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)

The effect of n-hexane, 2-hexanol, 5-hydroxy-2-hexanone, 2,5-hexanediol, methyl n-butyl ketone ( MnBK ) and 2,5-hexanedione (2,5-HD) has been studied in vitro on crystalline glyceraldehyde-3-phosphate dehydrogenase (GAPDH), DL-glyceraldehyde-3-phosphate: NAD oxidoreductase (phosphorylating) EC. 1.2.1.12 and phosphofructokinase (PFK) ATP: D-fructose-6-phosphate-1-phosphotransferase; EC. 2.7.1.11 and lactic dehydrogenase (LDH) L-lactate: NAD+ oxidoreductase, EC. 1.1.1.27. MnBK and 2,5-HD both inhibited GAPDH and PFK activities selectively. n-Hexane and 2-hexanol had no effect on GAPDH and PFK activities; 5-hydroxy-2-hexanone and 2,5-hexanediol exhibited a slight inhibitory effect on these enzymes. Neither metabolites of n-hexane have any effect on LDH activity. 2,5-Hexanedione did not inhibit transketolase (D-sedoheptulose-7-phosphate: D-glyceraldehyde-3-phosphate glycolaldehyde transferase, EC. 2.2.1.1) and succinate dehydrogenase (succinate: 2,6-dichlorophenol-indophenol oxidoreductase, EC. 1.3.99.1) activities. The levels of ATP were reduced in 2,5-HD-treated cat sciatic nerves and returned to normal levels by exposing the nerve to sodium pyruvate.
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PMID:In vitro effect of n-hexane and its metabolites on selected enzymes in glycolysis, pentose phosphate pathway and citric acid cycle. 623 75

We have previously found that the restoration of cartilage matrical proteoglycans is preceded by markedly increased activity of uridine diphosphoglucose dehydrogenase (UDPGD), an enzyme directly associated with glycosaminoglycan (GAG) synthesis, and by increased activity of enzymes of the major energy yielding pathways (glucose-6-phosphate dehydrogenase (G6PD), glyceraldehyde-3-phosphate dehydrogenase (GAPD) and succinate dehydrogenase (SDH)). We did not find an increase in lactate dehydrogenase (LDH). In the present longitudinal study of rabbits (from 5 weeks to 42 months of age), we looked for age related changes in the activity of these enzymes in auricular chondrocytes, as well as for collagen and GAG content. Collagen content (micrograms/wet weight) increased up to 12 months and remained stable; total GAG content (micrograms/wet weight) reached its maximal value at growth and then declined gradually, reducing the GAG/collagen ratio dramatically from 36 to 8. At any age LDH was two to three times more active than either G6PD, aldolase, or GAPD. SDH and UDPGD activities were even lower. The age related changes varied: (1) LDH and GAPD were stable and did not change with either growing or aging; (2) G6PD and aldolase reached their maximal activity at 3-9 months, followed by a sharp drop at 12 months. G6PD remained stable, while aldolase continued to decline, although more slowly; (3) Maximal activity of SDH and UDPGD was measured at 5 weeks. Thus, the changes in enzyme activity in chondrocytes with age were specific for each enzyme. The significant decline in G6PD, aldolase, the rate-limiting enzymes of the pentose shunt and classic glycolysis, and SDH markedly reduced the ability of chondrocytes to generate energy.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Differential decline of rabbit chondrocytic dehydrogenases with age. 778 68

We previously found that intermittent hyperbaric oxygen exposure increases metabolic enzyme activity in soleus muscle. Since the metabolic enzyme activities of the heart and diaphragm of healthy animals are difficult to alter, we questioned whether intermittent hyperbaric oxygenation would provide a stimulus sufficient to increase metabolic enzyme activity. Therefore, we exposed 36 rabbits (4 groups of 9) twice daily for 90 min 5 days/wk to either 100% O2 at 243 kPa, 8.5% O2, and 91.5% N2 at 243 kPa, 100% O2 at 101 kPa, or 21% O2 at 101 kPa. After 4 wk of treatment, the activities of citrate synthase, succinate dehydrogenase, alpha-glycerophosphate dehydrogenase, phosphofructokinase, and glyceraldehyde-3-phosphate dehydrogenase were measured. In both the heart and the diaphragm, none of the treatments significantly altered the mean enzyme activities for any of the enzymes measured. Therefore, it seems that the hyperbaric oxygenation treatment protocols used do not induce an increase in metabolic enzyme activity in the heart and diaphragm in healthy animals.
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PMID:Hyperbaric oxygenation treatments and metabolic enzymes in the heart and diaphragm. 806 60

