Zebrafish have an ethanol-inducible hepatic 4-nitrophenol hydroxylase that is not CYP2E1-like.

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Hartman, JH; Kozal, JS; Di Giulio, RT; Meyer, JN

Published Date

  • September 2017

Published In

Volume / Issue

  • 54 /

Start / End Page

  • 142 - 145

PubMed ID

  • 28728133

Pubmed Central ID

  • 28728133

Electronic International Standard Serial Number (EISSN)

  • 1872-7077

International Standard Serial Number (ISSN)

  • 1382-6689

Digital Object Identifier (DOI)

  • 10.1016/j.etap.2017.07.004

Language

  • eng