Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.4.1.4 (glutamate dehydrogenase)
 4,358 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The mitochondrial redox (NAD+/NADH) state can be used as a reflection of oxygen availability within the mitochondrion. Previous studies using isolated muscle preparations suggest that active muscle is not hypoxic during lactate production, whereas experiments with humans come to the opposite conclusion. Six men exercised for 5 min at 75% maximal O2 consumption (VO2max) and then at 100% VO2max to exhaustion. Ammonia, oxoglutarate (alpha-ketoglutarate), and glutamate, as well as lactate, were measured in biopsies (vastus lateralis) taken at the end of each exercise. The three former metabolites were used to determine the mass action ratio of glutamate dehydrogenase and thus were used as an estimate of the mitochondrial redox state. Muscle lactate increased (P less than 0.05) to 14.5 and 24.5 mmol/kg wet wt after 75 and 100% VO2max, respectively. At both exercise intensities, muscle ammonia rose (P less than 0.05), glutamate fell (P less than 0.05) to only 30-35% of rest levels, and oxoglutarate declined (P less than 0.05). Despite the high levels of muscle lactate accumulation, the estimated mitochondrial redox rate rose 300% (P less than 0.05) in both exercise bouts. This response should increase the activity of key oxidative enzymes and promote increased VO2. Furthermore the data do not support the concept that muscle lactate is formed because of tissue hypoxia.
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PMID:Estimation of the mitochondrial redox state in human skeletal muscle during exercise. 256 30

Cell bodies of cardio-vascular receptors localized in the ganglion nodosum of rabbits exposed to experimental emotional stress were studied with the light and electron microscope and histochemically. Under emotional stress some rabbits demonstrated almost unchanged arterial pressure and only a small increase in heart rate, while other animals displayed strongly marked disturbances of their blood circulation leading to the acute heart deficiency at the end of the experiment. In the stress-resistant rabbits, microscopic anatomy and ultrastructure of neurons indicated their increased activity. Activities of lysosomal enzymes--acid phosphatase and aminopeptidase--were found to be at the control level, while the activity of mitochondrial enzyme--glutamate dehydrogenase--was slightly increased. On the other hand morphological evidence of severe hyperactivity and exhaustion was revealed in neurons of the stress-predisposed rabbits. Moreover the activities of all three enzymes studied were significantly increased. These results indicate correlation between the structural and metabolic changes occurring under experimental emotional stress in nodosal neurons and the extent of hemodynamic changes.
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PMID:Changes in ganglion nodosum neurons associated with stress-related cardiac deficiency. 770 77

Six young men performed five 1-min bicycle exercise bouts to exhaustion. Muscle lactate increased to congruent with 114 mmol x kg(-1) dwt and pH decreased to congruent with 6.6. Mitochondria were prepared from a needle biopsy sample taken from m. vastus lateralis immediately after the last exercise bout. No significant effect of exhaustion on the proton permeability and amount of cytochromes c and aa3 in isolated mitochondria was detected. The activities of the following enzymes and systems were not altered either: citrate synthase, succinate dehydrogenase, cytochrome oxidase, succinate + glutamate respiration, malate + glutamate respiration, the respiratory chain, and the reactions involved in ATP synthesis. Thus, the mitochondria did not appear globally altered upon exhaustion. However, the following NAD-linked activities were significantly lowered: pyruvate dehydrogenase, alpha-ketoglutarate dehydrogenase, glutamate dehydrogenase and fatty acid beta-oxidation. The activities of alpha-glycerophosphate dehydrogenase and exo-NADH oxidase, enzymes that might catalyze the oxidation of sarcoplasmic NADH, were increased. These changes may be due to the action of reactive oxygen species, protons and Ca2+. Transient opening of the permeability transition pore may also be involved. Some effects may have been reversed during isolation of the mitochondria and the changes in mitochondrial function in situ upon exhaustion may have been more extensive than observed.
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PMID:The effect of high-intensity exhaustive exercise studied in isolated mitochondria from human skeletal muscle. 1171 42

