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)

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

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

Ability of mitochondria and submitochondrial particles (SMP) to generate a membrane potential on the addition of unpenetrating electron donors and acceptors and trimethylhydroquinone was used for specification of organization of the electron transfer chain. Ferri- and ferrocyanide added to mitochondria induce the membrane potential generation exchanging electrons only with cytochromes c or c1. Ferricyanide added to SMP induces the membrane potential taking electrons in three places: from NAD-H dehydrogenase, succinate dehydrogenase and in the presence of antimicyne A from cytochrome beta region. The difference of two sides of mitochondrial membrane is in agreement with the chemielectric hypothesis. According to this hypothesis protons from internal part of mitochondria are taken up to input H+-channel after electrons. That is why electrons come near the inner surface of the membrane and can be transferred from respiratory chain to water soluble acceptors. In output channels protons move under the action of intramembrane electrostatic field and in the direction of rising polarization of the medium. Protons are released to output channels while electrons are transferred to next carrier within the hydrophobic part of the membrane far from external surface of the membrane and cannot be transferred to water soluble acceptors.
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PMID:[Potential difference across the membrane of subcellular particles. IV. Study of the part of the respiratory chain from FAD to cytochrome c by the ion penetration technic]. 86 Dec 63

Ultrasonic treatment in vivo brought about distinct changes in liver mitochondria which developed in two directions as to oxygen consumption and oxidative phosphorylation. An increase of oxygen incorporation occurs with short term as well as with long-term experiences. The ratio P/O which expresses the step of oxidative phosphorylation decreases to 1 in the course of one hour after ultrasonic treatment. The results obtained and the supposition that they are related to modifications of NAD-coenzymes and flavoproteins, likewise of the activity of succinic dehydrogenase, of NADH2-cytochrom-c-reductases and cytochrom-c-oxidase, lead to the conclusion that ultrasonic energy is a factor intensifying the transfer of reduced equivalents in the shortened respiratory chain, a factor disturbing electron-proton transfer in the normal respiratory chain of NAD-coenzymes, and a releasing factor for two of the sites of coupling electron transfer with oxidative phosphorylation.
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PMID:[The influence of biophysical factors on biological oxidation and redox processes. 17. Changes in electron transfer and of oxidative phosphorylation steps in liver mitochondria after ultrasonic treatment (author's transl)]. 89 15

Two freshwater bacteria, a Pseudomonas sp. and a Spirillum sp., were grown in continuous culture under steady-state conditions in L-lactate-, succinate-, ammonium- or phosphate-limited media. In Pseudomonas sp., NAD-independent and NAD-dependent L-lactate dehydrogenases, aconitase, isocitrate dehydrogenase and glucose 6-phosphate dehydrogenase activities increased up to 10-fold as the dilution rate (D) was decreased from 0.5 to 0.02 h-1, regardless of whether the growth-limiting nutrient was carbon, ammonium or phosphate. In contrast, 2-oxoglutarate dehydrogenase and succinate dehydrogenase activities were not influenced by D, and NADH oxidase activity increased with D. Spirillum sp. gave different results in some respects, but it also exhibited an increase in the activity of several enzymes at low D values. Such increases may emanate from release of catabolite repression, and catabolite repressors for the five enzymes in Pseudomonas sp. showing such increases are probably compounds of carbon, nitrogen and phosphorus. It is likely that increased enzyme syntheses in low D cultures represent the normal physiological state for bacteria in aquatic environments where growth occurs slowly under nutrient limitations. Such increases probably permit a more effective utilization of nutrients present at sub-saturating concentrations.
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PMID:Influence of dilution rate on enzymes of intermediary metabolism in two freshwater bacteria grown in continuous culture. 95 May 55

The state-3 rate of respiration of potato tuber mitochondria is inhibited by concentrations of KCl or NaCl above 125 mM, and by concentrations of sucrose, lactose, or maltose above 500 mM, but not at all by mannitol, glucose, glycine, or proline up to a concentration of 1500 mM in the medium. Mitochondria from cauliflower, beetroot, cucumber, rock melon, and watermelon behave very similarly to those from potato tuber. The variable response to different solutes proves that the reduction in respiration is not a simple function of the chemical potential of water in the medium. Disruption of potato mitochondria by ultrasonic vibration does not relieve the inhibition of succinate oxidation caused by KCl or sucrose. However, treatment with detergent abolishes completely the inhibition of respiration by sucrose. Inhibition of succinate dehydrogenase [Succinate:PMS, oxidoreductase (EC.1.3.99.1)] and malate dehydrogenase [L-Malate:NAD oxidoreductase (EC.1.1.1.37)] activities by sucrose is less than the inhibition of succinate- and malate-dependent oxygen uptake by the potato mitochondria. Limited substrate uptake and, alternatively, reduced electron flow as a consequence of a direct effect of solute on the mitochondrial membrane are considered as possible mechanisms of inhibition.
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PMID:The response of plant mitochondria to media of high solute content. 97 40

Immunization of rabbits with increasing doses of Cl. botulinum toxoid, type B, led to the development in the kidneys of a focal intracapillary productive glomerulonephritis, and also of productive endo- and perivasculites. Blood letting (in the amount of 1% of body weight) aggravated the morphological picture of the affection on account of supervention of the alternative and exudative components. At the same time blood letting led to reduction of the NAD-diaphorase, succinic dehydrogenase and glucose-6-phosphatase activity in the epithelium of the proximal portions of the nephrons.
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PMID:[Histological and histochemical changes in the kidneys of rabbits immunized with Cl. botulinum toxoid type B in combination with blood loss]. 100 41


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