PUBLICATION
Zebrafish have an ethanol-inducible hepatic 4-nitrophenol hydroxylase that is not CYP2E1-like
- Authors
- Hartman, J.H., Kozal, J.S., Di Giulio, R.T., Meyer, J.N.
- ID
- ZDB-PUB-170721-1
- Date
- 2017
- Source
- Environmental Toxicology and Pharmacology 54: 142-145 (Journal)
- Registered Authors
- Di Giulio, Richard T.
- Keywords
- 4-Nitrophenol, CYP2E1, Ethanol, Zebrafish
- MeSH Terms
-
- Animals
- Brain/metabolism
- Cytochrome P-450 CYP2E1
- Enzyme Induction
- Ethanol/pharmacology*
- Liver/metabolism*
- Male
- Microsomes, Liver/metabolism
- Mitochondria/metabolism
- Mixed Function Oxygenases/biosynthesis
- Mixed Function Oxygenases/metabolism*
- Myocardium/metabolism
- Nitrophenols/metabolism*
- Rats
- Zebrafish
- Zebrafish Proteins/biosynthesis
- Zebrafish Proteins/metabolism*
- PubMed
- 28728133 Full text @ Environ. Toxicol. Pharmacol.
Citation
Hartman, J.H., Kozal, J.S., Di Giulio, R.T., Meyer, J.N. (2017) Zebrafish have an ethanol-inducible hepatic 4-nitrophenol hydroxylase that is not CYP2E1-like. Environmental Toxicology and Pharmacology. 54:142-145.
Abstract
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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping