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:3.1.3.9 (glucose-6-phosphatase)
3,081 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ethanol precipitate fraction (RG-WP) obtained from the hot water extract from rhizome of Rehmannia glutinosa Libosch. f. hueichingensis Hsiao is mainly composed of pectin-like polysaccharide, and exhibited hypoglycemic activity in normal and streptozotocin-induced mice by intraperitoneal administration of the fraction. The results obtained after chemical modification and proteinase treatments of RG-WP suggest that the activity exists in the polysaccharide moiety. Furthermore, the effect of RG-WP on the activities of enzymes responsible for the glucose metabolism in the liver of normal mouse was studied to elucidate the mechanism of the hypoglycemic activity. Administration of RG-WP to normal mice significantly increased the activities of hepatic glucokinase and glucose-6-phosphatase dehydrogenase, but decreased those of hepatic glucose-6-phosphatase and phosphofructokinase. RG-WP stimulated the secretion of insulin and reduced the glycogen content in the liver of normal mouse.
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PMID:[Hypoglycemic activity of polysaccharide fraction from rhizome of Rehmannia glutinosa Libosch. f. hueichingensis Hsiao and the effect on carbohydrate metabolism in normal mouse liver]. 143 91

Male Wistar rats weighing 200 +/- 10 g were intoxicated with ethanol 50% (1 ml/100 g b.w./, day, for 12 days) and concomitantly treated with hydroethanol extract of Chrysanthemum balsamita. An increase of liver glucose-6-phosphatase and phosphorylase a activities correlated with a liver glycogen breakdown as well as a decrease of glycemia were obtained in rats given ethanol 50%. It was found that Chrysanthemum balsamita extract counteracted ethanol effects and maintained at normal limit the metabolite parameters.
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PMID:Hepatoprotector effect of Chrysanthemum balsamita extract in ethanol intoxicated rats. 181 66

The activities of acid phosphatase, alkaline phosphatase, glucose-6-phosphatase, uridine diphosphatase, inosine diphosphatase, thiamine pyrophosphatase and 5'-nucleotidase have been investigated cytochemically in hepatocytes of the offspring of alcohol-fed rats, using cerium ions as a capturing agent and qualitative and quantitative electron microscopy. All these enzyme activities were decreased in the experimental animals compared with controls not exposed to ethanol. The pattern of deposition of the product of glucose-6-phosphatase activity in the cisternae of the endoplasmic reticulum was also different in the two groups. The phosphatases analyzed are functional markers of different cell components, and the results suggest that prenatal exposure of rats to ethanol causes functional alterations in the endoplasmic reticulum, Golgi apparatus, lysosomes and plasma membrane of hepatocytes.
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PMID:Alterations in the cytochemical activity of several phosphatases in hepatocytes from rats exposed prenatally to ethanol. 286 48

Interrelationships between the catalytic properties of glucose-6-phosphatase and the membrane structure of rat liver microsomes were investigated. Membrane modification and solubilization employing the nonionic surfactant Triton X-114 were standardized and analysed by ultracentrifugation, surface tension- and turbidity measurements. The effect of Triton X-114 on the glucose-6-phosphatase activity was studied systematically and the whole magnitude of time- and temperature-dependent inactivation of this enzyme has been demonstrated. The results show that the activity measured is always a resultant of two processes, the beginning of inactivation and the release of latency. Maximal activation of about 600% (83% of apparent latency) was obtained at 0 degree C. A correlation between membrane modification and solubilization and the conditions under preincubation and test incubation reveals that studies on detergent-disrupted microsomes are performed on structures reassembled from solubilizates and this implies a modified microenvironment in the reconstitutes. Kinetic analyses suggest interrelationships between Triton X-114 and the permeability barrier of the glucose-6-phosphatase system. At 0 degree C 2-propanol and ethanol are more potent tools for membrane modification than Triton X-114 and release 88% and 86% latent activity corresponding to an activation of the glucose-6-phosphatase of about 850% and 700%, respectively. These observations suggest that detergent treatment of microsomes could not preserve the functional integrity of the glucose-6-phosphate phosphohydrolase, which is one dogma of the substrate-transport hypothesis developed by Arion and his co-workers (Arion, W.J., et al. (1975) Mol. Cell. Biochem. 6, 75-83).
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PMID:Latency studies on rat liver microsomal glucose-6-phosphatase. Correlation of membrane modification and solubilization by Triton X-114 with the enzymatic activity. 298 63

Patients with deficient activity of hepatic glucose-6-phosphatase (glycogen storage disease type I [GSD-I]) have fasting-induced hypoglycemia, lactic acidemia, hyperuricemia, hyperlipidemia, and a markedly increased capacity for ethanol elimination. The mechanism(s) responsible for the rapid ethanol elimination is not known but has been thought to be directly related to the enzyme defect. We postulated however, that the increased elimination of ethanol was an adaptive phenomenon that would revert toward normal with correction of other blood abnormalities by long-term maintenance of normal blood glucose concentration. Six patients were observed before treatment (group A), and four of the six were observed again 3 to 6 months after dietary treatment had normalized all blood abnormalities (group B). Patients received 16 ml/m2 absolute ethanol as a 5% solution in 0.9% sodium chloride over a 20-minute period. The rate of ethanol elimination was significantly greater (P less than 0.03) in group A than in group B (55.1 +/- 11.1 vs. 37.5 +/- 8.6 mg/dl/hr). Changes in lactate level after ethanol were also significant between the two groups (P less than 0.005). Group A showed a decrease from 9.4 +/- 0.5 to 6.4 +/- 0.4 mEq/L, whereas group B showed an increase in lactate level from 2.7 +/- 0.2 to 4.4 +/- 0.64 mEq/L. Ethanol induced no significant change in blood glucose concentration in group A, whereas there was a significant increase (P less than 0.03) in group B from 93 +/- 6 to 123 +/- 9 mg/dl.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Rapid ethanol elimination in patients with type I glycogen storage disease is an adaptive change resulting from recurrent hypoglycemia. 345 5

