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:1.3.5.1 (succinate dehydrogenase)
8,177 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

NAD- and NADP-dependent dehydrogenases in gastric adenocarcinoma and undifferentiated cancer cells were studied comparatively. The activity of NADP-dependent malate dehydrogenase, glutamate dehydrogenase and glucose-6-phosphate dehydrogenase was found to be high in gastric adenocarcinoma, while there was noted a more high activity of succinate dehydrogenase and NAD-dependent malate dehydrogenase in undifferentiated cancer. Differences ni the activity of oxido-reductive enzymes in adrenocarcinoma and undifferentiated cancer are discussed from the standpoint of various histogenesis of these forms of gastric cancer.
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PMID:[Oxidoreductase activity in the cells of stomach cancer]. 48 98

Spinal ganlia of a 9-day chick embryo were cultivated by the method of "floating rafts" in common medium (control) and in the medium containing amizyl (100 microgram/ml) or a neuregrowth factor (50 microgram/ml). With the action of amizyl there proved to be an increase in the number of surviving neurons; the majority of these neurons contained monoaminoxidase; there was a rise of NAD-diaphorase activity, and, to a lesser extent, of lactic dehydrogenase and isocitric dehydrogenase activities. The neurogrowth factor caused an increase in the number of nerve cells with acetylcholinesterase; there was an elevation of NAD-diaphorase and some rise of malic dehydrogenase activities; the activity of lactic dehydrogenase became maximal; as to succinic dehydrogenase--its activity was somewhat suppressed.
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PMID:[Effect of nerve growth factor and amizil on the viability and metabolism of cultured spinal ganglia]. 56 23

Male albino rats were kept on copper-enriched diet for 2, 4, 6 and 8 weeks. Experiments were made to study the electron transported, oxidative phosphorylation and the activity of some respiratory enzymes (rotenone-insensitive NAD. H-cytochrome c-reductase, NAD. H-DCPIP-reductase, succinate-cytochrome c(DCPIP)-reductase and succinate dehydrogenase) depending on the duration of copper sulphate treatment and hepatic copper level. Copper content is found to rise as early as the 2nd week, after which it remains relatively constant. Oxygen consumption in State 3 decreases strongly during the 2nd week and remains low throughout the period studied. Oxygen consumption in State 4 also decreases in the 2nd week, after which it rises and reaches the values of the control animals. The enzyme activities studied are also strongly inhibited (32-57%) after a 14-day treatment, later they are recovered gradually, reaching 50-79% of the control values. The probable compensatory mechanism of copper metabolism in the liver and the participation of thiol groups in it are discussed.
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PMID:Effect of chronic copper loading on the functions of rat liver mitochondria. 61 29

A method of comparative microphotometry was applied to the study of the oxidative enzymes in the epithelial lining of the uterine cavity and the glandular epithelium of the ovariectomized rats during the climacteric disturbances. There was an increase in the activity of lactic dehydrogenase (LDH) and glucose-6-phosphoric dehydrogenase (G-6-PDH) and a fall of the succinic dehydrogenase (SDH) and NAD- and NADP-diaphorases activity in the cells of the epithelial lining the uterine cavity. The glandular epithelium displayed an elevation of the LDH activity and a sharp fall of the SDH, NAD- and NADP-disphorases activity. Administration of testosterone-propionate caused an marked elevation of the activity of the oxidative enzymes in the epithelium of the rat endometrium in comparison with level of their activity in control animals and rats given no hormone.
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PMID:[Microphotometric study of the activity of oxidative enzymes in the endometrial epithelium of rats following ovariectomy and administration of testosterone propionate]. 63 99

