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)

Transverse cryostat sections of skeletal muscle were fixed in a solution containing 1.5% glutaraldehyde and 1.5% sulfosalicylic acid and stained in a solution containing equal volumes of 3% hydrogen peroxide and 50% ethanol saturated with o-tolidine. Myoglobin in the sarcoplasm of muscle fibers was precipitated and stained blue. Applicability of this method to cryostat sections, without glutaraldehyde fixations prior to freezing, allowed the myoglobin content of individual muscle fibers to be correlated with other histochemical characteristics of the same fibers seen in serial sections. In the dark red bovine sternomandibularis muscle, fibers with weak adenosine triphosphatase (ATPase) and strong succinate dehydrogenase (SDH) activity always exhibited strong myoglobin staining. An equal degree of staining was found in many fibers with strong ATPase and intermediate to strong SDH activity. Fibers with strong ATPase and weak SDH activity were less strongly stained than the preceding types.
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PMID:A method for myoglobin in cryostat sections of muscle by precipitation with sulfosalicylic acid. 9 25

The effect of prolonged digoxin treatment (1 mg/kg day for 8 days) on the activity levels of some enzymes of energy metabolism (phosphofructokinase, lactate dehydrogenase, citrate synthase, succinate dehydrogenase) in rat myocardium was studied. In the control animals receiving the solvent mixture (glycerol:ethanol:water in 1:1:1) a transient decrease in the lactate dehydrogenase and citrate synthase activity levels was observed. In the hearts of digoxin treated rats the level of activity of phosphofructokinase was permanently lowered by the fourth day and the level of activity of citrate synthase permanently increased after the first day of treatment. A transient increase in the activity level of succinate dehydrogenase in the myocardium of digoxin treated animals was seen between days 1 and 6. In this study a permanent decrease in phosphofructokinase and an increase in citrate synthase activity levels in rat heart muscle was noted during prolonged digoxin treatment.
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PMID:Enzyme activities of myocardial energy metabolism during prolonged digoxin treatment in rats. 14 96

Yeast mutants deficient in the constitutive ADHI (adc 1) were used for the isolation of mutants with deficiencies of the intermediary carbon metabolism, and of mutants defective in carbon catabolite derepression. Mutants were recognized by their inability to grow on YEP-glycerol and/or on ethanol synthetic complete medium. They were either defective in isocitrate lyase (ic11), succinate dehydrogenase (sdh1), or malate dehydrogenase (mdh1, mdh2), mdh-mutants could not uniformely be appointed to one of the known MDH isozymes. Homozygous mdh and sdh1 diploids are unable to sporulate. Three gene loci could be identified by mutants pleiotropically defective in many or all of the enzymes tested In ccr 1 mutants, derepression of isocitrate lyase, fructose-1,6-diphosphatase, ADHII and possibly of the cytoplasmic MDH is prevented, whereas the mitochondrial TCA-cycle enzymes, succinate dehydrogenase and malate dehydrogenase, are not significantly affected. CCR2 and CCR3 have quite similar action spectra. Both genes are obviously necessary for derepression of all enzymes tested. It could be shown that ccr1, ccr2 and ccr3 mutants are not respiratory deficient.
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PMID:Isolation and characterization of yeast mutants defective in intermediary carbon metabolism and in carbon catabolite derepression. 19 91

The ESR spectra of beef heart submitochondrial particles were measured in the same samples at 240 degrees and 12 degrees K. There is close similarity between the inhibitory action of alpha-thenoyltrifluoroacetone, ethanol and ferricyanide on the non-saturating free radical signal SQ-2 observed at 240 degree K and peak at g=1.99 (and 2.04) which is visible only at very low temperatures. This result strongly supports our previous proposal that both ESR signals are manifestations of the ubisemiquinone complex with the High-Potential Iron-Sulfur protein of succinate dehydrogenase.
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PMID:[Interaction of ubisemiquinone with the high-potential iron-sulfur center of submitochondrial particle succinate dehydrogenase. EPR study at 240 and 12 degrees K]. 19 22

The inhibition of succinate- and NADH-oxidase activities of submitochondrial particles by 4,7-diphenyl-1,10-phenantroline was studied. The inhibition was shown to increase when the particles were pretreated with SH-reagents. The treatment of submitochondrial particles with ethanol in the presence of 1,10-phenantroline resulted in a complete inactivation of succinate oxidase and succinate: tetramethyl-n-phenyldiamine reductase; the succinate PMS reductase activity was only partially inhibited after such treatment. It is concluded that tetramethyl-n-phenyldiamine and phenazine metasulfate react with different sites of the succinate dehydrogenase complex. The changes in the properties of submitochondrial particles after ethanol--phenantroline treatment are apparently due to the effect of non-polar solvent rather than to the extraction of non-haem iron.
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PMID:[Inhibition of succinate and NADH oxidases of submitochondrial particles by iron chelators and sulfhydryl reagents]. 45 13

The object of the study was the liver of newborn rats. Specimens were taken from the 2nd to the 8th hour after birth. Tissue material was obtained from control animals and the newborns whose mothers had been ethanol fed throughout gestation period. 40% ethanol was administered in doses of 8.0 g/kg weight, by gastric tube. In the newborn liver ethanol ingestion had led to significant accumulation of lipids, a strong acid phosphatase reaction and to a drop in succinic dehydrogenase activity. Histochemically, the intensity of alcohol dehydrogenase activity did not show any difference when the ethanol treated newborn liver was compared with controls. Ultrastructurally, the changes in the liver cells were expressed by a disappearance of the rough endoplasmic reticulum elements. Mitochondria were often swollen and distorted.
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PMID:Ethanol toxic effect on the newborn rat liver.--Histochemical and electronmicroscopical investigations. 74 9

