The cloning and characterization of a soluble epoxide hydrolase in chicken. Academic Article uri icon


  • 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 kcat: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.

published proceedings

  • Poult Sci

author list (cited authors)

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

citation count

  • 10

complete list of authors

  • Harris, TR||Morisseau, C||Walzem, RL||Ma, SJ||Hammock, BD

publication date

  • February 2006