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)

Subepicardial and subendocardial arteries and arterioles in both the left and right normal canine ventricle were examined histochemically to determine their metabolic profiles. Aerobic metabolic capacity was assessed by determining the reactivities of the enzymes cytochrome oxidase, succinate dehydrogenase and NAD-isocitrate dehydrogenase. Glucose-6-phosphate dehydrogenase was examined to assess activity of the hexose-monophosphate-shunt. The substrate glycogen was determined as an evaluation of anaerobic metabolic capacity, while the amounts of deoxyribonucleic and ribonucleic acid were assessed as an indication of protein synthesis. Results of the present investigation indicate that despite known hemodynamic differences, the metabolic profile of the coronary vasculature is similar in all regions of ventricular myocardium. Reactivities of the enzymes succinate and NAD-isocitrate dehydrogenase and cytochrome oxidase are greater in smooth muscle of arterioles than in arteries. This suggests that arteriolar smooth muscle has a higher capacity for aerobic metabolism than does arterial smooth muscle. The greater reactivity of glycogen in arterial, than in arteriolar smooth muscle, suggests that arterial muscle is more adapted for anaerobic metabolism. Deoxyribonucleic and ribonucleic acids demonstrate a low reactivity in both arteries and arterioles from all regions of ventricular myocardium which conforms to the opinion that under normal conditions, coronary vasculature is quite stable with little cell proliferation. Glucose-6-phosphate dehydrogenase shows little reactivity in all myocardial vessels with implies a low capacity for nucleic acid and protein synthesis.
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PMID:A histochemical study of the microvasculature in the left and right cardiac ventricles of the dog. 21 88

The segmentation of the proximal tubules in the kidney of the female rat was studied by means of enzyme histochemical reactions and the results compared with those observed in male and recently described by Jacobsen and J0rgensen (1973 a). Reactions were performed for the following soluble, coezyme-dependent oxido-reductases: glucose 6-phosphate dehydrogenase, alpha-glycerophosphate dehydrogenase, 3 alpha-hydroxysteroid dehydrogenase, NAD-as well as NADP-dependent isocitrate dehydrogenases, NAD-dependent malate dehydrogenase, NADP-dependent, decarboxylating malate dehydrogenase, uridine diphosphate glucose dehydrogenase. Measures were taken to reduce enzyme diffusion and eliminate interference from tissue tetrazolium reductases. Furthermore, reactions were performed for a number of less soluble or insoluble enzymes: glucose 6-phosphatase, mitochondrial alpha-glycerophosphate dehydrogenase, beta-hydroxybutyrate dehydrogenase, succinate dehydrogenase and tetrazolium reductases. In the proximal tubules of the female rat all enzymes studied--except beta-hydroxybutyrate dehydrogenase--showed segmental differences, most of them clearly revealing three segments. Sex differences were found concerning all enzymes except uridine diphosphate glucose dehydrogenase and NADP-dependent isocitrate dehydrogenase. The most pronounced sex-related differences were seen in the third segment in which part the male rat showed highest activity in respect to tetrazolium reductases, NAD-dependent isocitrate dehydrogenase, succinate dehydrogenase, beta-hydroxybutyrate dehydrogenase, 3 alpha-hydroxysteroid dehydrogenase and glucose 6-phosphate dehydrogenase and the female in respect to glucose 6-phosphatase, alpha-glycerophosphate dehydrogenases, and NADP-dependent, decarboxylating malate dehydrogenase. A few of the enzymes exhibited minor sex differences in the first two segments.
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PMID:Enzyme histochemical observations on the segmentation of the proximal tubules in the kidney of the female rat. 23 55

Oxidative enzymes in the rat testes have been studied after gamma irradiation. The role of these enzymes in relation to spermatogenesis and steroidogenesis after radiation injury to testis has been discussed. Loss of succinic dehydrogenase and sorbitol dehydrogenase reflects the losts of germ cell population. Malic enzyme and malic dehydrogenase seem to the related to the deficiency of steroid hormones, whereas increase in glucose-6-phosphate dehydrogenase and NADP isocitric dehydrogenase is due to secondary stimulation of pituitary.
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PMID:Radiation effects on rat testes. IX. Studies on oxidative enzymes after partial body gamma irradiation. 24 Nov 37

Cooling of rats down to the rectal temperature of 33--35 degrees without the use of narcotic and neuroplegic drugs did not cause distinct alterations in activity of the oxidative enzymes of tricarboxylic acid cycle--isocitrate dehydrogenase, alpha-ketoglutarate dehydrogenase, malate-, succinate- and pyruvate dehydrogenases in brain tissue. At the same time, inhibition of the activity of these dehydrogenases occurred in profound hypothermia (cooling to 19--20 degrees). In this case the activity of succinate dehydrogenase was decreased less distinctly as compared with the activity of NAD-dependent dehydrogenases. Succinic acid appears to be an especially important substrate for oxidation in brain of the chilled rats.
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PMID:[Activity of Krebs cycle oxidative enzymes in the brain in hypothermia]. 45 97