It has been proposed that highly biosynthetic cells oxidize fatty acids to generate ATP while maintaining high levels of glucose metabolism through the glycolytic and pentose shunt systems to supply biosynthetic intermediates. We investigated the metabolic strategies and substrate for ATP production in the osteoclast. We used in situ quantitative microcytophotometric techniques to determine the maximal activity of the pentose shunt (glucose-6-phosphate dehydrogenase; G6PD), the glycolytic pathway (glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase; G3PD and LDH), fatty acid oxidation (beta-hydroxyacyl dehydrogenase; HOAD), and the Krebs cycle (succinate dehydrogenase; SDH) in human osteoclasts in situ, and related these enzyme activities to the degree of involvement of the cells in resorption. Unlike other highly biosynthetic cells, such as chondrocytes and macrophage polykaryons, osteoclasts associated with bone resorption were deficient in G3PD, LDH, and G6PD activity. However, osteoclasts did demonstrate a capacity for fatty acid oxidation which increased in cells apposed to the bone surface. The lack of significant glycolytic and pentose shunt activity in the osteoclast provides good evidence that resorbing osteoclasts, unlike phagocytosing macrophage polykaryons, have the metabolic characteristics of cells with greatly reduced capabilities of de novo mRNA synthesis but which do maintain high rates of ATP production. The possibility that the loss of glycolytic activity is a prelude to cell death is discussed.
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PMID:Microcytophotometric analysis of human osteoclast metabolism: lack of activity in certain oxidative pathways indicates inability to sustain biosynthesis during resorption. 815 31

The lipophilic iron chelator 1,10-phenanthroline has been used in mechanistic studies on intracellular oxidant damage because iron is assumed to play a role in the endogenous formation of highly reactive oxygen species. This study shows that 1,10-phenanthroline has enzyme-modulatory properties in addition to its antioxidant activity. In rat hepatocytes, 1,10-phenanthroline caused inhibition of respiration and enhancement of cellular ATP content, pyruvate release and CO2 formation from glycerol resulting from a modulatory action of 1,10-phenanthroline on various enzymes involved in cellular energy metabolism. In intact mitochondria and in submitochondrial particles, oxygen consumption, complex I activity, and ATPase degradation are inhibited by 1,10-phenanthroline. In submitochondrial particles, complex II activity can also be suppressed by 1,10-phenanthroline. The purified cytosolic enzymes lactate dehydrogenase and glycerol-3-phosphate dehydrogenase are inhibited while purified glyceraldehyde-3-phosphate dehydrogenase is activated by 1,10-phenanthroline. The results suggest that 1,10-phenanthroline modulates various enzyme activities linked to cellular energy metabolism and that this property must be taken into account when using 1,10-phenanthroline as a tool in experiments on oxidant effects in cells.
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PMID:Ortho-phenanthroline modulates enzymes of cellular energy metabolism. 865 62

In rat hepatocytes exposed to [2-13C]pyruvate, newly formed glucose was more efficiently labeled in the carbon C5 than C2, as well as in the carbon C6 than C1, suggesting enzyme-to-enzyme channeling of D-glyceraldehyde 3-phosphate between glyceraldehyde-3-phosphate dehydrogenase and phosphofructoaldolase. Likewise the C1/C2 and C6/C5 ratios for 13C abundance in newly formed glucose, which largely exceeded the C3/C2 ratio of lactate or alanine and could reflect reversibility in the fumarase reaction, were compatible with the enzyme-to-enzyme tunneling of symmetrical Krebs cycle intermediates in the sequence of reactions catalyzed by succinyl-CoA synthetase, succinate dehydrogenase, and fumarase. This study further indicates that the major fraction of pyruvate is metabolized via pyruvate carboxylase rather than pyruvate dehydrogenase.
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PMID:D-glucose generation from [2-13C]pyruvate in rat hepatocytes: implications in terms of enzyme-to-enzyme channelling. 880 44

The etiology of the selective neuronal death that occurs in Huntington's disease (HD) is unknown. Several lines of evidence implicate the involvement of energetic defects and oxidative damage in the disease process, including a recent study that demonstrated an interaction between huntingtin protein and the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Using spectrophotometric assays in postmortem brain tissue, we found evidence of impaired oxidative phosphorylation enzyme activities restricted to the basal ganglia in HD brain, while enzyme activities were unaltered in three regions relatively spared by HD pathology (frontal cortex, parietal cortex, and cerebellum). Citrate synthase-corrected complex II-III activity was markedly reduced in both HD caudate (-29%) and putamen (-67%), and complex IV activity was reduced in HD putamen (-62%). Complex I and GAPDH activities were unaltered in all regions examined. We also measured levels of the oxidative damage product 8-hydroxydeoxyguanosine (OH8dG) in nuclear DNA, and superoxide dismutase (SOD) activity. OH8dG levels were significantly increased in HD caudate. Cytosolic SOD activity was slightly reduced in HD parietal cortex and cerebellum, whereas particulate SOD activity was unaltered in these regions. These results further support a role for metabolic dysfunction and oxidative damage in the pathogenesis of HD.
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PMID:Oxidative damage and metabolic dysfunction in Huntington's disease: selective vulnerability of the basal ganglia. 915 27

