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 activities of adenine nucleotide translocase (ANT), Na+-K+-ATPase (EC 3.6.1.3) and Mg2+-ATPase (EC 3.6.1.3) together with mitochondrial marker enzymes, succinic dehydrogenase (EC 1.3.99.1) and glutamate dehydrogenase (EC 1.4.1.2), were measured in liver, kidney, brain and testis from normal and thyroidectomised rats. Na+-K+-ATPase decreased by approximately 50% in liver and kidney; ANT decreased only in liver (-40%) while the activity of ANT per gram kidney increased by 38%. The activity of Mg2+-ATPase closely correlated with the pattern of change of ANT. The hormonal and substrate regulation of ANT is discussed in relation to its role in the regulation of intracellular phosphate potential and compartmentation in liver and kidney.
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PMID:Adenine nucleotide translocase, Na+-K+-and Mg2+-ATPases and differential tissue response to hypothyroidism. 612 72

Lesions of CA 3 derived axons, comprising Schaffer's collaterals, were carried out in order to destroy their presumably glutamatergic nerve endings within CA 1. After a survival time of 20 days part of the stratum radiatum of CA 1 displayed statistically significant reduction of histochemically demonstrable glutamate dehydrogenase and succinate dehydrogenase activity by about 19 and 25 per cent, respectively, whereas alpha-glycerophosphate dehydrogenase was not affected. These findings are consistent with current biochemical and histochemical results on the relation between several glutamate producing enzymes and glutamatergic structures suggesting that glutamate dehydrogenase plays a major role in glutamate transmitter metabolism.
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PMID:Lesions of Schaffer's collaterals in the rat hippocampus affecting glutamate dehydrogenase and succinate dehydrogenase activity in the stratum radiatum of CA 1. A study with special reference to the glutamate transmitter metabolism. 614 78

Diurnal rhythms are demonstrated in five rat liver enzymes : argininosuccinate synthetase, ATP : citrate lyase, glutamate dehydrogenase, phosphoenolpyruvate carboxykinase, and succinate dehydrogenase. In a 12 : 12 h light-dark cycle, maxima of enzyme activities occur at the beginning of the dark phase in the case of phosphoenolpyruvate carboxykinase, at the end of the dark phase in ATP : citrate lyase, and in the middle of the dark phase in the other three enzymes. The diurnal increase of phosphoenolpyruvate carboxykinase is blocked by cycloheximide, cordycepin, alpha-amanitin, and 5-azacytidine. The maximum of ATP : citrate lyase is likewise suppressed at the levels of both translation and transcription, as shown by administration of cycloheximide and 5-azacytidine, respectively. Hence, these two enzymes appear to be regulated transcriptionally. The diurnal rise of argininosuccinate synthetase an glutamate dehydrogenase is also totally inhibited by cycloheximide, whereas cordycepin, alpha-amanitin, and 5-azacytidine are ineffective in the first phase of enzyme accumulation. In a later phase, however, alpha-amanitin and 5-azacytidine become inhibitory. The two enzymes therefore seem to be regulated sequentially by post-transcriptional and transcriptional mechanisms. The diurnal increase of succinate dehydrogenase is nearly insensitive to alpha-amanitin and 5-azacytidine; cycloheximide is only partially inhibitory and, in particular, almost ineffective during the late rise. Thus, the rhythm of this enzyme might be controlled mainly by an activation and, perhaps, by a transitory post-transcriptional mechanism.
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PMID:Different levels of gene realization in the diurnal control of rat liver enzymes. 617 90

