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

---

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

For the analysis of the molecular mechanism of the action of peroxisome proliferators, we attempted to establish the optimal conditions for obtaining the effects of the chemicals in vitro, employing an established cell line, Reuber rat hepatoma H4IIEC3. Histochemical analyses revealed a marked increase in the number, size, and catalase content of peroxisomes in the cells cultured on a medium containing 0.5 mM ciprofibrate, a peroxisome proliferator. The activity of acyl-CoA oxidase, the initial enzyme of the peroxisomal beta-oxidation system, was increased by more than 10-fold by the same treatment. Catalase was also induced significantly, whereas the activities of glutamate dehydrogenase and lactate dehydrogenase, mitochondrial and cytosolic marker enzymes, did not change upon the treatment. Immunoblotting and RNA-blotting analyses confirmed the increases in the amount of protein and mRNA for all the three enzymes of the peroxisomal beta-oxidation system. Cell fractionation experiments gave a partial separation of peroxisomes from other organelles for the induced culture. Thus, H4IIEC3 cells offer a good in vitro model system of the induction of peroxisomes and peroxisomal beta-oxidation enzymes by peroxisome proliferators.
...
PMID:Proliferation of peroxisomes and induction of peroxisomal beta-oxidation enzymes in rat hepatoma H4IIEC3 by ciprofibrate. 212 77

A study was conducted on the effects of 12-O-tetradecanoyl-phorbol-13-acetate (TPA) on peroxisomal enzyme activities in mouse embryo fibroblasts C3H/10T1/2 C18 cells and chemically transformed C3H/10T1/2 MCA16 cells. TPA is a potent tumour promoter and treatment with this compound of the two cell lines induced peroxisomal fatty acid beta-oxidation, carnitine acetyltransferase, palmitoyl-CoA hydrolase, and catalase activities after 240 h of treatment. Stimulation of the corresponding enzyme activities was dose-related and cycloheximide inhibited the TPA-induced enzyme activities, except that of carnitine acetyltransferase. The MCA16 cells appeared to be more sensitive than the C18 cells in inducing peroxisome-associated enzyme activities after TPA treatment. The activities of the microsomal marker, NADPH-cytochrome c reductase and the mitochondrial marker, glutamate dehydrogenase were not enhanced by TPA treatment. The results indicate that TPA has peroxisomal effects and may be classified as a peroxisome proliferator.
...
PMID:The tumour promoter 12-O-tetradecanoylphorbol-13-acetate increases the activities of some peroxisome-associated enzymes in in vitro cell culture. 286 50

L-Pipecolic acid oxidation was studied in the rabbit and cynomolgus monkey. Tissue homogenates from both species incubated with L-[2,3,4,5,6-3H]pipecolic acid produced a single radioactive product identified as alpha-aminoadipic acid. In the rabbit, L-pipecolic acid oxidation was greatest in kidney cortex with progressively lesser specific activities in liver, heart, and brain. When rabbit kidney cortex was fractionated by differential centrifugation or on Percoll gradients, activity paralleled that of the mitochondrial marker, glutamate dehydrogenase. In sonicated mitochondria, 92% of the activity was in the soluble fraction. Activity was inhibited by both rotenone and antimycin A and was maximal when FAD, phenazine ethosulfate, and glycerol were included in the assay; Km,app was 0.74 +/- 0.16 mM. Nipecotic acid, piperidine, and cis-2,4-piperidine dicarboxylic acid did not inhibit L-pipecolic acid oxidation, while L-proline had a Ki greater than or equal to 10 mM. D-Alanine and kojic acid, substrate and inhibitor of D-amino acid oxidase, respectively, were also not inhibitory. When monkey kidney cortex was fractionated on Percoll gradients, L-pipecolic acid oxidation activity paralleled that of the peroxisomal marker, catalase. After organellar subfractionation, the activity was membrane-associated and maximal at pH 8.5; Km,app was 4.22 +/- 0.30 mM. L-Pipecolic acid oxidation produced hydrogen peroxide, suggesting involvement of an oxidase in alpha-aminoadipic acid formation. Antimycin A did not inhibit the reaction. No specific cofactor requirements were identified and phenazine ethosulfate inhibited the reaction. D-Pipecolic acid, L-proline, and the other compounds cited above did not significantly inhibit the activity.
...
PMID:L-pipecolic acid oxidation in the rabbit and cynomolgus monkey. Evidence for differing organellar locations and cofactor requirements in each species. 291 18