The metabolism of Brettanomyces bruxellensis was investigated to determine the metabolic block responsible for the accumulation of acetate seen in cultures of this yeast. In glucose-grown cultures the major non-volatile intracellular organic acide was succinic acid. These cultures also had low levels of succinic dehydrogenase (succinate dehydrogenase, EC 1.3.99.1) and did not produce CO2 from the carbons of ethanol. It was concluded that a block in the oxidation of ethanol occurred at the level of succinic dehydrogenase. If glucose-grown cultures were transferred to ethanol medium, the block in the metabolism of ethanol was partially overcome; the level of succinic dehydrogenase increased, the concentration of the intracellular succinate decreased, and CO2 could be produced from C-1 of ethanol.
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PMID:The accumulation of succinate by the yeast Brettanomyces bruxellensis. 126 May 28

1. The hepatotoxic effects of heroin and methadone, and the effect of ethanol on opioid-induced hepatotoxicity, have been investigated in human cultured hepatocytes. Hepatocytes pretreated with 50 and 100 mM ethanol were exposed to increasing concentrations of heroin and methadone. 2. Cytotoxicity was evaluated by measuring leakage of intracellular lactate dehydrogenase, and by assessment of hepatocyte mitochondrial succinate dehydrogenase. The half-maximal cytotoxic concentration of heroin for human hepatocytes (TC50) was decreased by 70-55% by pre-exposure to 50 mM ethanol, and that for methadone was decreased by 60-40%. 3. Metabolic functions of human hepatocytes were significantly impaired at concentrations of opioids that had shown little cytotoxicity. Ethanol potentiated opioid-induced hepatotoxicity; concentrations of heroin and methadone that had little or no effect on hepatocyte metabolism in the absence of ethanol caused a significant decrease in urea synthesis rate, metabolism of glycogen and depletion of the intracellular GSH pool after ethanol pretreatment. 4. The increase in toxicity of heroin and methadone produced by ethanol is concomitant with a 40% increase in cytochrome P-450 levels of the pretreated hepatocytes.
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PMID:Potentiation of heroin and methadone hepatotoxicity by ethanol: an in vitro study using cultured human hepatocytes. 152 68

In the liver mitochondrial fraction of the first generation offspring of alcoholized male rats, decreased activities of monoamine oxidase (MAO) types A and B, rotenone-insensitive NADH-cytochrome c-reductase and succinate dehydrogenase were observed. The MAO-dependent inhibition of rotenone-insensitive NADH-cytochrome c-reductase and succinate dehydrogenase by biogenic amines, incubated with the mitochondrial fraction, was altered in the offspring of alcoholized animals as compared with control rats. The sensitivity of these enzymatic activities towards the inhibitory effect of 5-methoxyindol-3-ylacetaldehyde was markedly increased in the offspring of alcoholized male rats. The data obtained suggest the existence of a genetically determined predisposition of the mitochondrial metabolic processes in the offspring of the alcoholized rats to the effects of ethanol and to the toxic effects of acetaldehyde, formed during ethanol metabolism.
Alcohol Alcohol 1991
PMID:Studies on mitochondrial metabolic processes in offspring of alcoholized rats--I. Evidence for altered activity and sensitivity to monoamine oxidase-dependent control by biogenic amines of some membrane-bound enzymes. 180 36

Chronic ethanol consumption by baboons (50% of energy from a liquid diet) for 18 to 36 mo resulted in significant depletion of hepatic S-adenosyl-L-methionine concentration: 74.6 +/- 2.4 nmol/gm vs. 108.9 +/- 8.2 nmol/gm liver in controls (p less than 0.005). The depletion was corrected with S-adenosyl-L-methionine (0.4 mg/kcal) administration (102.1 +/- 15.4 nmol/gm after S-adenosyl-L-methionine-ethanol, with 121.4 +/- 11.9 nmol/gm in controls). Ethanol also induced a depletion of glutathione (2.63 +/- 0.13 mumol/gm after ethanol vs. 4.87 +/- 0.36 mumol/gm in controls) that was attenuated by S-adenosyl-L-methionine (3.89 +/- 0.51 mumol/gm in S-adenosyl-L-methionine-methanol vs. 5.22 +/- 0.53 mumol/gm in S-adenosyl-L-methionine controls). There was a significant correlation between hepatic S-adenosyl-L-methionine and glutathione level (r = 0.497; p less than 0.01). After the baboons received ethanol, we observed the expected increase in circulating levels of the mitochondrial enzyme glutamic dehydrogenase: 95.1 +/- 21.4 IU/L vs. 13.4 +/- 1.8 IU/L; p less than 0.001, whereas in a corresponding group of animals given S-adenosyl-L-methionine with ethanol, the values were only 30.3 +/- 7.1 IU/L (vs. 9.6 +/- 0.7 IU/L in the S-adenosyl-L-methionine controls). This attenuation by S-adenosyl-L-methionine of the ethanol-induced increase in plasma glutamic dehydrogenase (p less than 0.005) was associated with a decrease in the number of giant mitochondria (assessed in percutaneous liver biopsy specimens), with a corresponding change in the activity of succinate dehydrogenase, a mitochondrial marker enzyme.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:S-adenosyl-L-methionine attenuates alcohol-induced liver injury in the baboon. 230 95


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