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

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

Entomology

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

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:K_m 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

Cite this

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title = "The cloning and characterization of a soluble epoxide hydrolase in chicken",

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.",

keywords = "Epoxyeicosatrienoic acid, Pulmonary hypertension syndrome, Soluble epoxide hydrolase",

author = "Harris, {T. R.} and C. Morisseau and Walzem, {R. L.} and Ma, {S. J.} and Hammock, {B. D.}",

year = "2006",

language = "English (US)",

volume = "85",

pages = "278--287",

journal = "Poultry Science",

issn = "0032-5791",

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TY - JOUR

T1 - The cloning and characterization of a soluble epoxide hydrolase in chicken

AU - Harris, T. R.

AU - Morisseau, C.

AU - Walzem, R. L.

AU - Ma, S. J.

AU - Hammock, B. D.

PY - 2006

Y1 - 2006

N2 - 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.

AB - 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.

KW - Epoxyeicosatrienoic acid

KW - Pulmonary hypertension syndrome

KW - Soluble epoxide hydrolase

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VL - 85

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EP - 287

JO - Poultry Science

JF - Poultry Science

SN - 0032-5791

IS - 2

ER -

The cloning and characterization of a soluble epoxide hydrolase in chicken

Abstract

Keywords

ASJC Scopus subject areas

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