Zebrafish have an ethanol-inducible hepatic 4-nitrophenol hydroxylase that is not CYP2E1-like
| Autor: | Jordan S. Kozal, Joel N. Meyer, Jessica H. Hartman, Richard T. Di Giulio |
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| Rok vydání: | 2017 |
| Předmět: |
Male
0301 basic medicine Cytochrome Health Toxicology and Mutagenesis ved/biology.organism_classification_rank.species Mitochondrion Toxicology Article Mixed Function Oxygenases Nitrophenols 03 medical and health sciences 0302 clinical medicine Animals Enzyme inducer Model organism Zebrafish Pharmacology Ethanol biology ved/biology Myocardium fungi Brain Cytochrome P-450 CYP2E1 General Medicine Zebrafish Proteins CYP2E1 biology.organism_classification Mitochondria Rats 030104 developmental biology Liver Biochemistry Enzyme Induction Microsomes Liver biology.protein 030217 neurology & neurosurgery Drug metabolism Ex vivo |
| Zdroj: | Environmental Toxicology and Pharmacology. 54:142-145 |
| ISSN: | 1382-6689 |
| DOI: | 10.1016/j.etap.2017.07.004 |
| Popis: | Zebrafish are an attractive model organism for toxicology; however, an important consideration in translating between species is xenobiotic metabolism/bioactivation. CYP2E1 metabolizes small hydrophobic molecules, e.g. ethanol, cigarette smoke, and diesel exhaust components. CYP2E1 is thought to only be conserved in mammals, but recent reports identified homologous zebrafish cytochrome P450s. Herein, ex vivo biochemical measurements show that unlike mammals, zebrafish possess a low-affinity 4-nitrophenol hydroxylase (Km ~0.6 mM) in hepatic microsomes and mitochondria that is inducible only 1.5- to 2-fold by ethanol and is insensitive to 4-methylpyrazole inhibition. In closing, we suggest creating improved models to study CYP2E1 in zebrafish. |
| Databáze: | OpenAIRE |
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