Abstract
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 language | English (US) |
---|---|
Pages (from-to) | 278-287 |
Number of pages | 10 |
Journal | Poultry Science |
Volume | 85 |
Issue number | 2 |
State | Published - 2006 |
Keywords
- Epoxyeicosatrienoic acid
- Pulmonary hypertension syndrome
- Soluble epoxide hydrolase
ASJC Scopus subject areas
- Animal Science and Zoology