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:1.4.1.2 (glutamate dehydrogenase)
4,380 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activities of 6 dehydrogenases, lactate dehydrogenase (LDH), glucose-6-phosphate dehydrogenase (G6PDH), isocitrate dehydrogenase (ICDH), glycerol-3-phosphate dehydrogenase (GDH), succinate dehydrogenase (SDH) and glutamate dehydrogenase (GLDH), determined by means of flow cytometry in 13 primary human gastrointestinal tumour cell lines, including 10 esophageal carcinomas, one gastric cancer, and 2 pancreatic cancers. Two-parametric measurements of specific dehydrogenase activities in single cells were performed with DAPI as fluorochrome for the nuclear DNA and with the fluorescent redox system of 5-cyano-2,3-ditolyl-tetrazolium chloride (CTC) which forms brilliant red formazan crystals upon reduction by cellular redox enzymes. Furthermore, with the aid of the calibration procedure reported previously [18] the enzyme activities were expressed as biochemical units. This application of tetrazolium salt technique for demonstrating dehydrogenase activities in human tumour cells by flow cytometry offers an alternative tool to characterize malignant tumors.
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PMID:Flow-cytometric determination of dehydrogenase activities in primary human gastrointestinal tumor cell lines. 816

1. The carcinoma showed higher enzyme activities than the normal mammary tissue. 2. The ratios of glutamate dehydrogenase, glutathione reductase and catalase to lactate dehydrogenase were lower in carcinomas than in normal tissues. Similarly, the ratios of glutamate dehydrogenase, glutathione reductase and catalase to glucose-6-phosphate dehydrogenase were also significantly lower in carcinomas. 3. There were no significant differences in enzyme activities between stages I and II of disease, however in the metastatic tissues, there were significant differences between stages I and II. 4. SH groups were higher in the tissues of cancer patients than in normal tissues. The levels of thiols groups were higher in carcinomas at stage III of disease.
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PMID:Enzyme activities and level of SH groups in breast carcinomas. 822 79

Freeze-substituted rat liver embedded in glycol methacrylate (GMA) has been used to demonstrate the activities of several enzymes. The following enzymes could be detected in GMA-sections by the indicated histochemical procedure(s): 5'-nucleotidase (lead salt, cerium-diaminobenzidine), alkaline phosphatase (indoxyl-tetrazolium salt), catalase (diaminobenzidine), acid phosphatase (diazonium salt), lactate dehydrogenase (tetrazolium salt) and glutamate dehydrogenase (tetrazolium salt). The activities of all these enzymes were dramatically decreased compared with the activities demonstrated in unfixed cryostat sections, with the exception of catalase. The activities of the following enzymes could not be detected in GMA-sections: glucose-6-phosphate dehydrogenase (tetrazolium salt), xanthine oxidoreductase (tetrazolium salt), D-amino acid oxidase (cerium-diaminobenzidine-cobalt-hydrogen peroxide) and glucose-6-phosphatase (cerium-diaminobenzidine). The possible role of restricted penetration of reagents into the resin was studied by measuring cytophotometrically the enzyme activities in GMA-sections of 3 and 6 microns in thickness. For all the enzymes that could be detected, the 6 microns:3 microns ratio varied from 1.4 to 2.7. An eventual retarded penetration of reagents into the resin was investigated by measuring cytophotometrically the amount of final reaction product during incubation for acid phosphatase and glutamate dehydrogenase activities. In both cases linear relationships without a lag phase were found for the specific enzyme activities with incubation time. Chemical denaturation of proteins or masking of active sites in proteins due to embedding in the resin monomer may be considered to be the main cause of decreased enzyme activities.
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PMID:Quantitative aspects of enzyme histochemistry on sections of freeze-substituted glycol methacrylate-embedded rat liver. 827 44