Mycotoxic porcine nephropathy was induced by p.o. administration of crystalline ochratoxin A for periods of 5 days, 3 months and 2 years. Enzyme activities of the renal tissue were studied histochemically. These were NADH-tetrazolium reductase, NADPH-tetrazolium reductase, lactate dehydrogenase, isocitrate dehydrogenase, succinate dehydrogenase, glucose-6-phosphate dehydrogenase, alpha-glycerophosphate dehydrogenase, unspecific acid phosphatase and unspecific alkaline phosphatase. The activity of NADH-tetrazolium reductase and succinate dehydrogenase was reduced in the proximal tubule of all nephrons after 5 days ochratoxin A exposure and remained reduced after 3 months and 2 years exposure. The effect of ochratoxin A on these enzymes would appear to cause the impairment of proximal tubular function and the morphological changes observed in the proximal tubule in ochratoxin A-induced mycotoxic porcine nephropathy. The localization of alterations in enzyme activity corresponds to the localization of ochratoxin A previously demonstrated in the kidney. The activities of NADPH-tetrazolium reductase, lactate dehydrogenase, glucose-6-phosphate dehydrogenase and unspecific alkaline phosphatase were reduced focally corresponding to the areas with focal tubular atrophy and the degree of reduction was roughly parallel to the degree of atrophy.
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PMID:Ochratoxin A-induced mycotoxic porcine nephropathy: alterations in enzyme activity in tubular cells. 47 26

Intraacinar distribution of succinate dehydrogenase (SDH), malate dehydrogenase (MDH), NADP-dependent isocitrate dehydrogenase (IDH), glutamate dehydrogenase (GluDH), lactate dehydrogenase (LDH) and NADH-tetrazolium dehydrogenase (TR) was studied in rat liver cryostat sections by multipositional microphotometric activity determinations. By statistical evaluation, activity of individual enzymes could be related to the acinar topography. Activity was evaluated with regard to distance of measuring position either from afferent (portal) or efferent (hepatic) vessels. Two independent distribution curves were obtained for each enzyme. Acinar distribution of all the enzymes studied followed sigmoid courses with maximal activity of SDH, MDH and LDH in zone 1 ("periportal") and GluDH, IDH, TR in zone 3 ("pericentral"). For all enzymes, maximum activity gradients were confined to zone 2 of the acinus. Data were also evaluated as ratios of activities in zone 1 and zone 3. The following ratios zone 1/zone 3 were obtained: SDH = 1.9, MDH = 1.7, IDH = 0.5, GluDH = 0.5, LDH = 1.3 and TR = 0.6.
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PMID:Microphotometric studies on intraacinar enzyme distribution in rat liver. 52 13

The specific activity of human platelet monoamine oxidase from control subjects undergoing glucose tolerance tests is reduced drastically. Three hours after intake of 100 g of glucose only 25%-30% of the MAO-baseline activity was measured with tryptamine. beta-phenylethylamine and p-tyramine as substrates. At about 5 hr, platelet MAO activity has increased again. Inhibition was not due to small molecular weight inhibitors or other diffusible factors. Studies of other platelet enzymes, including succinate dehydrogenase and isocitrate dehydrogenase (NADP+ dependent) showed no parallel reductions; hGH, insulin, blood glucose and platelet glycogen concentrations did not correlate with platelet MAO activity. The changes of MAO activity in respect with p-tyramine and tryptamine as substrates 24 hr after glucose ingestion suggest changes of the lipid microenvironment of this enzyme of the outer mitochondrial membrane.
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PMID:Factors altering platelet monoamine oxidase. The influence of oral glucose intake. 76 48

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

The specific activity of a peroxisomal enzyme, lactate oxidase, and of pyruvate kinase and lactate dehydrogenase, which are not peroxisomal, increased rapidly when shaken cultures of Tetrahymena were transferred to conditions of oxygen restriction and supplemented with glucose. Two other peroxisomal enzymes, catalase and TPN-linked isocitrate dehydrogenase, did not increase substantially, nor did succinate dehydrogenase. The increases were reduced if glucose was not added at the time of transfer, and were prevented by actinomycin D or cycloheximide, but not by chloramphenicol. The results suggest an involvement of peroxisomes in the metabolism of glycolytic endproducts when the availability of oxygen to the cell is limiting.
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PMID:Synthesis of glycolytic and peroxisomal enzymes in Tetrahymena following a change in culture conditions. 80 70

In the presented study the influence of freezing and freeze-drying on enzyme activity is described. Attention is paid to 16 enzymes which can be used for quantitative enzyme histochemical techniques. With the exception of succinate dehydrogenase only, no significant inactivation during freezing and freeze-drying procedures could be demonstrated with lactate dehydrogenase, malate dehydrogenase (NAD+), malate dehydrogenase (decarboxylating) (NADP+), isocitrate dehydrogenase (NADP+), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, NADH-oxydoreductase, mitochondrial glycerol-3-phosphate dehydrogenase, cytochrome c oxidase, phosphoglucomutase, glucosephosphate isomerase, glucose-6-phosphatase, acid phosphatase, beta-glucuronidase and non specific aryl esterase. Therefore, the results supply a sound foundation for those quantitative enzyme histochemical techniques in which tissue specimens are frozen or frozen-dried before enzyme estimations are performed.
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PMID:The influence of freezing and freeze-drying of tissue specimens on enzyme activity. 87 Apr 61


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