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1 Department of Biopharmaceutical Sciences, University of California San Francisco, San Francisco, CA, USA
2 Department of Internal Medicine, University of California Davis, Davis, CA, USA
3 Department of Entomology and Cancer Research Center, University of California Davis, Davis, CA, USA
4 Department of Anatomic Pathology, University of California San Francisco, San Francisco, CA, USA
5 Department of Internal Medicine, University of California Davis, Davis, CA, USA; Department of Veteran's Affairs Medical Center, Mather, CA, USA
* To whom correspondence should be addressed. E-mail: deanna{at}itsa.ucsf.edu.
Epoxyeicosatrienoic acids are cytochrome P450 metabolites of arachidonic acid with multiple biological functions, including the regulation of vascular tone, renal tubular transport, cellular proliferation and inflammation. Epoxyeicosatrienoic acids are converted by soluble epoxide hydrolase into the corresponding dihydroxyeicosatrienoic acids, and epoxyeicosatrienoic acid hydration is regarded as one mechanism whereby their biological effects are eliminated. Previous animal studies indicate that soluble epoxide hydrolase plays an important role in the regulation of renal eicosanoid levels and systemic blood pressure. To begin to elucidate the mechanism of these effects, we determined the cellular localization of soluble epoxide hydrolase in human kidney by examining biopsies taken from patients with a variety of non-endstage renal diseases, as well as those without known renal disease. Immunohistochemical staining of acetonefixed kidney biopsy samples revealed that soluble epoxide hydrolase was preferentially expressed in the renal vasculature with relatively low levels in the surrounding tubules. Expression of soluble epoxide hydrolase was evident in renal arteries of varying diameter and was localized mostly in the smooth muscle layers of the arterial wall. Western blotting and functional assays confirmed the expression of soluble epoxide hydrolase in human kidney. There were no obvious differences in soluble epoxide hydrolase expression between normal and diseased human kidney tissue in the samples examined. Our results indicate that soluble epoxide hydrolase is present in human kidney, being preferentially expressed in the renal vasculature, and supports an essential role for this enzyme in renal hemodynamic regulation and its potential utility as a target for therapeutic intervention.
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