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)

Mitochondrial functions were investigated in permeabilized rat liver cells. For permeabilization isolated hepatocytes were treated with digitonin using a perifusion technique. After permeabilization the cell count was almost unchanged, and the mitochondrial marker enzyme, glutamate dehydrogenase, was decreased to as little as 83%. The mitochondria in permeabilized cells were functionally intact, a finding evident from a marked stimulation of respiration by ADP, inhibition by carboxyatractyloside, and stimulation by uncoupler. The ADP-stimulated and uncoupled respiration rates with succinate as substrate were comparable to those reported for isolated mitochondria, whereas the rates with NAD(+)-dependent substrates were somewhat higher. The ratios between ADP-stimulated and carboxyatractyloside-inhibited respiration rates were in the range noted for isolated mitochondria with identical substrates. Almost unchanged ADP-stimulated and carboxyatractyloside-inhibited respiration rates were found for at least 180 min after digitonin treatment. The preparation exhibited only a low extramitochondrial ATPase activity which was partially inhibited by vanadate.
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PMID:Characterization of mitochondrial functions in digitonin-permeabilized rat liver cells. 261 33

It has been proposed that cellular ageing may be caused by loss of mitochondrial function due to the action of free radicals. To investigate this hypothesis, antigenic structures of the mitochondrial inner membrane/matrix and of the outer mitochondrial membrane of human diploid fibroblasts were monitored by immunoblotting at four stages during cellular lifespan in vitro. At the same time, specific activities of the enzymes oligomycin-sensitive ATPase (O-S ATPase), malate dehydrogenase (MDH) and glutamate dehydrogenase (GDH) were assayed to assess the functional capacity of cellular oxidative phosphorylation and of the tricarboxylic acid cycle. No changes were found with ageing in inner mitochondrial membrane-associated matrix components, or in the activities of O-S ATPase and MDH. However GDH activity increased significantly with ageing in vitro, possibly indicating greater amino acid utilization for energy production in older cells. There was loss of an outer mitochondrial membrane antigen, of approximate molecular weight 60 kilodaltons (kDa), in the oldest cells tested, which may influence outer membrane transport capacity late in the cellular lifespan. Overall, the results fail to provide support for the hypothesis that ageing primarily results from free radical-induced impairment of mitochondrial function.
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PMID:Mitochondrial antigenic structure and enzyme activity in ageing human diploid fibroblasts. 278 45

The effects of several natural products extracted from the leaves of Stevia rebaudiana on rat liver mitochondria were investigated. The compounds used were stevioside (a non-caloric sweetener), steviolbioside, isosteviol and steviol. Total aqueous extracts of the leaves were also investigated. S. rebaudiana natural products inhibited oxidative phosphorylation, ATPase activity NADH-oxidase activity, succinate-oxidase activity, succinate dehydrogenase, and L-glutamate dehydrogenase. The ADP/O ratio was decreased. Substrate respiration (state II respiration) was increased at low concentrations (up to 0.5 mM) and inhibited at higher concentrations (1 mM or more). In uncoupled mitochondria, inhibition of substrate respiration was the only effect observed. Net proton ejection induced by succinate and swelling induced by several substrates were inhibited. Of the compounds investigated, the sweet principle stevioside was less active. It was concluded that, in addition to the inhibitory effects, S. rebaudiana natural products may also act as uncouplers of oxidative phosphorylation. The possible physiologic consequences of the ingestion of stevioside and S. rebaudiana aqueous extracts are discussed.
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PMID:Effects of Stevia rebaudiana natural products on rat liver mitochondria. 285 11