Oocystis sp., a unicellular green alga, contained two glutamate dehydrogenase isoenzymes: one was specific for NADH and the other for NADPH. Activity staining after gel electrophoresis indicated that one component in NADH-GDH was not specific for the cofactor and three components in NADPH-GDH. The optimal concentration of substrate, purification procedure and kinetic properties of both glutamate dehydrogenase (GDH) enzymes in vitro are presented. The kinetics of growth, nutrient removal and enzyme activities for Oocystis growing in wastewater showed that ammonia was preferentially utilized over nitrate and the medium was depleted before the maximum population was obtained in indoor culture. There was a sharp increase in NADPH-GDH activity following the exhaustion of ammonia from the medium but NADH-GDH activity remained unchanged. The NADPH-GDH activity at the outset increased exponentially with time in greenhouse culture but then decreased sharply accompanied by a rapid increase in biomass and nitrite concentration. The K(m) values for ammonia in this algal GDH was high, while glutamate synthase activity was not detected; this suggests that Oocystis may adapt to conditions of ammonia limitation by producing large quantities of NADPH-GDH instead of using glutamate synthase pathway.
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PMID:Occurrence of glutamate dehydrogenase isoenzymes during growth of Oocystis alga. 1855 83

Metabolic control of glutamine and glutamate synthesis from ammonia and oxoglutarate in Escherichia coli is tight and complex. In this work, the role of glutamine synthetase (GS) and glutamate dehydrogenase (GDH) regulation in this control was studied. Both enzymes form a linear pathway, which can also have a cyclic topology if glutamate-oxoglutarate amino transferase (GOGAT) activity is included. We modelled the metabolic pathways in the linear or cyclic topologies using a coupled nonlinear differential equations system. To simulate GS regulation by covalent modification, we introduced a relationship that took into account the levels of oxoglutarate and glutamine as signal inputs, as well as the ultrasensitive response of enzyme adenylylation. Thus, by including this relationship or not, we were able to model the system with or without GS regulation. In addition, GS and GDH activities were changed manually. The response of the model in different stationary states, or under the influence of N-input exhaustion or oscillation, was analyzed in both pathway topologies. Our results indicate a metabolic control coefficient for GDH ranging from 0.94 in the linear pathway with GS regulation to 0.24 in the cyclic pathway without regulation, employing a default GDH concentration of 8 microM. Thus, in these conditions, GDH seemed to have a high degree of control in the linear pathway while having limited influence in the cyclic one. When GS was regulated, system responses to N-input perturbations were more sensitive, especially in the cyclic pathway. Furthermore, we found that effects of regulation against perturbations depended on the relative values of the glutamine and glutamate output first-order kinetic constants, which we named k(6) and k(7), respectively. Effects of regulation grew exponentially with a factor around 2, with linear increases of (k(7) - k(6)). These trends were sustained but with lower differences at higher GS concentration. Hence, GS regulation seemed important for metabolic stability in a changing environment, depending on the cell's metabolic status.
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PMID:Robustness in Escherichia coli glutamate and glutamine synthesis studied by a kinetic model. 1966 95

The aim of the article was to study the cellular adaptation of newborn extracted by repeated cesarean section (RCS). The study of functional activity of monocytes was conducted. The activity of succinate dehydrogenase (SDG) and glutamate dehydrogenase (GDG), acid phosphatase (AP) and myeloperoxidase (MPO) of 120 newborns, extracted by RCS was determined by means of cytochemical methods. Analyses were performed in the dynamics of the neonatal period on 1-3, 5-7, 28-30 days of life of the infants. It was found that neonatal exposure to PCB on the cell membrane and intracellular structures is accompanied by high activity of the lysosomal acid phosphatase marker and low activity of mitochondrial enzymes SDG and GDG. Reduced activity of MPO from the 1st day of life and the lack of normalization of this index on the 28-30 days of life shows the exhaustion of mechanisms that determine the margin of safety of adaptive responses.
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PMID:[Peculiarities of clinical and metabolic adaptation of newborns extracted by repeated cesarean section]. 2554 19