Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.4.1.2 (glutamate dehydrogenase)
 4,380 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Desert sheep experimentally or naturally infected with Fasciola gigantica were used to study the influence of infection on the activities of some drug-metabolizing enzymes found in the liver. The enzymes investigated were aminopyrine N-demethylase, aniline 4-hydroxylase and UDP-glucuronyltransferase. The experimental infection was confirmed histologically by detection of Fasciola eggs in faeces and by measuring the activities of sorbitol dehydrogenase (SD), glutamate dehydrogenase (GD) and aspartate aminotransferase (AST) in plasma during the course of the disease. Liver specimens from naturally infected sheep were obtained from the slaughter house. The activities of aminopyrine N-demethylase and aniline 4-hydroxylase were significantly decreased in sheep either naturally infected or during the acute stage of experimental fascioliasis (killed 5 weeks post-infection). The activity of UDP-glucuronyltransferase was decreased in naturally infected sheep and those killed 9 or 13 weeks post-experimental infection.
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PMID:The effects of fascioliasis on the activities of some drug-metabolizing enzymes in desert sheep liver. 161 99

Periportal (pp) or perivenous (pv) liver parenchymal cells from female adult Uje: WIST rats were isolated after retro- or antegrade digitonin infusion followed by collagenase perfusion in the opposite direction. The morphological results revealed a distinct acinar-related destruction of the pv- or pp-zone by digitonin. The remaining cells of the respective other zone showed a good structural maintenance. After subsequent conventional collagenase perfusion the yield, viability and structural integrity of the isolated hepatocytes were high. The zonal cell separation was indicated by significant differences in the pp marker glucose-6-phosphatase and the pv marker glutamine synthetase found in the isolated pp or pv cell populations. Under our experimental conditions including the use of female rats, the alanine aminotransferase and glutamate dehydrogenase as well as ethylmorphine N-demethylase and ethoxycoumarin O-deethylase activities were evenly distributed in both preparations. Under stimulating conditions the capacity for urea synthesis was similar in both pv and pp cells.
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PMID:Biochemical and morphological studies on perivenous and periportal liver parenchymal cells from female rats isolated by digitonin-collagenase method. 168 Jul 46

The effects of oral administration of different doses of the latex of Calotropis procera on the activities of drug-metabolizing enzymes in the liver, kidneys and duodenal mucosa of Nubian goats were investigated. Lesions and changes in total plasma protein concentration and in the activities of plasma sorbitol dehydrogenase (SD), glutamate dehydrogenase (GD) and aspartate aminotransferase (AST) were studied. The daily oral administration of the latex at dose rates of 0.4 and 0.8 ml per kg for 7 days resulted in a significant inhibition of the activity of aniline 4-hydroxylase. No signfiicant effects on the activities of aminopyrine N-demethylase and UDP-glucuronyltransferase were observed. A single oral dose of 1.2 or 1.6 ml per kg killed goats within 7 h and resulted in increased activities of aminopyrine N-demethylase and aniline 4-hydroxylase. UDP-glucuronyltransferase was found to be insensitive to tissue injury induced by the latex of C. procera. There were no pathological changes in goats given 10 mg per kg of dieldrin alone or in those pretreated with dieldrin and given the latex at a dose rate of 1.2 ml per kg 14 days later. Dieldrin pretreatment resulted in the induction of the activities of drug-metabolizing enzymes in the liver, kidneys and duodenal mucosa and it may have protected goats from the lethal effects of the latex.
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PMID:The activities of drug-metabolizing enzymes in goats treated orally with the latex of Calotropis procera and the influence of dieldrin pretreatment. 206 26

The metabolism of trimethylamine (TMA) and dimethylamine (DMA) in Arthrobacter P1 involved the enzymes TMA monooxygenase and trimethylamine-N-oxide (TMA-NO) demethylase, and DMA monooxygenase, respectively. The methylamine and formaldehyde produced were further metabolized via a primary amine oxidase and the ribulose monophosphate (RuMP) cycle. The amine oxidase showed activity with various aliphatic primary amines and benzylamine. The organism was able to use methylamine, ethylamine and propylamine as carbon- and nitrogen sources for growth. Butylamine and benzylamine only functioned as nitrogen sources. Growth on glucose with ethylamine, propylamine, butylamine and benzylamine resulted in accumulation of the respective aldehydes. In case of ethylamine and propylamine this was due to repression by glucose of the synthesis of the aldehyde dehydrogenase(s) required for their further metabolism. Growth on glucose/methylamine did not result in repression of the RuMP cycle enzyme hexulose-6-phosphate synthase (HPS). High levels of this enzyme were present in the cells and as a result formaldehyde did not accumulate. Ammonia assimilation in Arthrobacter P1 involved NADP-dependent glutamate dehydrogenase (GDH), NAD-dependent alanine dehydrogenase (ADH) and glutamine synthetase (GS) as key enzymes. In batch cultures both GDH and GS displayed highest levels during growth on acetate with methylamine as the nitrogen source. A further increase in the levels of GS, but not GDH, was observed under ammonia-limited growth conditions in continuous cultures with acetate or glucose as carbon sources.
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PMID:Nitrogen metabolism in the facultative methylotroph Arthrobacter P1 grown with various amines or ammonia as nitrogen sources. 258 50