Studies of various parameters of amino acid and catecholamine metabolism in human cerebral cortex have provided a number of biochemical markers that appear to delineate areas of focal epileptic activity. These observations have been consolidated further by investigations of a number of experimental models of epilepsy in animals. In appraising this data, it is important to take into consideration whether the tissue samples were obtained during an actual seizure state or in an interictal period. It is also important when possible to assess the extent of astrogliosis and neuronal loss. Sites of spontaneously active epileptic spiking in the cerebral neocortex have a somewhat different amino acid profile when compared to gray matter obtained from surrounding nonspiking gyri several centimeters away. There is an elevation in glycine content, a relative diminution in taurine, and a trend towards lowered glutamic acid levels. However, the concentrations of the eight amino acids measured appear in both the foci and surround to still be within the general range for normal tissue. Measurements of key enzymes involved in the synthesis and regulation of neurotransmitters provide a complementary method of evaluating functional changes in epileptic brain as they are generally less labile than their substrates. There is a moderate increase in the activity of glutamic acid dehydrogenase, an enzyme that plays an important role in the synthesis of glutamic acid from glucose. In some patients a decrease in glutamic acid decarboxylase has also been reported: this enzyme forms gamma-aminobutyric acid (GABA) from glutamic acid and is thus important for inhibition in the central nervous system. Moreover, there is a striking increase in the activity of tyrosine hydroxylase, the rate-limiting enzyme responsible for catecholamine synthesis. The possibility of a focal abnormality in catecholamine metabolism is reinforced by the simultaneous finding of a relative decrease in the number of alpha-1 postsynaptic receptor sites. An important marker of energy metabolism in neural tissue, Na+,K+-ATPase activity, has also been found to be decreased in actively spiking human cerebral cortex. Data from experimental animal foci produced by topical application of convulsant agents show a consistent drop in glutamic acid tissue content. This can be matched to an efflux of glutamic acid from the cortical surface, which in turn is proportional to the electrographic activity of the spike focus. In addition, there is often also a decrease in taurine and GABA in such foci, as well as an increase in the levels of a number of neutral amino acids.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Amino acid and catecholamine markers of metabolic abnormalities in human focal epilepsy. 287 18

Activities of glutamate-, succinate-, malate dehydrogenases and H+-ATPase were studied in liver tissue and these of malate- and glutamate dehydrogenases--in blood serum of rats which received nitrosodimethylamine (0.1, 1.0 and 10 mg per I l of water) within 2.5 and 10 months. Cyclic alterations in activities of malate- and succinate dehydrogenases were found in liver tissue of these rats, while the activities of glutamate dehydrogenase and H+-ATPase were changed depending on concentration and duration of the carcinogen effect. Unfavourable alterations in the functional state of mitochondrial enzymatic systems were increased according to intensity and duration of nitrosodimethylamine effect.
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PMID:[Effect of various concentrations of nitrosodimethylamine on the functional state of enzyme systems in rat liver mitochondria depending upon the duration of exposure]. 296 45

The ATP-binding component (Component II, hereafter referred to as ClpA) of a two-component, ATP-dependent protease from Escherichia coli has been purified to homogeneity. ClpA is a protein with subunit Mr 81,000. It has an intrinsic ATPase activity and activates degradation of protein substrates only in the presence of a second component (Component I, hereafter referred to as ClpP), Mg2+, and ATP. The amount of ClpA varies by less than a factor of 2 in cells grown in different media and at temperatures from 30 to 42 degrees C. ClpA does not appear to be a heat-shock protein since its synthesis is not dependent on htpR. Antibodies against purified ClpA were used to identify lambda transducing phage bearing the clpA gene. The cloned gene contains a DNA sequence expected to code for the first 28 amino acids of ClpA, which were determined by protein sequencing of purified ClpA. The clpA gene in the phage was mutated by insertion of delta kan defective transposons and the mutations were transferred to E. coli by homologous recombination. The clpA gene was mapped to 19 min on the E. coli chromosome. Mutant cells with insertions early in the gene produce no ClpA protein detectable in Western blots, and extracts of such mutant cells have no detectable ClpA activity. clpA- mutants grow well under all conditions tested and are not defective in turnover of proteins during nitrogen starvation nor in the turnover of such highly unstable proteins as the lambda proteins O, N, and cII, or the E. coli proteins SulA, RcsA, and glutamate dehydrogenase. The degradation of abnormal canavanine-containing proteins is defective in clpA mutants especially in cells that also have a lon- mutation. Extracts of clpA- lon- cells have ATP-dependent casein degrading activity.
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PMID:The two-component, ATP-dependent Clp protease of Escherichia coli. Purification, cloning, and mutational analysis of the ATP-binding component. 304 6

