Identification of two epoxide hydrolases in Caenorhabditis elegans that metabolize mammalian lipid signaling molecules

Todd R. Harris, Pavel A. Aronov, Paul D. Jones, Hiromasa Tanaka, Michael Arand, Bruce D. Hammock

Research output: Contribution to journalArticle

20 Scopus citations

Abstract

We have identified two genes in the genomic database for Caenorhabditis elegans that code for proteins with significant sequence similarity to the mammalian soluble epoxide hydrolase (sEH). The respective transcripts were cloned from a mixed stage cDNA library from C. elegans. The corresponding proteins obtained after recombinant expression in insect cells hydrolyzed standard epoxide hydrolase substrates, including epoxyeicosatrienoic acids (EETs) and leukotoxins (EpOMEs). The enzyme activity was inhibited by urea-based compounds originally designed to inhibit the mammalian sEH. In vivo inhibition of the enzymes using the most potent of these compounds resulted in elevated levels of the EpOMEs in the nematode. These results suggest that the hydrolases are involved in the metabolism of possible lipid signaling molecules in C. elegans.

Original languageEnglish (US)
Pages (from-to)139-149
Number of pages11
JournalArchives of Biochemistry and Biophysics
Volume472
Issue number2
DOIs
StatePublished - Apr 15 2008

Keywords

  • 12,13-Epoxy-9-octadecenoate
  • 9,10-Epoxy-12-octadecenoate
  • Epoxyeicosatrienoic acid
  • Leukotoxin
  • Lipid signaling
  • Soluble epoxide hydrolase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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