Mechanism of Soluble Epoxide Hydrolase

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Soluble Epoxide Hydrolase in Atherosclerosis

Like many eicosanoids, epoxyeicosatrienoic acids (EETs) have multiple biological functions, including reduction of blood pressure, inflammation, and atherosclerosis in multiple species. Hydration of EETs by the soluble epoxide hydrolase (sEH) is the major route of their degradation to the less bioactive diols. Inhibition of the sEH stabilizes EETs, thus, enhancing the beneficial effects of EETs...

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Soluble epoxide hydrolase in rat inflammatory cells is indistinguishable from soluble epoxide hydrolase in rat liver.

Soluble epoxide hydrolase (sEH) is a ubiquitous mammalian enzyme for which liver and kidney are reported to have the highest activity. We have shown that the soluble epoxide hydrolase (sEH) activity present in rat neutrophils and macrophages is kinetically, immunologically, and physically indistinguishable from rat liver cytosolic sEH. Cytosol from rat liver or inflammatory cells and recombinan...

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Measurement of soluble epoxide hydrolase (sEH) activity.

The human soluble epoxide hydrolase (sEH; EC 3.3.3.2) is the product of the EXPH2 gene. The sEH catalyzes the addition of a water molecule to an epoxide, resulting in the corresponding diol. Early work suggested a role of sEH in detoxifying a wide array of xenobiotic epoxides; however, recent findings clearly implicate the sEH in the regulation of blood pressure, pain, and inflammation through ...

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Soluble epoxide hydrolase inhibition modulates vascular remodeling.

The soluble epoxide hydrolase enzyme (SEH) and vascular remodeling are associated with cardiovascular disease. Although inhibition of SEH prevents smooth muscle cell proliferation in vitro, the effects of SEH inhibition on vascular remodeling in vivo and mechanisms of these effects remain unclear. Herein we determined the effects of SEH antagonism in an endothelium intact model of vascular remo...

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Polymorphisms in human soluble epoxide hydrolase.

Human soluble epoxide hydrolase (hsEH) metabolizes a variety of epoxides to the corresponding vicinal diols. Arachidonic and linoleic acid epoxides are thought to be endogenous substrates for hsEH. Enzyme activity in humans shows high interindividual variation (e.g., 500-fold in liver) suggesting the existence of regulatory and/or structural gene polymorphisms. We resequenced each of the 19 exo...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1995

ISSN: 0021-9258

DOI: 10.1074/jbc.270.45.26923