caa a22 4500 467905452 CHVBK 20180406152832.0 cr unu---uuuuu 170328e20060501xx s 000 0 eng 10.1007/s10735-006-9050-9 doi (NATIONALLICENCE)springer-10.1007/s10735-006-9050-9 Distribution of soluble epoxide hydrolase, cytochrome P450 2C8, 2C9 and 2J2 in human malignant neoplasms [Elektronische Daten] [Ahmed Enayetallah, Richard French, David Grant] Summary: Soluble epoxide hydrolase (sEH) is a bifunctional enzyme with a C-terminal epoxide hydrolase activity and an N-terminal phosphatase activity. Arachidonic acid epoxides, previously suggested to be involved in apoptosis, oncogenesis and cell proliferation, are generated by cytochrome P450 epoxygenases and are good substrates of the sEH C-terminal domain. In addition, the N-terminal phosphatase domain hydrolyzes isoprenoid mono- and pyrophosphates, which are involved in cell signaling and apoptosis. Here we provide a comprehensive analysis of the distribution of sEH, CYP2C8, 2C9 and 2J2 in human neoplastic tissues using tissue micro-arrays. The human neoplastic tissue micro-arrays provide a well-controlled side by side analysis of a wide array of neoplastic tissues and their surrounding normal tissue controls. Many of the neoplastic tissues showed altered expression of these enzymes as compared to normal tissues. Altered expression was not limited to the neoplastic tissues but also found in the surrounding non-neoplastic tissues. For example, sEH expression in renal and hepatic malignant neoplasms and surrounding non-neoplastic tissues was found to be significantly decreased, whereas expression was found to be increased in seminoma as compared to normal tissues. Our study warrants further investigation of the role of altered expression of these enzymes in neoplastic tissues. Springer Science+Business Media B.V., 2006 Soluble epoxide hydrolase nationallicence Cytochrome P450 nationallicence Epoxides nationallicence Isoprenoids nationallicence Enayetallah Ahmed Department of Pharmaceutical Sciences, University of Connecticut, 69 North Eagleville Road, 06269, Storrs, CT, USA aut French Richard Department of Pathobiology and Veterinary Science, University of Connecticut, 06269, Storrs, CT, USA aut Grant David Department of Pharmaceutical Sciences, University of Connecticut, 69 North Eagleville Road, 06269, Storrs, CT, USA aut Journal of Molecular Histology Kluwer Academic Publishers 37/3-4(2006-05-01), 133-141 1567-2379 37:3-4<133 2006 37 10735 https://doi.org/10.1007/s10735-006-9050-9 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10735-006-9050-9 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Enayetallah Ahmed Department of Pharmaceutical Sciences, University of Connecticut, 69 North Eagleville Road, 06269, Storrs, CT, USA aut NATIONALLICENCE 700 1- French Richard Department of Pathobiology and Veterinary Science, University of Connecticut, 06269, Storrs, CT, USA aut NATIONALLICENCE 700 1- Grant David Department of Pharmaceutical Sciences, University of Connecticut, 69 North Eagleville Road, 06269, Storrs, CT, USA aut NATIONALLICENCE 773 0- Journal of Molecular Histology Kluwer Academic Publishers 37/3-4(2006-05-01), 133-141 1567-2379 37:3-4<133 2006 37 10735 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer