Search results for "Epoxide hydrolase activity"

Cytosolic epoxide hydrolase in humans: development and tissue distribution.

1988

Cytosolic epoxide hydrolase activity was measured towards trans-stilbene oxide in 41 human adult livers, in 40 fetal livers, in 17 placentas and in fetal and adult lungs, kidneys and gut. The cytosolic epoxide hydrolase activity was measurable in all specimens investigated. The rate of formation of trans-stilbene glycol (pmol/min per mg protein, mean +/- SD) was 55.2 +/- 89.6 (fetal liver). 303.2 +/- 73.2 (adult liver) and 18.8 +/- 13.1 (placenta) In the fetal extrahepatic tissues, the cytosolic epoxide hydrolase activity was 70.0 +/- 9.4 (adrenals), 47.6 +/- 7.2 (gut), 69.4 +/- 22.5 (kidneys) and 43.2 +/- 19.2 (lungs) pmol/min per mg protein, whereas in the adult tissues it was 131.2 +/- 6…

Characterization of an epithelial, nearly diploid liver cell strain, from Chinese hamster, able to activate promutagens

1987

Epithelial liver cells of the Chinese hamster (CHEL cells) were propagated in culture for 35 passages. At favourable cell densities, the population doubling time in normal medium, was 20 h. L-Tyrosine amino transferase activity was retained at a measurable level, but its enhancement by dexamethasone was detected solely in cells of early passages. Pyruvate kinase was strongly activated by fructose-1,6-biphosphate at low substrate concentrations. These enzymatic properties suggest that the CHEL cells are derived from a sub-population of parenchymal hepatocytes or from cells closely related to parenchymal hepatocytes. With a lag period of a few hours, CHEL cultures metabolized benzo[a]pyrene. …

Effects of the modulation of epoxide hydrolase activity on the binding of benzo[a]pyrene metabolites to DNA in the intact nuclei.

1983

‘Threshold effect’ of increasing tocopherol ingestion upon the microsomal epoxide hydrolase activity of rat liver

1990

Evidence for Several Hepatic Proteins Related to Microsomal Epoxide Hydrolase

1989

Epoxide hydrolases catalyze the conversion of epoxides, some of which have been shown to be carcinogenic, to dihydrodiols (Guenthner and Oesch 1981). At least three forms of epoxide hydrolases exist in rats, two of which, namely mEHb and mEHch, are associated mainly with the microsomal fraction (Oesch et al 1984; Levin et al 1983) whereas one form namely cEH is found to a large extent in the cytosolic fraction (Gill and Hammock 1981). These three forms differ in their immunological and catalytic properties quite considerably (Guenthner et al 1981). In the case of mEHb the existence of several closely related isoenzymes with an identical apparent subunit molecular weight (Mrs) of 50,000 was …

Modulation of Epdxide Hydrolase Activity; Effect on the Activation of Benzo Cal Pyrene and Its Covalent Binding to Dna in the Nucleus

1982

Benzo[a]pyrene (BP), a model polycyclic aromatic hydrocarbon mutagen and carcinogen, requires bioactivation for the expression of its carcinogenic and mutagenic properties. This process occurs in multiple steps, the initial step being a conversion of BP to epoxide(s) by membrane-bound monooxygenases. The subsequent disposition of these electrophilic species can be directed towards toxic or nontoxic endpoints, depending upon the relative preponderance of several enzymatic and nonenzymatic processes within the cell. Epoxides formed from BP can rearrange to form phenols, be conjugated to glutathione, be converted by epoxide hydrolase to dihydrodiols or bind to cellular macromolecules (Jerina a…

Asp333, Asp495, and His52.3 Form the Catalytic Triad of Rat Soluble Epoxide Hydrolase

1996

On the basis of the sequence similarity between mammalian epoxide hydrolases and bacterial haloalkane dehalogenase reported earlier (Arand, M., Grant, D. F., Beetham, J. K., Friedberg, T., Oesch, F., and Hammock, B. D. (1994) FEBS Lett. 338, 251-256; Beetham, J. K., Grant, D., Arand, M., Garbarino, J., Kiyosue, T., Pinot, F., Oesch, F., Belknap, W. R., Shinozaki, K., and hammock, B. D. (1995) DNA Cell. Biol. 14, 61-71) we selected candidate amino acid residues for the putative catalytic triad of the rat soluble epoxide hydrolase. The predicted amino acid residues were exchanged by site-directed mutagenesis of the epoxide hydrolase cDNA, followed by the expression of the respective mutant en…

Peroxisomes and Hepatotoxicity

1995

Peroxisomes are ubiquitous organelles of eukaryotic cells and are present in significant amounts in hepatic liver cells. Peroxisomal enzymes contribute to several metabolic pathways including fatty acid, purine and amino acid catabolism or bile acid synthesis. The peroxisomal oxidative reactions produce hydrogen peroxide, mostly degraded by catalase which prevents oxidative stress. Moreover, peroxisomes are involved in arylderivative drug detoxification through its epoxide hydrolase activity.

Epoxide Hydrolases: Structure, Function, Mechanism, and Assay

2005

Epoxide hydrolases are a class of enzymes important in the detoxification of genotoxic compounds, as well as in the control of physiological signaling molecules. This chapter gives an overview on the function, structure, and enzymatic mechanism of structurally characterized epoxide hydrolases and describes selected assays for the quantification of epoxide hydrolase activity.

Endogenous Role of Microsomal Epoxide Hydrolase

2005

The specific activities of microsomal epoxide hydrolase with 16α,17α-epoxyandrosten-3-one (androstene oxide) as substrate were measured in various metabolically important and in various steroidogenic organs of the male and female rat and compared with the activities of 16α,17α-epoxyestratrienol (estroxide) and benzo[a]pyrene 4,5-oxide. Androstene oxide was an exceptionally good substrate. The specific activities differed widely between organs but the ratio of the activities towards these substrates was constant in all organs investigated. The ratios compared to benzo[a]pyrene 4,5-oxide were 2.5 for estroxide, and 8.6 for androstene oxide. The ontogenetic development of specific epoxide hydr…