Squalene synthetase activity in liver microsomes from rats sacrificed at three different times of the diurnal cycle showed no significant differences. Addition of 4% cholestyramine to the food resulted in a marked increase in activity (280% of control), independent of the time of killing. 3-Hydroxy-3-methylglutaryl coenzyme A reductase and cholesterol 7 alpha-hydroxylase activity, determined as positive controls, were also found to be elevated by cholestyramine and additionally showed a diurnal variation. On the other hand, five control enzyme activities, not directly related to cholesterol metabolism, i.e. glutamate dehydrogenase, NADPH cytochrome-c reductase, beta-hexosaminidase, catalase and acyl coenzyme A oxidase, showed neither an influence of cholestyramine feeding nor a time of sacrifice dependent variation.
...
PMID:Regulation of squalene synthetase activity in rat liver: elevation by cholestyramine, but no diurnal variation. 294 75

Serum catalase activity was moderately increased in fatty liver, acute alcoholic hepatitis and in the decompensated form of cardiac circulatory failure. It showed significant increase in acute yellow atrophy and in toxic hepatitis while no changes were detected in liver cirrhosis and viral hepatitis. Serum catalase activity showed a good correlation (r = 0.820) with the serum glutamate dehydrogenase activity. In accordance with our results, the inexpensive assay of serum catalase activity is suggested for the detection of severe liver cell damage.
...
PMID:Serum catalase enzyme activity in liver diseases. 345 88

A new carnitine palmitoyltransferase (CPT) was purified to homogeneity from bovine liver mitochondria which were 96% free of peroxisomal contamination, as judged by catalase and glutamate dehydrogenase activities. The enzyme is easily removed from mitochondria, without the use of detergent. It is monomeric (Mr 63,500), unlike other preparations of CPT from mitochondria, and is most active with myristoyl-CoA and palmitoyl-CoA. The Km values are between 0.8 and 4 microM for a range of substrates from hexanoyl-CoA to stearoyl-CoA; these are much lower than values reported for other purified CPT preparations. The Km for L-carnitine is 185 microM measured with palmitoyl-CoA, and does not vary greatly with the chain length. This is also lower than the values reported for other CPT preparations, but higher than those cited for the medium-chain transferases. Kinetic and inhibitor studies were consistent with a rapid-equilibrium random-order mechanism. 2-Bromopalmitoyl-CoA, which is an inhibitor of the outer CPT, inhibited the enzyme competitively with palmitoyl-CoA as the variable substrate, when added without preincubation. If the enzyme was preincubated with 2-bromopalmitoyl-CoA and carnitine, the activity did not reappear after gel filtration of the protein. The inhibitor was bound in a 1:1 stoichiometry per subunit of enzyme.
...
PMID:Purification and properties of the soluble carnitine palmitoyltransferase from bovine liver mitochondria. 366 21

Experiments were conducted on 128 male rats kept on a retinol-deprived diet during 12-14 weeks, that resulted in vitamin A deficiency. The content of phospholipids, total lipids, proteins and the activity of esterase, glutamate dehydrogenase, catalase, glutathione-S-transferase, aldehyde dehydrogenase and aldehyde oxidase were assayed in the bronchoalveolar lavage fluid, in homogenates and microsomes of the lungs. The content of phospholipids in the bronchoalveolar lavage fluid was reduced up to 63.9%, as compared to that in the control rats, while the protein content was unchanged. The levels of phospholipids, total lipids and protein rose in the homogenates and microsomes of the lungs. Esterase activity decreased up to 38.6% of the control level, catalase--up to 73.2%, glutamate dehydrogenase--up to 79%. There was a tendency to decrease in glutathione-S-transferase activity, while aldehyde dehydrogenase and aldehyde oxidase activities remained unchanged. It is suggested that the disorders in the enzymatic activity and lipid content in the surfactant can be responsible for the changes in the xenobiotic biotransformation and for the rise in xenobiotic toxicity.
...
PMID:[Effect of vitamin A deficiency on surfactants and enzymes of xenobiotic metabolism in the rat lung]. 367 17

Thirty strains were isolated from pasteurized soil samples by enrichment culture in aerobiosis at 32 degrees C in a minimal medium containing one of the following compounds as sole source of carbon and energy: quinate, p-hydroxybenzoate, phthalate, isophthalate or trimellitate. These bacteria were rods (0.8 X 2-7 micron), motile by peritrichous flagella. Endospores were oval (1.4-1.8 X 2 micron) and distinctly swelled the sporangia. The Gram reaction was variable but the Gram type was positive. Colonies were smaller on peptone (0.4%) agar than on minimal salts-glucose (0.2%) agar. The following characters were always present: growth in the presence of lysozyme, cytochrome c oxidase, catalase, nitrate assimilation, urease, amylase and L-glutamate dehydrogenase. The cells contained glycogen. In anaerobiosis, glucose was not fermented and nitrate was not used as a respiratory acceptor of electrons. Of 215 substrates tested, 31 (including 9 aromatic compounds) were used as sole carbon and energy sources by all 30 strains, and 38 substrates (including 13 aromatic compounds) were used by only some of them; 146 substrates (including 49 aromatic compounds) were not used by any of the 30 strains. No amino acid could be used as sole carbon and energy source. Numerical analysis of the 30 strains showed an aggregate cluster made of 5 phena. The mean G + C content of the DNA was 55 +/- 0.6 mol %. The described bacteria are clearly different from the 2 known species of the second morphological group which cannot ferment carbohydrates: Bacillus brevis and B. azotoformans. Strain Q1 (ATCC 29948) is the holotype of Bacillus gordonae sp. nov.
...
PMID:[Bacillus gordonae sp. nov., a new species belonging to the second morphological group, degrading various aromatic compounds]. 367 81