In a detailed study focused on the methodological problems in dehydrogenase histochemistry [e.g., fixation, diffusion of enzymes and of reduced inermediates, conversion of NADPH and NADP to NADH and NAD, respectively, penetration of tetrazolium salt and formazan substantivity, 'nothing dehydrogenase' reaction, use of exogenous CoQ10 and of flavoprotein substitute (PMS)], the distribution and activity of succinate dehydrogenase, NAD(P)H-tetrazolium reductase, glucose-6-phosphate dehydrogenase, lactate dehydrogenase (H and M types), and of L-glutamate dehydrogenase (E.C.1.4.1.2 and E.C.1.4.1.3) have been investigated in the rat cerebellum. It was evident from the study that reliable results could only be obtained if all the aforementioned factors had been considered. The image of actual concentration of SDH in the neuropil of the molecular layer could only be recorded by adding CoQ10, while other structures exhibited greater balance between SDH and endogenous mitochondrial CoQ. Contrary to previous studies, a reversed localization of the activity of G-6-PDH and LDH was noticed. The elements of molecular and Purkinje layers were rich in G-6-PDH, while the granular layer was nearly depleted. The actual level of LDH could only be recorded if NADH-tetrazolium reductase was bypassed with PMS. The H and M types of LDH coexisted in the three cortical layers, the H type being prevalent and the M type attaining its highest level in synaptic glomeruli followed by the structures of the molecular layer and the Purkinje cells. High activity of GDH was noticed in Bergmann glia followed by synaptic glomeruli, while most other structures showed weak to moderate activity. The two GDH types coexisted in all structures showing activity, except for Bergmann cells, which only showed presence of the E.C. 1.4.1.3 type. Furthermore, Bergmann glia was exceptional by showing no activity of SDH and LDH, but strong activity of G-6-PDH and NADPH-tetrazolium reductase. The granular cells were exceptional by showing weak or no activity of all enzymes in question.
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PMID:Methodological aspects of the histochemical localization and activity of some cerebellar dehydrogenases. 66 87

In the cells of RH, SPEV and HEp-2 lines irradiated with 6.5 mm radiowaves of 1 mW/cm2 flux density the following phenomena were established: activation of succinate dehydrogenase and ATPase; reduction of cytochrome oxidase, NAD- and NADP-diaphorase, acid and alkaline phosphatase activities; repression of 3H-thymidine incorporation in DNA and of 3H-uridine incorporation in RNA; violation of ultrastructure; suppression of cellular proliferation; decrease of mitotic activity; occurrence of pathological forms of mitosis.
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PMID:[Biological oxidation in cells exposed to microwaves in the millimeter range]. 68 31

The rabbits being repeatedly poisoned with small doses of sodium cyanide, the activity of succinic dehydrogenase in the tissues does not essentially change. The activity of NAD.H2-cytochrome-c-reductase and NAD.H2-diaphorase in the brain, myocardium and kidneys increases. Under histotoxic hypoxia the level of iron in the tissues increases by 52-93%, that of copper--by 28-36%, of zinc--by 21-74% and of cobalt by 28-40%. There existed a positive correlation between the content of iron and the activity of NAD-dependent enzymes. In nonlethal form of histotoxic hypoxia the content of nonhemin iron and the activity of NAD.H2-cytochrome-c-reductase in the mitochondria of the brain increases by 25% and 17%, respectively, and a direct correlation is revealed between them.
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PMID:[Iron, copper, zinc and cobalt content and activity of respiratory metalloenzymes in animal tissues under toxic hypoxia]. 68 69

