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)

Subcellular organellles from livers of rats three days prenatal to 50 weeks postnatal were separated on sucrose gradients. The peroxisomes had a constant density of 1.243 g/ml throughout the life of the animal. The density of the mitochondria changed from about 1.236 g/ml at birth to a constant value of 1.200 g/ml after two weeks. The peroxisomal and mitochondrial fatty acid beta-oxidation and the peroxisomal and supernatant activities of catalase and glycerol-3-phosphate dehydrogenase were measured at each age, as well as the peroxisomal core enzyme, urate oxidase, and the mitochondrial matrix enzyme, glutamate dehydrogenase. All of these activities were very low or undetectable before birth. Mitochondrial glutamate dehydrogenase and peroxisomal urate oxidase reached maximal activities per g of liver at two and five weeks of age, respectively. Fatty acid beta-oxidation in both peroxisomes and mitochondria and peroxisomal glycerol-3-phosphate dehydrogenase exhibited maximum activities per g of liver between one and two weeks of age before weaning and then decreased to steady state levels in the adult. Peroxisomal beta-oxidation accounted for at least 10% of the total beta-oxidation activity in the young rat liver, but became 30% of the total in the liver of the adult female and 20% in the adult male due to a decrease in mitochondrial beta-oxidation after two weeks of age. The greatest change in beta-oxidation was in the mitochondrial fraction rather than in the peroxisomes. At two weeks of age, four times as much beta-oxidation activity was in the mitochondria as in the peroxisomal fraction. Peroxisomal glycerol-3-phosphate dehydrogenase activity accounted for 5% to 7% of the total activity in animals younger than one week, but only 1% to 2% in animals older than one week. Up to three weeks of age, 85% to 90% of the liver catalase was recovered in the peroxisomes. The activity of peroxisomal catalase per g of rat liver remained constant after three weeks of age, but the total activity of catalase further increased 2.5- to 3-fold, and all of the increased activity was in the supernatant fraction.
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PMID:Postnatal development of peroxisomal and mitochondrial enzymes in rat liver. 11 70

Adaptation of Ehrlich ascites tumor cells to serial cultivation in media with progressively elevated (hypertonic) NaCl content ("high NaCl"-tolerant cells) has resulted in progressive increases of the cellular activities of NAD-dependent glycerol-3-phosphate dehydrogenase (EC 1.1.1.8), NAD-dependent malate dehydrogenase (EC 1.1.1.37), glutamate--oxalacetate transaminase (EC 2.6.1.1), NAD (P)-dependent glutamate dehydrogenase (EC 1.4.1.3), NADP-dependent isocitrate dehydrogenase (EC 1.1.1.42). The activities of glutamate-pyruvate transaminase (EC 2.6.1.2.) and of glycolytic enzymes as phospho-fructokinase (EC 2.7.1.11), glyceraldehydephosphate dehydrogenase (EC 1.2.1.12) and lactate dehydrogenase (EC 1.1.1.27) were only slightly and not in progressive manner (in response to the progressive increase of the environmental NaCl concentration) affected. These changes are discussed with respect to a metabolic pattern of these "high NaCl"-tolerant cells which is compatible with increased energy requirements, especially for active cation transport. It is suggested that these increased cellular enzyme activities reflect an increased transfer of reducing equivalents across mitochondrial membranes (via the "glycerophosphate cycle and the malate-aspartate shuttle") and possibly a stimulated lipid metabolism. These alterations in the level of enzyme activities must be regarded asan adaptive cellular response to the "high NaCl" environment, since readaptation to growth in regular isotonic media resulted in a reversion to the enzyme pattern characteristic of the parent cells.
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PMID:Changes in enzyme pattern of Ehrlich ascites tumor cells following serial cultivation in media with increased (hypertonic) NaCl content. 12 1

Enzyme-histochemical methods were used to study the metabolic activity of specialized ependyma of the ventrolateral walls and floor of the third ventricle in young male and female rats during the "critical period" of sexual differentiation of the hypothalamus (one week after birth). Histochemical tests were conducted for glutamic dehydrogenase, lactic dehydrogenase, glucose-6-phosphate dehydrogenase, glycerophosphate dehydrogenase and NADH2-dehydrogenase. Enzyme activity was judged by cytospectrophotometry. All the data were treated statistically. It was found that the specialized ependyma of the ventrolateral wall and floor of the third ventricle (median eminence) in rats differed in their enzyme behaviour in males and females during the "critical period" of sexual differentiation of the hypothalamus. At the level of the arcuate nucleus (alpha2-tanycytes) and the medial part of the median eminence (beta2-tanycytes) the ependyma was characterized by similar indices of metabolic activity in males and females in the decisive terms of the "critical period" (days 3, 5, and 7). On day 5 metabolic activity of these cells was reduced both in the males and in the females. Prominent sexual differences in the intensity of the enzyme reactions studied were noted in the ependyma of the lateral parts of the median eminence (beta1-tanycytes) in the "critical period". On day 5 metabolic activity of beta1-tanycytes was reduced in males and increased in females. It is suggested that these differences are caused by the receptor nature of beta1 tanycytes and suggest their implication in the mechanisms of sexual differentiation of hypothalamus.
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PMID:Morphological aspects of the hypothalamic-hypophyseal system. VI. The tanycytes: their relation to the sexual differentiation of the hypothalamus. An enzyme-histochemical study. 99 Dec 50

