Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.6.99.3 (diaphorase)
5,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The effect of fenitrothion on testicular microsomal system was analyzed and compared to the modifications induced by the drug at the hepatic level. 2. Acute (165 mg/kg, 1 day) and subacute (55 mg/kg, 3 days) administration of fenitrothion caused a significant decrease on testicular cytochrome P-450 content (51 and 50% respectively) but no modification on cytochrome b5 and NADPH cytochrome c reductase. No changes were induced by fenitrothion in testicular microsomal system after chronic treatment (5.5 mg/ml, 30 days). 3. Results obtained in the liver were very similar to those observed in testis even though the percentage of cytochrome P-450 inhibition obtained after acute and subacute drug administration (45 and 43%) was smaller. 4. In addition, changes in testosterone blood concentrations were also analyzed. A significant reduction of hormone plasma levels were detected at 165 and 55 mg/kg doses of fenitrothion (98% in both cases). Fenitrothion was not able to modify the levels of testosterone in the blood after chronic administration.
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PMID:Modification of testicular cytochrome P-450 after fenitrothion administration. 792 97

The chemopreventive role of an Indian medicinal plant Mikania cordata (Compositae), which is consumed as vegetable and advocated in folk-medicine, has been evaluated through its effects on Phase 1 and 2 of the hepatic drug-detoxifying enzyme system in rats. Although oral administration of a methanolic extract of this plant root (50, 100 or 150 mg/kg for 4, 8 or 12 weeks) has been found to have very little or no effect on hepatic microsomal cytochrome P-450 and cytochrome b5 contents as well as NADPH cytochrome c reductase activity, it afforded a marked induction of uridine diphosphoglucuronyl transferase activities of liver microsomes. The extract also significantly increased the activities of microsomal uridine diphosphoglucose dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate): quinine reductase and cytosolic glutathione s-transferases with a concomittant elevation in the contents of reduced glutathione. All these effects were found to be dose-dependent and maintained during 12 weeks of the extract treatment. Results of the study clearly indicate that the intracellular contents of active intermediates of various xenobiotics including chemical carcinogens would be reduced by the specific enhancement of drug-detoxifying enzymes in the liver of rats treated with the plant extract.
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PMID:Anticarcinogenic biological response of Mikania cordata: reflections in hepatic biotransformation systems. 801 37

Rat liver mitochondrial NADH-linked aquacobalamin reductase was characterized to clarify its enzymological properties. Most of the enzyme was solubilized with 10 g/L Triton X-100 from rat liver mitochondrial membranes. The elution behavior of the solubilized enzyme was identical to that of NADH-cytochrome c reductase (b-type cytochromes/cytochrome b5 reductase complex) during DEAE-Sepharose Fast Flow column chromatography. By mixing both purified cytochrome b5-like hemoprotein (outer membrane-cytochrome b) and cytochrome b5 reductase, cob(II)alamin was formed from aquacobalamin and NADH. These results provide evidence that the outer membrane-cytochrome b/cytochrome b5 reductase complex has the activity of the NADH-linked aquacobalamin reductase in rat liver mitochondria. Some properties of the NADH-linked aquacobalamin reductase were studied using the function of rat liver mitochondrial membranes. The specific activity (109.5 +/- 14.3 nmol.min-1.mg protein-1) of the enzyme was shown under physiological conditions (pH 7.1 at 40 degrees C). The optimal pH and temperature for activity were 7.1 and 40 degrees C, respectively. The apparent Km values were 41.9 mumol/L for aquacobalamin in the presence of 0.2 mmol/L NADH and 14.4 mumol/L for NADH in the presence of 0.1 mmol/L aquacobalamin. The enzyme was specific for aquacobalamin, because cyanocobalamin could not be reduced by the enzyme.
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PMID:Cytochrome b5-like hemoprotein/cytochrome b5 reductase complex in rat liver mitochondria has NADH-linked aquacobalamin reductase activity. 802 53