Sixteen obese (fa/fa) Zucker rats, sixteen lean (Fa/-) Zucker rats and sixteen Wistar rats, all male rats aged 7-8 weeks, were given either a control (C) diet containing no ethanol or an ethanol (E) diet in which 36% of the energy was supplied by ethanol, for a period of 4 weeks. The activities of glucose-6-phosphate dehydrogenase (EC 1.1.1.49), glucose-6-phosphatase (EC 3.1.3.9) and glycerol kinase (EC 2.7.1.30) and the glycogen content in the livers of obese (fa/fa) rats were lower in animals given diet E than in those given diet C. As a result, hepatic lipogenesis and fatty degeneration of the liver were reduced in obese (fa/fa) rats given diet E.
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PMID:Paradoxical effect of ethanol on liver lipogenesis in the genetically-obese Zucker rat. 406 99

It is shown that the administration of ethanol to male Wistar rats (3 g/kg by gastric tube 3 times a week for 2 months) before or at the beginning of the N-nitrosodiethylamine (NDEA) treatment (2.5 mg/kg 6 times a week in drinking water) reduces the hepatocarcinogenicity of NDEA. This was expressed macroscopically by less important neoplastic changes and biochemically by the higher glucose-6-phosphatase and lower glucose-6-phosphate dehydrogenase activities in the liver.
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PMID:[Effect of ethanol on the hepatocarcinogenic action of N-nitrosodiethylamine in rats]. 406 16

The three Golgi fractions isolated from rat liver homogenates by the procedure given in the companion paper account for 6-7% of the protein of the total microsomal fraction used as starting preparation. The lightest, most homogeneous Golgi fraction (GF(1)) lacks typical "microsomal" activities, e.g., glucose-6-phosphatase, NADPH-cytochrome c-reductase, and cytochrome P-450. The heaviest, most heterogeneous fraction (GF(3)) is contaminated by endoplasmic reticulum membranes to the extent of approximately 15% of its protein. The three fractions taken together account for nearly all the UDP-galactose: N-acetyl-glucosamine galactosyltransferase of the parent microsomal fraction, and for approximately 70% of the activity of the original homogenate. Omission of the ethanol treatment of the animals reduces the recovery by half. The transferase activity is associated with the membranes of the Golgi elements, not with their content. Galactose is transferred not only to N-acetyl-glucosamine but also to an unidentified lipid-soluble component.
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PMID:Golgi fractions prepared from rat liver homogenates. II. Biochemical characterization. 435 72

The effects of 4-weeks ethanol application (20% ethanol, w/w, 2 g X kg-1 on the alcohol oxidizing systems and gluconeogenic enzyme activities of the liver in guinea pigs kept in the cold (+4 degrees C) and at room temperature (+20 degrees C) were studied. The controls were guinea pigs reared at room temperature or in a cold environment without ethanol. The study showed a significant increase (1.5-fold) in liver microsomal cytochrome P-450 after chronic ethanol treatment at room temperature, but not in a cold environment. Microsomal NADPH oxidase activity did not significantly change in any group. Ethanol treatment in a cold environment resulted in a significant increase in liver mitochondrial cytochromes, aa3 and c+c1, and at room temperature in cyt aa3. The activities of total liver homogenate alcohol dehydrogenase or catalase did not change after chronic ethanol treatment. The activity of liver fructose-1.6-diphosphatase showed a significant ethanol induced decrease at room temperature, an effect not observed in the cold environment. Ethanol increased glucose-6-phosphatase activity in the cold, but not at room temperature. In conclusion, the stimulation of liver mitochondrial cytochromes and microsomal cyt P-450 as a consequence of chronic ethanol treatment indicated an increased oxidation capacity for ethanol. The stimulation of glucose-6-phosphatase in a cold environment might be responsible for increasing glucose for heat production after chronic ethanol treatment in cold adapted animals.
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PMID:Liver alcohol oxidizing systems and gluconeogenic enzyme activities after long term ethanol application in cold exposed guinea pigs. 609 47

Effect of chronic ethanol administration on some enzyme activities was studied in plasma membranes, brain homogenate cytoplasmic reticulum and cytosol, liver homogenate and microsomal fractions and blood serum. Ethanol was ingested as a constituent of isocaloric "semiliquid" diet. The investigation was carried out to estimate the diagnostic value of certain enzymes in evaluation of alcohol intoxication. In male rats ethanol caused remarkable hyperlipidemia, accumulation of lipids in liver tissue and elevation of gamma-glutamyl transpeptidase activity in blood serum and brain tissue. In liver tissue moderate induction of glucose-6-phosphatase, NADPH-cytochrome c reductase and alkaline phosphatase was observed. The putative mechanism of elevation of organospecific enzyme activities in blood serum during chronic ethanol consumption is discussed.
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PMID:[Effect of chronic administration of ethanol on the enzyme activity of rat serum, liver and brain]. 614 65


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