The cloning and characterization of a soluble epoxide hydrolase in chicken

T. R. Harris, C. Morisseau, R. L. Walzem, S. J. Ma, B. D. Hammock

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


The mammalian soluble epoxide hydrolase (sEH) plays a role in the regulation of blood pressure and vascular homeostasis through its hydrolysis of the endothelial-derived messenger molecules, the epoxyeicosatrienoic acids. This study reports the cloning and expression of a sEH homolog from chicken liver. The resulting 63-kDa protein has an isoelectric point of 6.1. The recombinant enzyme displayed epoxide hydrolase activity when assayed with [ 3H]-trans-1,3-diphenylpropene oxide (t-DPPO), as well as trans-9,10-epoxystearate and the cis-8,9-, 11,12-, and 14,15- epoxyeicosatrienoic acids. The chicken enzyme displayed a lower k cat:Km for t-DPPO than the mammalian enzymes. The enzyme was sensitive to urea-based inhibitors developed for mammalian sEH. Such compounds could be used to study the role of chicken sEH in conditions in which endothelial-derived vasodilation is believed to be impaired, such as pulmonary hypertension syndrome.

Original languageEnglish (US)
Pages (from-to)278-287
Number of pages10
JournalPoultry Science
Issue number2
StatePublished - 2006


  • Epoxyeicosatrienoic acid
  • Pulmonary hypertension syndrome
  • Soluble epoxide hydrolase

ASJC Scopus subject areas

  • Animal Science and Zoology


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