A gene has been constructed coding for a chimeric flavocytochrome b5 protein that comprises the soluble domain of rat hepatic cytochrome b5 as the NH2-terminal portion of the chimera and the flavin-containing domain of spinach assimilatory NADH:nitrate reductase as the C terminus. The chimeric protein has been expressed in Escherichia coli and purified to homogeneity using a combination of ammonium sulfate precipitation, affinity chromatography on 5'-ADP-agarose, anion-exchange chromatography, and fast protein liquid chromatography gel filtration with an estimated molecular mass of 43 kDa from polyacrylamide gel electrophoresis. Visible and fluorescence spectroscopy indicated the purified protein contained both a b-type cytochrome and FAD prosthetic groups. The chimeric hemoflavoprotein immunologically cross-reacted with both anti-rat cytochrome b5 and anti-spinach nitrate reductase polyclonal antibodies, indicating the conservation of antigenic determinants from both native domains. NH2-terminal and internal amino acid sequencing of the native and CNBr-digested protein confirmed the presence of peptides derived from both the heme- and flavin-binding portions of the sequence which were identical to the deduced amino acid sequence. The chimera exhibited both NADH: ferricyanide reductase and NADH:cytochrome c reductase activities with Vmax values of 88 and 37 mumol of NADH consumed per min/nmol of heme (mu = 0.05 and pH 7.0) and Km values of 2.1, 32, and 1.4 microM for NADH, ferricyanide, and cytochrome c, respectively. This work represents the first successful bacterial expression of a mammalian-plant chimeric metalloflavoprotein. The chimera exhibited properties extremely similar to those of the native cytochrome b5 heme and spinach nitrate reductase FAD components.
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PMID:Construction and expression of a flavocytochrome b5 chimera. 817 67

Oral administration (250 mg/kg) of menthofuran, a monoterpene furan, to rats once daily for 3 days caused hepatotoxicity as judged by a significant increase in serum glutamate pyruvate transaminase (SGPT) and decreases in glucose-6-phosphatase and aminopyrine N-demethylase activities. Administration of menthofuran also resulted in a decrease in the levels of liver microsomal cytochrome P-450, whereas cytochrome b5 and NAD(P)H-cytochrome c reductase activities were not affected. These effects of menthofuran were both dose- and time-dependent. Pretreatment of rats with phenobarbital (PB) prior to menthofuran treatment potentiated hepatotoxicity suggesting that a PB-induced cytochrome P-450 catalyzed the formation of reactive metabolite(s) responsible for the hepatotoxicity.
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PMID:Effects of menthofuran, a monoterpene furan on rat liver microsomal enzymes, in vivo. 819 89

Rats were immunized by intraperitoneal injection of ovalbumin emulsified with Freund incomplete adjuvant, and then the effect of an intravenous challenge with ovalbumin on hepatic drug-metabolizing enzyme activities was examined. The cytochrome P-450 content and ethylmorphine N-demethylase, benzphetamine N-demethylase, arylhydrocarbon hydroxylase and 7-ethoxycoumarin O-deethylase activities significantly decreased in rats treated with ovalbumin compared with control groups treated with saline, whereas there was no significant reduction in cytochrome b5, NADPH-cytochrome c reductase and NADH-cytochrome c reductase.
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PMID:Effect of systemic anaphylaxis on the hepatic drug-metabolizing system in rats. 823 Aug 68

Vitamin E, the major lipid chain-breaking antioxidant in erythrocyte membranes, is present in low concentration, suggesting that mechanisms should exist to protect against its loss. Enzymatic pathways for the recycling of vitamin E from its tocopheroxyl radical have been observed previously in inner membranes of mitochondria and microsomes. These pathways use electron transport enzymes and their substrates to regenerate vitamin E. Erythrocyte membranes also contain significant NADH-cytochrome c reductase activity, as well as cytochrome b5, the function of which is not yet known. Using an enzymatic oxidation system composed of lipoxygenase and arachidonic acid, free radicals were produced in human erythrocyte membranes, and their reaction with chromanols was followed by ESR and high performance liquid chromatography (HPLC). Since the endogenous vitamin E content of the membranes is very low, we used a vitamin E homologue lacking the hydrocarbon chain (2,2,5,7,8-pentamethyl-6-hydroxychromane) as a probe molecule for ESR measurements. However, parallel HPLC determinations of lipid hydroperoxides and of endogenous vitamin E confirmed the results obtained by ESR. It was found that protection against the loss of vitamin E can be provided either by NADH-cytochrome b5-dependent enzymatic recycling or by a nonenzymatic pathway involving ascorbate and dihydrolipoic acid.
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PMID:Vitamin E recycling in human erythrocyte membranes. 838 77

