Journal of Histochemistry and Cytochemistry Priciples for Free Access to Science
  Search:   
    >> Advanced Search

Guidelines | Subscriptions | About | exPRESS - Current - Archive | Business Information | Contact
Originally published as JHC exPRESS on March 3, 2008.
doi:10.1369/jhc.2008.950659
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Data for this article
Right arrow All Versions of this Article:
jhc.2008.950659v1
56/6/551    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Google Scholar
Right arrow Articles by Sura, P.
Right arrow Articles by Grant, D. F.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sura, P.
Right arrow Articles by Grant, D. F.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?
Journal of Histochemistry and Cytochemistry
Volume 56 (6): 551-559, 2008
Copyright ©The Histochemical Society, Inc.

Distribution and Expression of Soluble Epoxide Hydrolase in Human Brain

Priyanka Sura, Radhakrishna Sura, Ahmed E. EnayetAllah and David F. Grant

Department of Pharmaceutical Sciences (PS,AEE,DFG) and Department of Pathobiology and Veterinary Science (RS), University of Connecticut, Storrs, Connecticut

Correspondence to: David F. Grant, School of Pharmacy, 69 North Eagleville Road, Storrs, CT 06269. E-mail: david.grant{at}uconn.edu

Epoxyeicosatrienoic acids (EETs) are cytochrome P450 metabolites of arachidonic acid, which function in the brain to regulate cerebral blood flow and protect against ischemic brain injury. EETs are converted by soluble epoxide hydrolase (sEH) to the corresponding inactive diol metabolites. Previous animal studies have indicated that sEH gene deletion or treatment with sEH inhibitors results in increased levels of EETs and protection against stroke-induced brain damage. To begin elucidating the underlying mechanism for these effects, we sought to determine the distribution, expression, and activity of sEH in human brain samples obtained from patients with no neurological changes/pathologies. Immunohistochemical analyses showed the distribution of sEH mainly in the neuronal cell bodies, oligodendrocytes, and scattered astrocytes. Surprisingly, in the choroid plexus, sEH was found to be highly expressed in ependymal cells. Vascular localization of sEH was evident in several regions, where it was highly expressed in the smooth muscles of the arterioles. Western blot analysis and enzyme assays confirmed the presence of sEH in the normal brain. Our results indicate differential localization of sEH in the human brain, thus suggestive of an essential role for this enzyme in the central nervous system. This manuscript contains online supplemental material at http://www.jhc.org. Please visit this article online to view these materials. (J Histochem Cytochem 56:551–559, 2008)

Key Words: soluble epoxide hydrolase • epoxyeicosatrienoic acids • central nervous system • cerebral blood flow • cytochrome P450 epoxygenase


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?





Guidelines | Subscriptions | About | exPRESS - Current - Archive | Business Information | Contact
The Journal of Histochemistry & Cytochemistry is owned, published, and licensed by The Histochemical Society © 2008