biophysics Pyrazole Hydroxylation Biochemistry Binding Competitive Acetone Rats Sprague-Dawley chemistry.chemical_compound Cytochrome P-450 Enzyme System medicine Animals Molecular Biology Chromatography High Pressure Liquid chemistry.chemical_classification Ethanol biology Lauric Acids Cytochrome P-450 CYP2E1 Oxidoreductases N-Demethylating Cell Biology CYP2E1 Lauric acid Rats Isoenzymes Enzyme chemistry Polyclonal antibodies Chlorzoxazone Enzyme Induction biology.protein Microsomes Liver Pyrazoles medicine.drug Methylcholanthrene |
| Zdroj: | Biochemical and biophysical research communications. 203(2) |
| ISSN: | 0006-291X |
| Popis: | The present study examined changes in hepatic CYP2E1 content and (omega-1)-hydroxylation of lauric acid in rats treated with pyridine, pyrazole, acetone, ethanol and 3-methylcholanthrene. The (omega-1)-hydroxylase activity was strongly correlated with chlorzoxazone 6-hydroxylation (r = 0.76) and 4-nitrophenol-hydroxylase (r = 0.91). Both these activities are carried out by CYP2E1. (omega-1) hydroxylase activity was inhibited by ethanol (Ki = 3.5 mM), dimethylsulfoxide and diethyldithiocarbamate. Furthermore, polyclonal antibody directed against rat CYP2E1 inhibited (omega-1)-hydroxylation by more than 90% while it had no effect on the omega-hydroxylation. These results suggest that the (omega-1)-hydroxylation of lauric acid is mediated principally by the CYP2E1 enzyme in rat liver microsomes. |
| Databáze: | OpenAIRE |
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