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)

1. The metabolic response of livers to perfusion with ethanol with and without avenaciolide, has been followed by measuring the perfusate levels of glucose, lactate, pyruvate, beta-hydroxybutyrate, ethanol, amino acids, urea and lipid. 2. Analysis of the perfused livers showed changes in the activities of some of the key enzymes of glycolysis, gluconeogenesis and lipogenesis. Ethanol perfusion decreased the levels of phosphofructokinase, glucokinase and cytosolic isocitrate dehydrogenase, while avenaciolide lowered pyruvate carboxylase and phosphoenolpyruvate carboxykinase as well as glucokinase. Isocitrate dehydrogenase and phosphofructokinase were unchanged, but the ionophore increased the level of fructose-1,6-diphosphatase. Ethanol plus avenaciolide showed the same pattern as ethanol alone, together with the decrease in phosphoenolpyruvate carboxykinase found with avenaciolide. 3. Neither ethanol nor avenaciolide had any effect on kexokinase, pyruvate kinase or acetyl-CoA carboxylase. There were small changes in glucose-6-phosphatase and malic enzyme, and a tendency for citrate lyase levels to decline in avenaciolide perfusions.
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PMID:The actions of avenaciolide and ethanol on glucose metabolism and on related enzyme activities in the isolated perfused rat liver. 94 10

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

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

The binding characteristics of hGH to Golgi and liver plasma membranes isolated from normal adult female rats have been compared to assess the biological differences between the Golgi and plasma membrane receptor. The effect of cations and the time course of binding were qualitatively similar for both Golgi and plasma membranes. The Golgi membranes from normal rats exhibited maximum binding at pH 6-7 compared to 5-6 for other membrane fractions. The highest apparent affinities (approx. 1 x 10(9) M-1) for hGH were observed in the light Golgi membranes from normal rats and the light and intermediate Golgi membranes from ethanol treated rats. The lowest apparent affinities (0.026 -0.1 x 10(9)M-1 if determined by competitive binding curves or 0.07 - 0.32 x 10(9)M-1 by Scatchard plots) for hGH were observed in plasma membranes isolated by either Neville's or Ray's method or a combination of both methods. The hGH receptors were determined to be lactogenic by competitive binding curves. The affinities of Golgi membranes were not affected by alterations in isolation procedures. Ethanol treatment of the rats prior to sacrifice and membrane isolation resulted in linear Scatchard plots for hGH binding to Golgi membranes compared to curved Scatchard plots for the Golgi membranes of normal rats. The marker enzyme activities of glucose-6-phosphatase and adenylate cyclase were lower in Golgi from ethanol treated rats while the galactosyl transferase activity increased in lighter golgi fractions from ethanol treated rats.
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PMID:Comparison of human growth hormone binding to rat liver plasma and Golgi membranes. 627 78

Ethanol-induced birth defects may be metabolic or structural. The aim of this study was to examine the effects of prenatal ethanol exposure on the ontogeny of gluconeogenic enzymes. Female rats were fed either liquid diets containing 35% ethanol-derived calories or control diets with isocaloric substitution of corn oil for ethanol. Control diets were pair-fed or given ad libitum. Animals were acclimated to the liquid diets for 7 weeks prior to breeding and the diets were continued through gestation. On day 21, at 4 hr post-caesarean section, ethanol-exposed pups exhibited reduced activities of phosphoenolpyruvate carboxykinase and glucose-6-phosphatase when compared to pair-fed and ad libitum controls. It is concluded that prenatal ethanol exposure delays or impairs the development of gluconeogenic enzymes.
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PMID:Effects of maternal ethanol consumption on the ontogeny of gluconeogenesis in the perinatal period. 667 58