Effects of 2,2'-methylenebis (4-ethyl-6-tert-butylphenol) (MBEBP) on hepatic mitochondrial oxidative phosphorylation in vitro, and on hepatic peroxisomal enzymes activities and microsomal mixed-function oxidase activities were studied. 1. A low concentration of MBEBP, less than 50 microM, increased state 4 respiration and decreased state 3 respiration. However, a higher concentration of MBEBP, greater than 100 microM, acted as a respiratory inhibitor. Therefore, MBEBP was found to act as an uncoupler of oxidative phosphorylation in rat liver mitochondria. 2. MBEBP significantly decreased peroxisomal enzymes, cyanide-insensitive palmitoyl-CoA oxidizing activity and catalase activity in the livers of rats fed 0.2, 1.0 or 5.0% MBEBP for 4 weeks. 3. In microsomal enzyme assay, NADPH cytochrome c reductase activity was significantly increased, however, cytochrome P-450, cytochrome b5 levels, aminopyrine N-demethylase and benzo [a] pyrene hydroxylase activities were not significantly increased in the livers of rats fed 1.0 or 5.0% MBEBP for 4 weeks. The weight loss and the decrease of serum triglyceride level observed in the MBEBP-treated rats seemed to be caused by its uncoupling effects, which might also be the cause of the testicular damage induced by MBEBP.
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PMID:Toxicity studies of a synthetic antioxidant, 2,2'-methylenebis (4-ethyl-6-tert-butylphenol) in rats. 2. Uncoupling effect on oxidative phosphorylation of liver mitochondria. 847 50

Effects of acute or subchronic administration of human placental extract (HPE), a worldwide clinically used agent, on hepatic drug metabolizing enzyme activities were evaluated in rats. Hepatic microsomal cytochrome P-450 (Cyt. P450) and cytochrome b5 (Cyt. b5) contents and cytosolic glutathione S-transferase (GST) activities were maximally induced after various periods of time following a single intraperitoneal injection of HPE (4 ml/kg) whereas microsomal UDP-glucuronyltransferase (UDPGT) activities were inhibited significantly. All these altered effects were returned almost to the basal levels after 96 h of treatment. Subchronic treatment (30 days) with HPE (1,2 or 4 ml/kg) afforded a significant induction of Cyt. P-450 and Cyt. b5 levels and that of GST activities with a concurrent suppression of the activities of UDPGT and these results were found to be dose-dependent. However, microsomal NADPH cytochrome c reductase activity was not affected either by acute or subchronic treatment. The observed variations in the levels and activities of above house-keeping enzymes were discussed in relation to the possible carcinogenic risk of long-term treatment with this pharmaceutical agent.
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PMID:Effects of human placental extract on hepatic drug metabolizing enzyme. 854 51

An intraperitoneal administration of PB at a daily dose of 50 mg Kg-1 body wt for 4 days increased the specific content of hepatic microsomal heme, cytochrome P450 and the activity of aminopyrine N-demethylase by 1.8, 2.8 and 3.5 fold respectively. These results were substantiated by the intensification of the 52.5 KDa polypeptide in the electrophoretogram of sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the hepatic microsomes obtained from PB-pretreated versus control macaques. PB did not affect the hepatic content of cytochrome b5 and the activity of NADPH cytochrome c reductase, whereas it decreased the activity of NADH cytochrome c reductase in the rhesus monkeys. To the best of our knowledge this is a first report on the induction of hepatic cytochrome P450 and related enzymes by PB in rhesus monkeys.
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PMID:Induction of hepatic cytochrome P450 by phenobarbitone in rhesus monkey (Macaca mulatta). 882 15


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