Soluble epoxide hydrolase: Gene structure, expression and deletion

Todd R. Harris, Bruce D. Hammock

Research output: Contribution to journalArticle

85 Citations (Scopus)

Abstract

Mammalian soluble epoxide hydrolase (sEH) converts epoxides to their corresponding diols through the addition of a water molecule. sEH readily hydrolyzes lipid signaling molecules, including the epoxyeicosatrienoic acids (EETs), epoxidized lipids produced from arachidonic acid by the action of cytochrome p450s. Through its metabolism of the EETs and other lipid mediators, sEH contributes to the regulation of vascular tone, nociception, angiogenesis and the inflammatory response. Because of its central physiological role in disease states such as cardiac hypertrophy, diabetes, hypertension, and pain sEH is being investigated as a therapeutic target. This review begins with a brief introduction to sEH protein structure and function. sEH evolution and gene structure are then discussed before human small nucleotide polymorphisms and mammalian gene expression are described in the context of several disease models. The review ends with an overview of studies that have employed the sEH knockout mouse model.

Original languageEnglish (US)
Pages (from-to)61-74
Number of pages14
JournalGene
Volume526
Issue number2
DOIs
StatePublished - Sep 10 2013

Fingerprint

Epoxide Hydrolases
Gene Deletion
Gene Expression
Lipids
Nociception
Epoxy Compounds
Cardiomegaly
Cytochromes
Arachidonic Acid
Knockout Mice
Blood Vessels
Nucleotides
Hypertension
Pain
Acids
Water

Keywords

  • EPHX2
  • Epoxyeicosatrienoic acid
  • Hypertension
  • Inflammation
  • Lipid signaling

ASJC Scopus subject areas

  • Genetics

Cite this

Soluble epoxide hydrolase : Gene structure, expression and deletion. / Harris, Todd R.; Hammock, Bruce D.

In: Gene, Vol. 526, No. 2, 10.09.2013, p. 61-74.

Research output: Contribution to journalArticle

Harris, Todd R. ; Hammock, Bruce D. / Soluble epoxide hydrolase : Gene structure, expression and deletion. In: Gene. 2013 ; Vol. 526, No. 2. pp. 61-74.
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