A developmental block is induced by phosphate in rat embryos at the late two-cell stage. The present study was designed to examine the energy metabolism of rat two-cell blocked and non-blocked embryos. Enzyme activity was measured in individual embryos by histochemical techniques. The activities of malate dehydrogenase, isocitrate dehydrogenase, lactate dehydrogenase, pyruvate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, glutamate dehydrogenase, glucose-6-phosphate dehydrogenase, glucose-6-phosphatase, and phosphorylase did not differ among non-blocked and blocked embryos. However, the activity of succinate dehydrogenase was significantly decreased in blocked embryos compared with non-blocked embryos. In blocked embryos, cytochrome oxidase activity was distributed homogeneously, but was located at the perinuclear region in non-blocked embryos. Active mitochondrial organization was visualized using the fluorescent probe rhodamine 123 and laser scanning confocal microscopy. In both non-blocked and blocked embryos, mitochondria were distributed homogeneously. The concentration of H2O2 measured fluorometrically in embryos cultured without phosphate did not change significantly during the culture period, but decreased in embryos cultured with phosphate. The timing corresponded to the occurrence of the two-cell block. In summary, these results suggest that the developmental block in rat two-cell embryos is induced by disturbance of mitochondrial energy metabolism.
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PMID:Microscopic analysis of enzyme activity, mitochondrial distribution and hydrogen peroxide in two-cell rat embryos. 986 Nov 63

The hexosamine pathway has been implicated in the pathogenesis of diabetic complications. We determined first that hyperglycemia induced a decrease in glyceraldehyde-3-phosphate dehydrogenase activity in bovine aortic endothelial cells via increased production of mitochondrial superoxide and a concomitant 2.4-fold increase in hexosamine pathway activity. Both decreased glyceraldehyde-3-phosphate dehydrogenase activity and increased hexosamine pathway activity were prevented completely by an inhibitor of electron transport complex II (thenoyltrifluoroacetone), an uncoupler of oxidative phosphorylation (carbonyl cyanide m-chlorophenylhydrazone), a superoxide dismutase mimetic [manganese (III) tetrakis(4-benzoic acid) porphyrin], overexpression of either uncoupling protein 1 or manganese superoxide dismutase, and azaserine, an inhibitor of the rate-limiting enzyme in the hexosamine pathway (glutamine:fructose-6-phosphate amidotransferase). Immunoprecipitation of Sp1 followed by Western blotting with antibodies to O-linked GlcNAc, phosphoserine, and phosphothreonine showed that hyperglycemia increased GlcNAc by 1.7-fold, decreased phosphoserine by 80%, and decreased phosphothreonine by 70%. The same inhibitors prevented all these changes. Hyperglycemia increased expression from a transforming growth factor-beta(1) promoter luciferase reporter by 2-fold and increased expression from a (-740 to +44) plasminogen activator inhibitor-1 promoter luciferase reporter gene by nearly 3-fold. Inhibition of mitochondrial superoxide production or the glucosamine pathway prevented all these changes. Hyperglycemia increased expression from an 85-bp truncated plasminogen activator inhibitor-1 (PAI-1) promoter luciferase reporter containing two Sp1 sites in a similar fashion (3.8-fold). In contrast, hyperglycemia had no effect when the two Sp1 sites were mutated. Thus, hyperglycemia-induced mitochondrial superoxide overproduction increases hexosamine synthesis and O-glycosylation of Sp1, which activates expression of genes that contribute to the pathogenesis of diabetic complications.
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PMID:Hyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation. 1105 Feb 44

There is spontaneous cure of a large portion of Ascaris suum 4th-stage larvae (L4) from the jejunum of infected pigs between 14 and 21 days after inoculation (DAI). Those L4 that remain in the jejunum continue to develop while those that have moved to the ileum are eventually expelled from the intestines. Although increases in intestinal mucosal mast cells and changes in local host immunity are coincidental with spontaneous cure, the population of L4 that continue to develop in the jejunum may counteract host protective mechanisms by the differential production of factors related to parasitism. To this end, a cDNA library was constructed from L4 isolated from pig jejunum at 21 DAI, and 93% of 1920 original clones containing a single amplicon in the range 400-1500 bp were verified by gel electrophoresis and printed onto glass slides for microarray analysis. Fluorescent probes were prepared from total RNA isolated from: (1) 3rd stage-larvae from lung at 7 DAI, (L3); (2) L4 from jejunum at 14 DAI (L4-14-J); (3) L4 from jejunum at 21 DAI (L4-21-J); (4) L4 from ileum at 21 DAI (L4-21-I, and; (5) adults (L5). Cy3-labeled L3, L4-14-J, L4-21-I and L5 cDNA, and Cy5-labeled L4-21-J cDNA were simultaneously used to screen the printed arrays containing the L4-21-J-derived cDNA library. Several clones showed consistent differential gene expression over two separate experiments and were grouped into 3 distinct transcription patterns. The data showed that sequences from muscle actin and myosin, ribosomal protein L11, glyceraldehyde-3-phosphate dehydrogenase and the flavoprotein subunit of succinate dehydrogenase were highly expressed in L4-21-J, but not in L4-21-I; as were a collection of un-annotated genes derived from a worm body wall-hypodermis library, and a testes germinal zone tissue library. These results suggest that only actively developing A. suum L4 are destined to parasitize the host and successfully neutralize host protective responses.
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PMID:Ascaris suum: cDNA microarray analysis of 4th stage larvae (L4) during self-cure from the intestine. 1455 58


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