1. In rat liver mitochondria in vitro, an activation of succinate dehydrogenase [succinate: (2,6-dichloroindophenol)oxido-reductase], an inner membrane enzyme, was induced by Ca2+ at extramitochondrial concentrations (about 1.3 micron) close to those estimated in the cytosol. 2. The activation required both substrate (succinate) and ATP, and occurred whether mitochondria were coupled (Ca2+ could be accumulated) or uncoupled (Ca2+ could not be accumulated) by classical uncouplers. 3. The activation by Ca2+ of the uncoupled mitochondria was accompanied by a modest but significant change in the mitochondrial morphology as judged from light scattering measurements and electron microscopy. 4. In the uncoupled mitochondria, oxaloacetate added externally diminished the activation by Ca2+. In addition, the amount of oxaloacetate produced endogenously from succinate via malate fell after Ca2+ and ATP addition. However, the extent of the fall in mitochondrial oxaloacetate did not correlate with the degree of activation of succinate dehydrogenase. 5. The activation by Ca2+ of the uncoupled mitochondria was accompanied by a reductive shift of pyridine nucleotide and coenzyme Q, and an oxidative shift of flavoproteins and cytochromes b, c, and a-a3. 6. In the situation where the Ca2+-induced activation of succinate dehydrogenase (and consequently succinate oxidation) took place in the uncoupled mitochondria, oxidations of 3-hydroxybutyrate and pyruvate were markedly suppressed. 7. From the above findings, it is concluded that Ca2+ action on the mitochondrial inner membrane activates mitochondrial succinate dehydrogenase, and this action produces an inhibition of electron transport between NAD and flavoprotein. In view of the location of these reactions in the inner membrane, a conformation change of the membrane is suggested as a common cause.
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PMID:Ca2+-induced activation of succinate dehydrogenase and the regulation of mitochondrial oxidative reactions. 76 52

The activities of twelve enzymes were measured in crude extracts from cells of Escherichia coli K-10 grown aerobically or anaerobically in a defined medium in the presence or absence of nitrate. The activities of isocitrate dehydrogenase, aconitate hydratase, 2-oxoglutarate dehydrogenase, malate dehydrogenase, malic enzyme, and D-lactate dehydrogenase (NAD+-independent) were found to be higher in cells grown in nitrate respiration than in those in fermentation, but lower than in those in respiration. This finding may explain the incomplete oxidation in nitrate respiration and, on the other hand, suggests the operation of the tricarboxylic acid even under these conditions. The activities of succinate dehydrogenase and alcohol dehydrogenase in relation to the formation of fermentation product were as high in cells grown in fermentation as in those in respiration and were low in those in nitrate respiration. However, that ratio of the activities in the latter case to the activities in respiration was the same as the ratio for most enzymes in the tricarboxylic acid cycle. The level of lactate dehydrogenase (NAD+-dependent) was not affected by nitrate respiration but its activity in the extract was inhibited by nitrate and nitrite. The absence of lactate in the anaerobic culture with nitrate may be due to this inhibition as well as NADH oxidation by nitrate. Levels of glucose-6-phosphate dehydrogenase and glutamate dehydrogenase were not altered by the growth conditions and that of pyruvate dehydrogenase was low only in cells grown in fermentation.
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PMID:Effect of nitrate reduction on the enzyme levels in carbon metabolism in Escherichia coli. 77 52

A sporadic case of central core disease in a 5 1/2-year-old girl is reported. Clinically, a retarded motor development existed, furthermore, a muscle weakness and hypotonia of the extremities and trunk, contractures of the hip- and knee-joint,and luxation of both hip-joints. Biopsy specimens are taken from both Mm. gastrocnemii. Muscle fibres show, by morphologic examination, 95 per cent cores, which are characteristic for this myopathy. A further abnormality is seen inthe histochemical preparations for phosphorylase, succinate dehydrogenase, NAD diaphorase tetrazolium reductase, myofibrillar ATPase as well as AS-reaction with and without diastase digestion. With these techniques the muscle fibres show an uniform reaction pattern in which the activities of the oxidative andglycolytic enzymes correspond to the type I fibres of healthy persons. The cores show a lack of a activity of the oxidative and glycolytic enzymes as well as are ATPase- and PAS-negative. By reason of this histochemical behaviour it is suggested that the cores are predominantly unstructured. The cause of this disease might be complex disturbances in the neuro-muscular system manifested in the fetal period.
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PMID:[A case of central core disease. Light microscopic and histochemical studies (author's transl)]. 84 74


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