The effects of zinc on the enzymes of hepatic mitochondria were investigated in rats that had been given zinc sulfate (10 mg Zn2+/100 g body wt) p.o. Administration of zinc caused a marked elevation of succinate dehydrogenase, glutamate dehydrogenase, cytochrome c oxidase and ATPase activities, whereas it did not cause significant changes in pyruvate carboxylase, malate dehydrogenase and isocitrate dehydrogenase activities. The effect of zinc as a function of time was greatest on succinate dehydrogenase. Zinc also produced a marked elevation of ATP concentration in the hepatic cytosol and a corresponding increase in ATPase activity in the hepatic mitochondria. Zinc content of the inner membrane of mitochondria was raised significantly by administration of zinc. The removal of zinc by washing in 10 mM EDTA caused a significant decrease of the increased succinate dehydrogenase activity caused by administration of zinc, while it did not lower ATPase activity. The addition of zinc in amounts of 10-10(3) ng Zn2+ per mg protein produced a significant increase in succinate dehydrogenase activity in the inner membrane of mitochondria, whereas ATPase activity was elevated significantly at 10(3)-10(4) ng Zn2+ per mg protein, indicating that zinc activated succinate dehydrogenase more sensitively than ATPase. The present investigation suggests that zinc taken up by hepatic mitochondria stimulates the electron transport system and oxidative phosphorylation and, as a result, increases the ATP concentration in the hepatic cytosol.
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PMID:Role of zinc as an activator of mitochondrial function in rat liver. 621 62

Oxygen and glucose consumption and lactate production of the peritoneal membrane and intra-abdominal adhesions were measured in rats after a single intra-peritoneal colloidal silica injection. Enzyme histochemical studies were made of lactate dehydrogenase, succinate dehydrogenase, NADH2-diaphorase, NADPH2-diaphorase, glucose-6-phosphate dehydrogenase, glutamate dehydrogenase, acid phosphatase, leucylaminopeptidase and alkaline phosphatase in the peritoneal membrane. Anaerobic glycolysis comprises 47% of the total glucose consumption in the the normal peritoneum. Glucose consumption and lactate production of the peritoneal membrane increased sharply in the early phase of silica-induced peritonitis and stayed at a high level for a week indicating an enhanced anerobic metabolism. Oxygen and aerobic glucose consumption increased more slowly than anaerobic glucose consumption and reached their maxima 1 week after silica injection, indicating that the rate of aerobic metabolism is also higher in chemical peritonitis than in the controls. On the other hand, glucose consumption and lactate production increased in a parallel fashion in adhesions and in the peritoneum in the early phase of peritonitis. However, the maximum and later levels were less in adhesions than in the peritoneum. In the enzyme histochemical study high activities of enzymes indicating anaerobic energy metabolism and metabolism via the pentose phosphate shunt were seen in cells of the peritoneal membrane during the early phase of peritonitis. No activity was identified in enzymes indicating aerobic energy metabolism and increased catabolism before the end of the first week.
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PMID:Energy metabolism of the peritoneal membrane in silica-induced peritonitis. A biochemical and enzyme histochemical study. 625 64

Enzyme histological changes have been studied in several optic projection areas after right optic nerve lesion in goldfish. An increase in acid phosphatase activity was found in the optic tectum, nucleus rotundus, nucleus geniculatus lateralis and area pretectalis between 2 and 15 days postoperatively. The enzymes glutamate dehydrogenase, lactate dehydrogenase, NADH tetrazolium reductase, cytochrome oxidase, succinate dehydrogenase and beta-hydroxybutyrate dehydrogenase showed a decrease in activity in all or some of these projection areas. No changes were found in acetylcholinesterase activity after optic nerve lesions. Three weeks postoperatively, all enzyme activities returned to the same level as on the normal side. The results are discussed in relation to possible neurotransmitters in goldfish optic terminals.
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PMID:Enzyme histochemical changes in some optic projection areas of the goldfish after optic nerve lesions. 626 19