Berenil (4,4-diamidinodiazoaminobenzene-diacetamide acetate) or Suramin [sodium salt of 8-(3-benzamido-4-methylbenzamido)-naphthalene-1,3,5-trisulfonic acid] treatment of rats infected with Trypanosoma b. brucei enhanced hepatic microsomal aniline hydroxylase and p-aminopyrine N-demethylase activities. While Suramin inhibited significantly the activities of cytoplasmic glutamate dehydrogenase and lactate dehydrogenase, Berenil had no effect. The kinetic profiles of these enzymes consistently showed a Km value similar to that of controls. Both cytosolic and microsomal glutathione-S transferase and microsomal epoxide hydratase were unaffected by Suramin. However, a significant increase in cytosolic glutathione-S transferase was observed with Berenil. Microsomal phospholipids were not affected by any of the drugs.
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PMID:Response of the rat's hepatic drug-metabolizing enzyme system to chemotherapy of Trypanosoma b. brucei infections with Berenil and Suramin. 673 75

Acute, oral administration of 7.0 mg/kg calcium carbimide (calcium cyanamide) to rats, 2 h before sacrifice, produced complete inhibition of hepatic, low-Km (less than 1 microM acetaldehyde) mitochondrial and cytosolic aldehyde dehydrogenase enzymes and significantly inhibited high-Km (approximately 1 mM acetaldehyde) mitochondrial, cytosolic, and microsomal aldehyde dehydrogenase isozymes. Calcium carbimide had no effect on several other hepatic enzyme activities including mitochondrial glutamate dehydrogenase and monoamine oxidase, cytosolic alcohol dehydrogenase, microsomal NADPH-cytochrome c reductase, benzo[a]pyrene hydroxylase and aminopyrine N-demethylase activities, and microsomal cytochrome P-450 content. It is concluded that calcium carbimide is a more specific inhibitor of hepatic aldehyde dehydrogenase enzymes than disulfiram.
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PMID:Specificity of hepatic aldehyde dehydrogenase inhibition by calcium carbimide (calcium cyanamide) in the rat. 686 Oct 4

This study was undertaken to evaluate the effects of chronic ethanol consumption on the hepatotoxicity of acetaminophen. Male Sprague-Dawley rats were pair fed a nutritionally adequate liquid diet containing either ethanol or isocaloric carbohydrate for 4-6 wk. Acetaminophen (0.5 g/kg body wt) was given intraperitoneally 12 h after ethanol withdrawal. By 36 h, frank hepatic centrilobular necrosis and a decrease in hepatic aminopyrine N-demethylase activity were observed in the ethanol-fed rats, whereas in controls the changes were minimal. Serum glutamyl oxaloacetic transaminase and glutamate dehydrogenase activities were significantly increased in ethanol-fed rats. Hepatic damage in ethanol fed rats was apparent already at 6 h, as evidenced by elevated serum enzyme activities and ultrastructural changes, particularly of the mitochondria. The depletion of hepatic glutathione content and the covalent binding of acetaminophen metabolite(s) were significantly greater in ethanol-fed rats than in controls. Urinary excretion of mercapturic acid conjugate during the first 12 h was also increased in ethanol-fed rats. In an in vitro study, covalent binding of acetaminophen metabolite(s) to microsomal protein was increased after ethanol feeding for 4-6 wk. Thus, chronic ethanol feeding increases the hepatotoxicity of acetaminophen; enhanced production of reactive metabolite(s) may be responsible.
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PMID:Increased hepatotoxicity of acetaminophen after chronic ethanol consumption in the rat. 719 62

The effect of oral administration of praziquantel at different dose levels on the activities of metabolizing hepatic enzymes (aminopyrine N-demethylase, aniline 4-hydroxylase and UDP-glucuronyltransferase) was studied in healthy locally bred rabbits. The pathological changes resulting from drug's toxicity were assessed histologically, by measurement of total plasma protein concentration and of the activities of the plasma enzymes sorbitol dehydrogenase (SD), glutamate dehydrogenase (GD) and aspartate aminotransferase (AST). No significant changes were obtained after praziquantel administration at dose levels of 40 and 800 mg/kg body weight, whereas 1600 mg/kg and 2000 mg/kg of praziquantel resulted in a significant decrease in the activities of the three drug-metabolizing hepatic enzymes under investigation in the livers of treated rabbits. All rabbits which received praziquantel at the dose rate of 2000 mg/kg died 10-20 hours following praziquantel treatment.
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PMID:The effect of praziquantel on the activities of some drug-metabolizing hepatic enzymes in rabbits. 760 Sep 44