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

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 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.

authors

• Walzem, Rosemary

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

publisher

• Elsevier  Publisher

published in

• Poultry Science  Journal

keywords

• Amino Acid Sequence
• Animals
• Base Sequence
• Chickens
• Cloning, Molecular
• DNA, Complementary
• Endothelium, Vascular
• Epoxide Hydrolases
• Epoxy Compounds
• Liver
• Male
• Molecular Sequence Data
• Recombinant Proteins
• Sequence Alignment
• Solubility
• Substrate Specificity
• Tritium
• Vasodilation

PubMed Central ID

• 16523628

Digital Object Identifier (DOI)

• 10.1093/ps/85.2.278

start page

• 278

end page

• 287

volume

• 85

issue

• 2

URL

• http%3A%2F%2Fdx.doi.org%2F10.1093%2Fps%2F85.2.278