The effects of gossypol, a polyphenolic compound isolated from the cotton plant upon six oxidoreductases from cultured epimastigotes of Typanosoma cruzi were studied. Gossypol was a powerful inhibitor of the alpha-hydroxyacid and malate dehydrogenases, NAD-linked enzymes, and of glutamate dehydrogenase, malic enzyme and glucose-6-phosphate dehydrogenase, NADP-dependent enzymes. The drug did not have an effect on succinate dehydrogenase, a flavoprotein. The Ki values with respect to substrate were 0.73, 0.3 and 3.5 microM for alpha-hydroxyacid, malate and glutamate dehydrogenases, respectively, and 1.1, 0.19 and 7.8 microM with respect to the coenzyme. Inhibition was noncompetitive with respect to substrate and uncompetitive in relation to the coenzyme.
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PMID:Inhibition by gossypol of oxidoreductases from Trypanosoma cruzi. 637 Feb 65

In porcine interareolar placental epithelia, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetylhexosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, acid phosphatase, alkaline phosphatase, nonspecific esterases, cytochrome oxidase, 5-nucleotidase, leucine aminopeptidase, adenosine triphosphatase, diaphorases (NADH, NADPH), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase (NAD, NADP), beta-hydroxybutyrate dehydrogenase, glycero-3-phosphate dehydrogenase, NAD-glycero-3-phosphate dehydrogenase, glutamate dehydrogenase (NAD, NADP), lactate dehydrogenase. The results show that most of the enzyme activities remained almost unchanged during the period of investigation. Only G-6-PDH and 6-PGDH activities increased within the uterine epithelium and nonspecific esterase activity within uterine as well as chorionic epithelia during the 2nd half of pregnancy. Within chorionic and uterine epithelia, hydrolases but not dehydrogenases demonstrated a higher activity at the bases of chorionic villi as compared to the apices and flanks of the latter. The action and influence of the demonstrated enzymes on metabolism, energy transfer, secretory, and resorptive activities of chorionic and uterine epithelia are discussed.
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PMID:[Enzyme histochemical studies of the swine placenta. Histoptics of enzymes in interareolar placental epithelia]. 643 35

In autopsied brain tissue from three cases with Leigh disease (subacute necrotizing encephalomyelitis, SNE) and controls, the activity of pyruvate dehydrogenase complex (PDHC) was determined under different conditions. It was found to be at the control level or increased, but not deficient. The activities of succinate dehydrogenase, fumarase, succinate cytochrome c reductase, cytochrome c oxidase, and glutamate dehydrogenase were measured as additional mitochondrial markers and showed no essential differences between SNE and control tissue. The metabolic defect in SNE remains unknown. According to the literature, the defect may be localized to the mitochondrial systems. However, the reported results indicate that it cannot be ascribed to PDHC function. Extensive biochemical studies are necessary for understanding of the pathogenesis in the fatal genetic metabolic disease.
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PMID:Pyruvate dehydrogenase activity is not deficient in the brain of three autopsied cases with Leigh disease (subacute necrotizing encephalomyelopathy, SNE). 643 63

NADH:ubiquinone reductase (complex I) of the mitochondrial inner membrane respiratory chain binds a number of mitochondrial matrix NAD-linked dehydrogenases. These include pyruvate dehydrogenase complex, alpha-ketoglutarate dehydrogenase complex, mitochondrial malate dehydrogenase, and beta-hydroxyacyl-CoA dehydrogenase. No binding was detected between complex I and cytosolic malate dehydrogenase, glutamate dehydrogenase, NAD-isocitrate dehydrogenase, lipoamide dehydrogenase, citrate synthase, or fumarase. The dehydrogenases that bound to complex I did not bind to a preparation of complex II and III, nor did they bind to liposomes. The binding of pyruvate dehydrogenase complex, alpha-ketoglutarate dehydrogenase complex, and mitochondrial malate dehydrogenase to complex I is a saturable process. Based upon the amount of binding observed in these in vitro studies, there is enough inner membrane present in the mitochondria to bind the dehydrogenases in the matrix space. The possible metabolic significance of these interactions is discussed.
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PMID:Complex I binds several mitochondrial NAD-coupled dehydrogenases. 643 16


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