Within the uterine glands, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetyl-hexosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, acid phosphatase, alkaline phosphatase, esterases, cytochrome oxidase, 5-nucleotidase, leucine aminopeptidase, adenosine triphosphatase, diaphorases (NADH, NADPH), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase (NAD, NADP), beta-hydroxybutyrate dehydrogenase, glycero-3-phosphate dehydrogenase, NAD-glycero-3-phosphate dehydrogenase, glutamate dehydrogenase (NAD, NADP), lactate dehydrogenase. The results show that the activities of G-6-PDH, 6-PGDH, and cytochrome oxidase increase within secreting cells during the 2nd half of pregnancy. The activities of the other enzymes remained almost unchanged during the period of investigation. The description of our results distinguishes between gland neck, middle, and distal part of the secretory unit, respectively. In general, the enzyme activities are similar within the middle and distal gland segments, but lower in the epithelia of the neck region. The activity of dehydrogenases was medium to intensive within the middle and distal gland segments, but only low to medium within the neck portion. Of the hydrolases, the acid phosphatase, ATPase, leucine aminopeptidase, and beta-galactosidase demonstrated an intensive activity within activity secreting cells. The enzyme activities of the gland epithelia are compared with these of the uterine surface epithelia and the histochemical results are discussed in context with their significance in histiotrophic nutrition.
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PMID:[Enzyme histochemistry of the pig placenta. III. Histotopics of enzymes in the uterine epithelium]. 309 49

Treatment of the inner membrane matrix fraction of rat liver mitochondria with the nonionic detergent Lubrol WX solubilized about 70% of the total protein and 90% or more of the following matrix activities: malate dehydrogenase, glutamate dehydrogenase, and isocitrate dehydrogenase (NADP). The Lubrol-insoluble fraction was enriched in cytochromes, phospholipids, and a Mg(++)-stimulated ATPase activity. Less than 2% of the total mitochondrial activity of monoamine oxidase, an outer membrane marker, or adenylate kinase, an intracristal space marker could be detected in this inner membrane fraction. Electron micrographs of negatively stained preparations showed vesicles (</=0.4 micro diameter) literally saturated on the periphery with the 90 A ATPase particles. These inner membrane vesicles, which appeared for the most part to be inverted with respect to the normal inner membrane configuration in intact mitochondria, retained the succinicoxidase portion of the electron-transport chain, an intact phosphorylation site II with a high affinity for ADP, and the capacity to accumulate Ca(++). A number of biochemical properties characteristic of intact mitochondria and the inner membrane matrix fraction, however, were either absent or markedly deficient in the inner membrane vesicles. These included stimulation of respiration by either ADP or 2,4-dinitrophenol, oligomycin-sensitive ADP-ATP exchange activity, atractyloside sensitivity of adenine nucleotide requiring reactions, and a stimulation of the Mg(++)-ATPase by 2,4-dinitrophenol.
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PMID:Biochemical and ultrastructural properties of a mitochondrial inner membrane fraction deficient in outer membrane and matrix activities. 425 78

The activities of adenine nucleotide translocase (ANT), Na+-K+-ATPase (EC 3.6.1.3) and Mg2+-ATPase (EC 3.6.1.3) together with mitochondrial marker enzymes, succinic dehydrogenase (EC 1.3.99.1) and glutamate dehydrogenase (EC 1.4.1.2), were measured in liver, kidney, brain and testis from normal and thyroidectomised rats. Na+-K+-ATPase decreased by approximately 50% in liver and kidney; ANT decreased only in liver (-40%) while the activity of ANT per gram kidney increased by 38%. The activity of Mg2+-ATPase closely correlated with the pattern of change of ANT. The hormonal and substrate regulation of ANT is discussed in relation to its role in the regulation of intracellular phosphate potential and compartmentation in liver and kidney.
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PMID:Adenine nucleotide translocase, Na+-K+-and Mg2+-ATPases and differential tissue response to hypothyroidism. 612 72

Content of progesterone and cortisol was studied in blood plasma. Activities of organelle-specific enzymes were estimated in mitochondria (malate dehydrogenase, glutamate dehydrogenase, H + ATPase) and in endoplasmic reticulum (inosine-5-diphosphatase) of liver, kidney tissues and blood serum of rats, which were born after the influence of embryotoxic effectors. Correlation was found in alterations of the patterns studied. The steroid hormonal systems appear to affect the stability of mitochondrial and microsomal membranes in liver and kidney tissues of experimental animals.
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PMID:[Correlation between the changes in the functional state of enzyme and hormonal systems of the mature rat]. 614 50


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