Flow cytometric measurements of the activities of lactate dehydrogenase, glucose-6-phosphate dehydrogenase, isocitrate dehydrogenase, glycerol-3-phosphate dehydrogenase, succinate dehydrogenase and glutamate dehydrogenase in single Ehrlich ascites tumour cells are described using a tetrazolium salt/fluorescent formazan reaction. Applying cyano-ditolyl-tetrazolium chloride (CTC) as redox dye indicating enzyme reaction, and DAPI as a fluorochrome for nuclear DNA staining, the bivariate flow cytometric assay of enzyme activity and cell cycle analysis was established. Furthermore, adopting the calibration procedure reported formerly, consisting of biochemical determination and flow cytometry of the same sample performed parallelly, the enzyme activities were expressed in biochemical units. The dehydrogenase activities found in Ehrlich ascites cells were 97.5 fmol H2 per average positive cell during 5 min for lactate dehydrogenase, 69.0, 10.6, 25.3, 29.7, and 19.0 fmol H2 per average positive cell during 20 min for glucose-6-phosphate dehydrogenase, isocitrate dehydrogenase, glycerol-3-phosphate dehydrogenase, succinate dehydrogenase and glutamate dehydrogenase, respectively. This quantitative procedure can offer an alternative analytic tool for enzyme cytology.
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PMID:Enzyme activities of six different dehydrogenases in Ehrlich ascites cells measured by flow cytometry. 835 66

The effect of storage of unfixed cryostat sections from rat liver for 4 h, 24 h, 3 days and 7 days at -25 degrees C was studied on the activities of lactate dehydrogenase, glucose-6-phosphate dehydrogenase, xanthine oxidoreductase, glutamate dehydrogenase, succinate dehydrogenase (all demonstrated with tetrazolium salt procedures), glucose-6-phosphatase (cerium-diaminobenzidine method), 5'-nucleotidase (lead salt method), dipeptidyl peptidase II, acid phosphatase (both simultaneous azo coupling methods), D-amino acid oxidase (cerium-diaminobenzidine-cobalt-hydrogen peroxide procedure) and catalase (diaminobenzidine method). The effect of drying of the cryostat sections at room temperature for 5 and 60 min was investigated as well. The enzyme activities were quantified by cytophotometric measurements of test and control reactions. The test minus control reaction was taken as a measure for specific enzyme activity. It was found that the activities of all the enzymes investigated, with one exception, were affected neither by storage of the cryostat sections at -25 degrees C for up to 7 days, nor by drying of the sections at room temperature for up to 60 min. The exception was xanthine oxidoreductase, whose activity was reduced by 20% after 5 min drying of sections or after 4 h storage. Therefore, only incubations for xanthine oxidoreductase activity have to be performed immediately after cutting cryostat sections, whereas for the other enzymes a considerable margin appears to exist.
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PMID:The effects of storage on the retention of enzyme activity in cryostat sections. A quantitative histochemical study on rat liver. 846 85

Sixty-one isolates and collection strains of Aspergillus fumigatus were compared for their phenotypic (morphological features and isoenzyme profiles) and genotypic (restriction enzyme-generated mitochondrial DNA and ribosomal DNA profiles and random amplified polymorphic DNA patterns) features. The examined strains exhibited highly variable colony morphologies and growth rates at different temperatures, but their micromorphologies and conidial diameters were characteristic of the species. Of the isoenzymes studied, the beta-arylesterase and phosphatase patterns were the most divergent, and the 61 strains could be classified into seven groups. The glucose 6-phosphate dehydrogenase and catalase isoenzyme patterns displayed only a limited variability, while the profiles of superoxide dismutase, lactate dehydrogenase, and glutamate dehydrogenase were highly conserved. The HaeIII-generated mitochondrial DNA patterns and SmaI-digested repetitive DNA and ribosomal DNA hybridization patterns of almost all strains were also invariable. The level of variation was much higher when random amplified polymorphic DNA analysis was applied. Although the patterns of the strains were very similar with most of the primers, the application of some primers made it possible to cluster the A. fumigatus isolates into several groups. The results indicate that the random amplified polymorphic DNA technique could be used more efficiently than isoenzyme analysis for typing A. fumigatus isolates. A good correlation was found between the dendrograms obtained from the isoenzyme and random amplified polymorphic DNA data, but the isoenzyme and amplified DNA patterns did not correlate with the pathogenicity, pigment production, or geographical origin of the strains. One "A. fumigatus" strain (strain FRR 1266) exhibited unique isoenzyme, mitochondrial DNA, ribosomal DNA, and random amplified polymorphic DNA patterns; it is proposed that this strain represents a new species of the section Fumigati.
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PMID:Phenotypic and genotypic analysis of variability in Aspergillus fumigatus. 856 84

