Toxicological Sciences, Vol 50, 30-35, Copyright © 1999 by Society of Toxicology
AJ Draper and BD Hammock
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 recombinant rat sEH were incubated with
trans-diphenylpropene oxide (tDPPO), a selective substrate for sEH. The
tDPPO hydration activity we observed in inflammatory cell cytosol was lower
than that from liver. The Km for tDPPO hydration observed in rat
inflammatory cell cytosol was the same as the Km for rat liver cytosol (10
microM). Recombinant rat sEH and cytosol from rat liver or inflammatory
cells were incubated with the sEH inhibitors, chalcone oxide,
4-fluorochalcone oxide, and 4-phenylchalcone oxide. The IC50 values were
40, 8, and 0.4 microM, respectively, in all samples. Furthermore, sEH
activity could be completely immunoprecipitated out of the samples, and the
amount of antibody required to do so was apparently identical, regardless
of the source of enzyme. SDS- polyacrylamide gel electrophoresis followed
by Western blot analysis revealed a single sEH band with a molecular weight
of 62 kDa. Isoelectric focusing followed by Western blot analysis revealed
multiple bands containing tDPPO-hydrating activity. Although the
inflammatory cell bands had the same pattern as those from liver cytosol,
the recombinant sEH showed a different banding pattern. These multiple
bands were not an artifact of the IEF gel selected. Furthermore, in a
2-dimensional IEF gel, the bands re-migrated to the same position. The
presence of sEH in inflammatory cells suggests that this enzyme may have an
important endogenous function.
ARTICLES
Soluble epoxide hydrolase in rat inflammatory cells is indistinguishable from soluble epoxide hydrolase in rat liver
Department of Entomology, University of California, Davis 95616, USA.
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