The occurrence and levels of activity of various enzymes of carbohydrate catabolism in culture forms (promastigotes) of 4 human species of Leishmania (L. brasiliensis, L. donovani, L. mexicana, and L. tropica) were compared. These organisms possess enzymes of the Embden-Meyerhof pathway but lack lactate dehydrogenase. No evidence could be found for the production of lactic acid by growing cultures and lactic acid could not be detected either in cell-free preparations or after incubation of cell-free extracts with pyruvate and NADH under appropriate conditions. All 4 species possess alpha-glycerophosphate dehydrogenase and alpha-glycerophosphate phosphatase which together could regenerate NAD, thus compensating for the absence of lactate dehydrogenase. The oxidative and nonoxidative reactions of the hexose monophosphate pathway are present in all 4 species. Cell-free extracts have pyruvate dehydrogenase activity which allows the entry of pyruvate into and its subsequent oxidation through the tricarboxylic acid cycle. All enzymes of this cycle, including a thiamine pyrophosphate dependent alpha-ketoglutarate dehydrogenase, are present. Both NAD and NADP-linked malate dehydrogenase activities are present. The isocitrate dehydrogenase is NADP specific. There is an active glutamate dehydrogenase which could compete with alpha-ketoglutarate dehydrogenase for the common substrate (alpha-ketoglutarate). Replenishment of C4 acids is accomplished by heterotrophic CO2 fixation catalyzed by pyruvate carboxylase. All 4 species have high levels of NADH oxidase activity. Several enzymes thus far not found in any species of Leishmania have been demonstrated. These are: phosphoglucose isomerase, triose phosphate isomerase, fructose-1, 6-diphosphatase, 3-phosphoglycerate kinase, enolase, alpha-glycerophosphate dehydrogenase, alpha-glycerophosphate phosphatase, pyruvate dehydrogenase complex, citrate synthase, aconitase, alpha-ketoglutarate dehydrogenase, glutamate dehydrogenase, and NADH oxidase.
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PMID:Enzymes of carbohydrate metabolism in four human species of Leishmania: a comparative survey. 100 46

When cultured mouse pancreatic islets were exposed for 30 min to streptozotocin (STZ; 1.8 mM) and then maintained for 7 days in tissue culture, they displayed a decreased secretory response to D-glucose and an impairment of both FAD-linked glycerophosphate dehydrogenase and NAD-dependent 2-ketoglutarate dehydrogenase specific activities, with little change in either NAD-linked glycerophosphate dehydrogenase or glutamate dehydrogenase activity. The enzymatic defect was not reproduced by prolonged exposure of either rat islets to interleukin-1 (10 U/ml) or mouse islets to a high concentration of D-glucose (28 mM). In the former, but not latter, situation, the secretory response to D-glucose was again impaired. These findings reveal that STZ, but not all beta-cytotoxic agents, lowers the activity of selected islet mitochondrial dehydrogenases. Such enzymatic defects, especially the suppression of FAD-linked glycerophosphate dehydrogenase, may explain the preferential alteration of the B-cell metabolic and secretory responses to D-glucose, as previously observed in islets of adult rats injected with STZ during the neonatal period.
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PMID:Long term in vitro effects of streptozotocin, interleukin-1, and high glucose concentration on the activity of mitochondrial dehydrogenases and the secretion of insulin in pancreatic islets. 153 41