In order to study the intracellular localization of the proteolytic processing steps in the maturation of alpha-glucosidase and cathepsin D in cultured human skin fibroblasts we have used incubation with glycyl-L-phenylalanine-beta-naphthylamide (Gly-Phe-NH-Nap) as described by Jadot et al. [Jadot, M., Colmant, C., Wattiaux-de Coninck, S. & Wattiaux, R. (1984) Biochem. J. 219,965-970] for the specific lysis of lysosomes. When a homogenate of fibroblasts was incubated for 20 min with 0.5 mM Gly-Phe-NH-Nap, a substrate for the lysosomal enzyme cathepsin C, the latency of the lysosomal enzymes alpha-glucosidase and beta-hexosaminidase decreased from 75% to 10% and their sedimentability from 75% to 20-30%. In contrast, treatment with Gly-Phe-NH-Nap had no significant effect on the latency of galactosyltransferase, a marker for the Golgi apparatus, and on the sedimentability of glutamate dehydrogenase and catalase, markers for mitochondria and peroxisomes, respectively. The maturation of alpha-glucosidase and cathepsin D in fibroblasts was studied by pulse-labelling with [35S]methionine, immunoprecipitation, polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate and fluorography. When homogenates of labelled fibroblasts were incubated with Gly-Phe-NH-Nap prior to immunoprecipitation, 70-80% of all proteolytically processed forms of metabolically labelled alpha-glucosidase and cathepsin D was recovered in the supernatant. The earliest proteolytic processing steps in the maturation of alpha-glucosidase and cathepsin D appeared to be coupled to their transport to the lysosomes. Although both enzymes are transported via the mannose-6-phosphate-specific transport system, the velocity with which they arrived in the lysosomes was consistently different. Whereas newly synthesized cathepsin D was found in the lysosomes 1 h after synthesis, alpha-glucosidase was detected only after 2-4 h. When a pulse-chase experiment was carried out in the presence of 10 mM NH4Cl there was a complete inhibition of the transport of cathepsin D and a partial inhibition of that of alpha-glucosidase to the lysosomes. Leupeptin, an inhibitor of lysosomal thiol proteinases, had no effect on the transport of labelled alpha-glucosidase to the lysosomes. However, the early processing steps in which the 110-kDa precursor is converted to the 95-kDa intermediate form of the enzyme were delayed, a transient 105-kDa form was observed and the conversion of the 95-kDa intermediate form to the 76-kDa mature form of the enzyme was completely inhibited.(ABSTRACT TRUNCATED AT 400 WORDS)
...
PMID:Biosynthesis and intracellular transport of alpha-glucosidase and cathepsin D in normal and mutant human fibroblasts. 390 6

Five enzymes were measured in 50 liver specimens (18 normal liver, 20 Reye liver, 12 diverse liver disorders other than Reye syndrome). The enzymes were: glutamic dehydrogenase (E.C. 1.4.1.3), monoamine oxidase (E.C. 1.4.3.4), lactate dehydrogenase (E.C. 1.1.1.27), D-glucose-6-phosphate dehydrogenase (E.C. 1.1.1.49), catalase (E.C. 1.11.1.6). The Reye syndrome group showed significant decreases in glutamic dehydrogenase (56%) and monoamine oxidase (70%) compared to normal control tissue and these changes were not characteristic of the non-Reye liver disorder group as a whole. Neither catalase nor lactate dehydrogenase appeared to be altered significantly in the Reye or in the abnormal control group compared with normal controls. Thus, only the prominent decreases in the mitochondrial enzyme activities appeared to be highly characteristic of Reye syndrome. Paradoxically, the means of the five hepatic enzymes and the admission levels of two serum enzymes indicative of liver damage (alanine and aspartate aminotransferase) were remarkably similar for both survivors and nonsurvivors of Reye syndrome.
...
PMID:Quantitative evaluation of the extent of hepatic enzyme changes in Reye syndrome compared with normal liver or with non-Reye liver disorders: objective criteria for animal models. 396 10


<< Previous 1 2 3 4 5 6 7 8 Next >>

---