Employing RNA gel mobility shift assays we detected specific binding events between several dehydrogenases and various regions of the GLUT1 mRNA 3'-untranslated region. In particular, the enzymes glyceraldehyde 3-phosphate dehydrogenase (G3PDH), lactate dehydrogenase (LDH), and glucose 6-phosphate dehydrogenase (G6PDH) bound to the GLUT1 3'-UTR while isocitrate dehydrogenase (IDH) and glutamate dehydrogenase (GluDH) did not. Comparison of shifts obtained with purified dehydrogenases to those obtained using authentic cell extracts indicate that G3PDH and G6PDH may play a role in the intact cell.
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PMID:Dehydrogenase binding to the 3'-untranslated region of GLUT1 mRNA. 866 Mar 40

The pregnant rats were treated with formaldehyde (0.5 mg/kg daily per os) during whole period of pregnancy. The activity of cytochrome-c-oxidase, malate dehydrogenase, nucleotidase, glucose-6-phosphatase, beta-glucuronidase, N-acetyl-beta-glucosaminidase, beta-galactosidase, H(+)-ATPase, glutamate dehydrogenase, NAD- and NADP-isocitrate dehydrogenase, fructose-bisphosphate aldolase, glucose-6-phosphate dehydrogenase and content of protein in liver celts of offsprings (newborns, 2 weeks age and 2 months age) were studied. It was shown differences in development enzyme systems of control and experimental animals during ontogenesis.
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PMID:[Experimental study of the effect of formaldehyde during embryogenesis on the activity of rat liver enzyme systems in ontogenesis]. 913 53

We measured enzyme activities along a heterothermic tissue, the visceral retia mirabilia of the bluefin tuna, to test current theories of enzyme temperature adaptation. The heterothermic tissue model is ideal for the study of fundamental temperature adaptation because it eliminates confounding effects of whole animal acclimation. Enzymes were measured at six positions along the rete at four temperatures (15, 20, 25, and 30 degrees C). Five enzymes (aspartate aminotransferase, citrate synthase, glucose-6-phosphate dehydrogenase, glutamate dehydrogenase, and pyruvate kinase) exhibited a significant positive compensatory effect, with activity at the cold end of the rete 1.2-3.1 times higher than at the warm end. Two enzymes (alanine aminotransferase and lactate dehydrogenase) exhibited no significant compensation. On the basis of activation energies of enzymes along the rete, differences in activity were due to differences in enzyme concentration and not isozymes or enzyme modification. Analysis of the compensatory responses of the enzymes in light of their thermal sensitivities leads us to conclude that the pentose phosphate shunt is especially enhanced at the cold end of the rete.
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PMID:Enzyme adaptation along a heterothermic tissue: the visceral retia mirabilia of the bluefin tuna. 922 97

This study was conducted to determine the time course of metabolic changes associated with a switch from a high-fat to a low-fat diet in rats. Adult rats, maintained on a high-fat diet (42% of energy from fat) for 4-5 weeks were switched to a low-fat diet (11% of energy from fat), and the activities of several liver enzymes were followed. Three different phases could be distinguished. The early phase, complete by 2 days after the switch in diets, included an increase in the activity of glucose 6-phosphate dehydrogenase (pentose phosphate pathway), an increase in pyruvate kinase and pyruvate dehydrogenase activities (terminal end of the glycolytic pathway) and an increase in ATP-citrate lyase and fatty acid synthetase (fatty acid synthesis pathway). The early phase also included a decrease in the activity of phosphoenolpyruvate carboxykinase (PEPCK, gluconeogenesis) and a lower branched-chain amino acid dehydrogenase activity (BCAADH, branched-chain amino acid degradation). The concentration of the allosteric phosphofructokinase regulator, fructose 2,6-bisphosphate (Fru-2,6-P2, glycolysis), decreased during the early phase. An intermediate phase could also be discerned between 3 and 10 days after the switch in diets. In this phase, the decreased Fru-2,6-P2 concentration and the decreased PEPCK and BCAADH activities observed in the early phase were reversed. The late phase occurred 10 days after the dietary switch and was characterized by an increase in the activities of glucokinase (glycolytic pathway) and glycogen phosphorylase (associated with glycogenolysis) and by a decrease in glutamate dehydrogenase, PEPCK and BCAADH activities. These measurements indicate that at least 20 days are required before metabolic changes associated with a switch in diet are complete.
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PMID:Time course of enzyme changes after a switch from a high-fat to a low-fat diet. 944 Feb 29


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