In islets from adult rats injected with streptozocin during the neonatal period, the oxidative and secretory responses to D-glucose are more severely affected than those evoked by L-leucine. A possible explanation for such a preferential defect was sought by comparing the rate of aerobic glycolysis, taken as the sum of D-[3,4-14C]glucose conversion to labeled CO2, pyruvate, and amino acid, with the total glycolytic flux, as judged from the conversion of D-[5-3H]glucose to 3H2O. A preferential impairment of aerobic relative to total glycolysis was found in islets from diabetic rats incubated at either low or high D-glucose concentration. This coincided in islet mitochondria of diabetic rats with a severe decrease in both the basal (no-Ca2+) generation of 3H2O from L-[2-3H]glycerol-3-phosphate and the Ca2(+)-induced increment in [3H]glycerophosphate detritiation. The mitochondria of diabetic rats were also less efficient than those of control animals in generating 14CO2 from [1-14C]-2-ketoglutarate. The diabetes-induced alteration of 2-ketoglutarate dehydrogenase in islet mitochondria was less marked, however, than that of the FAD-linked glycerophosphate dehydrogenase and was not associated with any change in responsiveness to Ca2+. Sonicated islet mitochondria of diabetic rats displayed normal to slightly elevated glutamate dehydrogenase activity. We propose, therefore, that the preferential impairment of the oxidative and secretory responses of islet cells to D-glucose in this experimental model of diabetes may be at least partly attributable to an altered transfer of reducing equivalents into the mitochondria as mediated by the glycerol phosphate shuttle.
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PMID:Impairment of glycerol phosphate shuttle in islets from rats with diabetes induced by neonatal streptozocin. 182 72

Injection of streptozotocin (30-40 mg/kg body weight) to adult rats caused within 4-6 days a sizeable decrease in the activity of FAD-linked glycerophosphate dehydrogenase in pancreatic islets, with little change in either glutamate dehydrogenase or 2-oxoglutarate dehydrogenase activity. The severity of the enzymatic defect was related to that of the diabetic state, although a decreased enzymic activity was also observed in islets from virtually normoglycemic animals examined 2-3 weeks after streptozotocin injection. The administration of nicotinamide prior to that of streptozotocin prevented the change in enzymic activity. It is proposed that the enzymatic defect, rather than being attributable to a genomic effect of streptozotocin, may reflect the preferential impairment of a subpopulation of pancreatic B-cells.
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PMID:Streptozotocin-induced suppression of FAD-linked glycerophosphate dehydrogenase in pancreatic islets of adult rats. 183 60

The vinylogue of NAD, 3-pyridylacryloamide adenine dinucleotide, was prepared from NAD and 3-pyridylacryloamide through the snake venom NADase-catalyzed transglycosidation reaction. The analog, purified by ion-exchange chromatography, was obtained in a 55% yield. The cyanide adduct and reduced form of the analog exhibited absorbance maxima at 358 nm and 378 nm, respectively, with extinction coefficients in each case being 2.3-times higher than those reported for the corresponding NAD derivatives. 3-Pyridylacryloamide adenine dinucleotide served as a coenzyme with bovine liver glutamic dehydrogenase and to a lesser extent with malate and lactate dehydrogenases. The analog was not reduced in reactions catalyzed by yeast and horse liver alcohol dehydrogenases, sheep liver sorbitol dehydrogenase, and rabbit muscle glycerophosphate dehydrogenase. Substitution of the pyridylacryloamide analogs for NAD and NADH in the assay of substrates for glutamic dehydrogenase was demonstrated.
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PMID:Preparation and characterization of the NAD vinylogue, 3-pyridylacryloamide adenine dinucleotide. 188 17

Cytochemical activity of succinate dehydrogenase (SDG), L-glycerophosphate dehydrogenase (L-GPDG), lactate dehydrogenase (LDG), and glutamate dehydrogenase (GDG) increased immediately after total-body irradiation with a dose of 129 mC/kg. After 2 h, LDG activity only returned to the control level. Irradiation of the head with the same dose caused less pronounced changes. Changes caused by lethal irradiation (1290 mC/kg) were different: there was an increase after exposure of the abdomen and a decrease in the activity of SDG and L-GPDG after irradiation of the head.
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PMID:[Effect of gamma-irradiation on the enzyme activity of cerebrospinal fluid lymphocytes in dogs]. 397 72

As topochemically demonstrated, glutamate dehydrogenase is present within the dendritic layers of the rat hippocampus formation. Its activity increased in parallel to the postnatal maturation of synaptic structures. The results point to a contribution of glutamate dehydrogenase in the synthesis of transmitter glutamate. concomitantly, the activity of succinate and alpha-glycerophosphate dehydrogenase increased in the hippocampal dendritic areas during the postnatal development which is discussed expressing of metabolic activity. The results of the formazan elution technique reflect the topochemical findings in a quantitative manner.
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PMID:Topographic and quantitative characteristics of glutamate dehydrogenase of the hippocampus formation during the postnatal development of the rat brain. Comparative studies on succinate and alpha-glycerophosphate dehydrogenase with special reference to putatively glutamatergic structures. 612 55


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