Nuclear Epoxide Hydrolase in the Human Fetal and Adult Liver

Pacifici, Gian Maria; Colizzi, Cesare; Giuliani, L.; Rane, Anders

doi:10.1159/000137980

Cited by 12 publications

(1 citation statement)

References 17 publications

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“…The intestine homogenates were filtered on gauze to remove cell debris. The procedure for the isolation of nuclear and microsomal fractions has been described in detail pre viously [Pacifici et al, 1984b]. Each nuclear prepara tion was examined by phase-contrast microscopy (Leitz, Wetzlar.…”

Section: Preparation O F Subcellular Fractionsmentioning

confidence: 99%

Glucuronidation of 1-Naphthol in Nuclear and Microsomal Fractions of the Human Intestine

1986

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The glucuronyl transferase activity was measured with 1 -naphthol as a substrate in nuclear and microsomal fractions of the human intestinal mucosa. The mucosa was obtained from different parts of the intestine. The rate of 1-naphthol glucuronidation ranged between 0.70 and 1.26 nmol/mg/min (nuclear fraction) and 0.21 and 0.54 nmol/mg/min (microsomal fraction). The average (± SEM) of the nuclear/microsomal ratios of the glucuronyl transferase was 2.48 ± 0.19. The epoxide hydrolase activity towards styrene oxide was measured in the same subcellular fractions; it was undetectable in the nuclear fraction, whereas it was 0.46 ± 0.04 nmol/mg/min (mean ± SEM) in the microsomal fraction. The glucuronyl transferase activity was also measured in nuclear and microsomal fractions of the human liver. The activity (mean ± SEM) was 1.14 ± 0.21 nmol/mg/min (nuclei) and 5.00 ± 0.80 (microsomes). The average of the nuclear to microsomal ratios (mean ± SEM) was 0.32 ± 0.03.

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Section: Preparation O F Subcellular Fractionsmentioning

confidence: 99%

Glucuronidation of 1-Naphthol in Nuclear and Microsomal Fractions of the Human Intestine

1986

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The expression of cytochrome P-450, epoxide hydrolase, and glutathione s-transferase in hepatocellular carcinoma

Murray

Paterson

Weaver

et al. 1993

Cancer

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Background. Cytochrome P‐450, epoxide hydrolase, and glutathione S‐transferase (GST) all play a key role in the metabolism of chemical carcinogens, mutagens, and various anti‐cancer drugs. All these functionally associated enzymes might be involved in both the development of hepatocellular carcinoma and in determining the anti‐cancer drug sensitivity of such tumors. Methods. The expression of two forms of cytochrome P‐450 (P‐450 IA and P‐450 IIIA), microsomal epoxide hydrolase, and three classes of cytosolic GST (alpha, mu, and pi) have been studied immunohistochemically in human hepatocellular carcinoma. Results. The hepatocellular carcinomas were characterized by a consistently high expression of epoxide hydrolase and variable expression of the cytochromes P‐450 and GST. Cytochrome P‐450 IA and IIIA stained in 64.5% and 41.9% of the 31 hepatocellular carcinomas studied, respectively. Epoxide hydrolase was present in all tumors, and GST types alpha, pi, and mu were identified in 48.4%, 38.7%, and 74.2% of the hepatocellular carcinomas, respectively. Conclusions. This study showed that the expression of xenobiotic‐metabolizing enzymes in hepatocellular carcinoma is complex and the presence of different xenobiotic enzymes in hepatocellular carcinoma may contribute to the intrinsic drug resistance of these tumors. Cancer 1993; 71:36‐43.

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Nuclear UDP-Glucuronosyltransferases: Identification of UGT2B7 and UGT1A6 in Human Liver Nuclear Membranes

Radominska‐Pandya

Pokrovskaya

et al. 2002

Archives of Biochemistry and Biophysics

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Nuclear Epoxide Hydrolase in the Human Fetal and Adult Liver

Cited by 12 publications

References 17 publications

Glucuronidation of 1-Naphthol in Nuclear and Microsomal Fractions of the Human Intestine

Glucuronidation of 1-Naphthol in Nuclear and Microsomal Fractions of the Human Intestine

The expression of cytochrome P-450, epoxide hydrolase, and glutathione s-transferase in hepatocellular carcinoma

Nuclear UDP-Glucuronosyltransferases: Identification of UGT2B7 and UGT1A6 in Human Liver Nuclear Membranes

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