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JHC exPRESS: First Published November 28, 2005. doi:10.1369/jhc.5A6808.2005
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A more recent version of this article appeared on March 1, 2006.
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Cell-specific Subcellular Localization of Soluble Epoxide Hydrolase in Human Tissues

Ahmed E. Enayetallah 1, Richard A. French 1, Michele Barber 1 and David F. Grant 1*

1 Department of Pharmaceutical Sciences (AEE,DFG), Pathobiology and Veterinary Science (RAF), and Biotechnology / Bioservices Center (MB), University of Connecticut, Storrs, Connecticut

* To whom correspondence should be addressed. E-mail: David.grant{at}uconn.edu.

Submitted on August 9, 2005
Accepted on 19 October 2005


  Abstract
Soluble epoxide hydrolase (sEH) is a phase I xenobiotic metabolizing enzyme having both an N-terminal phosphatase activity and a C-terminal epoxide hydrolase activity. Endogenous hydrolase substrates include arachidonic acid epoxides, which have been suggested to be involved in regulating blood pressure and inflammation. The subcellular localization of sEH has been controversial. Earlier studies using mouse and rat liver suggested that sEH may be cytosolic and/or peroxisomal. In this study, we applied immunofluorescence and confocal microscopy using markers for different subcellular compartments to evaluate sEH colocalization in an array of human tissues. Results showed that sEH is both cytosolic and peroxisomal in human hepatocytes and renal proximal tubules, and exclusively cytosolic in other sEH containing tissues such as pancreatic islet cells, intestinal epithelium, anterior pituitary cells, adrenal gland, endometrium, lymphoid follicles, prostate ductal epithelium, alveolar wall and blood vessels. sEH was not found to be exclusively peroxisomal in any of the tissues evaluated. Our data suggests that human sEH subcellular localization is tissue dependant and that sEH may have tissue- or cell-type specific functionality. To our knowledge, this is the first report showing the subcellular localization of sEH in a wide array of human tissues.

Key Words: subcellular localization, soluble epoxide hydrolase, confocal microscopy, peroxisomal targeting


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