Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.3.3.1 (citrate synthase)
 4,488 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We investigated whether X-irradiation could induce the enzyme superoxide dismutase (SOD) in intestinal muscle. Groups of rats received abdominal irradiation and the time course and dose response for SOD activity determined. Jejunal smooth muscle homogenates were analyzed for the activities of copper/zinc (CuZn) and manganese (Mn) SOD activity and for a mitochondrial marker enzyme, citrate synthase. A progressive rise in Mn SOD activity occurred at 20, 46, and 72 h after 1500 R. No significant changes in Cu-Zn SOD activity occurred at any time after 1500 R. At 20 h after 250 R of X-irradiation, Mn SOD activity increased but no further increase occurred at higher irradiation exposures. At the same time, CuZn SOD activity at 20 h after irradiation was greater than controls only at an exposure of 1000 R (p less than 0.05). Using Western blotting, we were able to clearly demonstrate an increase in immunoreactive Mn SOD protein in muscle samples 20 h after 1500 R. The rise in Mn SOD is not simply due to increase in mitochondrial numbers or increase in all mitochondrial enzyme activities because activity of the mitochondrial marker enzyme citrate synthase was decreased after X-irradiation. Transmission electron microscopic studies demonstrated damage to mitochondria after a dose of 3000 R. The data yield evidence that free radicals play a role in irradiation-induced intestinal smooth muscle injury.
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PMID:Irradiation increases superoxide dismutase in rat intestinal smooth muscle. 274 76

Local X-irradiation of mouse heart caused a large increase in manganese superoxide dismutase activity (MnSOD) in this organ but not in copper and zinc containing superoxide dismutase (Cu-Zn SOD) activity. MnSOD induction was both dose and time dependent. Another mitochondrial enzyme, citrate synthase, was not induced by X-irradiation. The amount of immunoreactive MnSOD also increased after X-irradiation, showing that the amount of MnSOD protein increased after X-irradiation. The response to X-irradiation was found to be biphasic--with one large peak and one smaller peak of manganese superoxide dismutase activity. The effect of various inhibitors of cellular activities on these two peaks of MnSOD activity was examined. Cycloheximide, a cytosolic protein synthesis inhibitor, abolished both peaks of MnSOD activity, while chloramphenicol, a mitochondrial protein synthesis inhibitor, has no effect on either peak. Actinomycin D, a RNA-synthesis inhibitor, lowered both peaks, but had more of an effect on the second peak than on the first. In vivo protein synthesis studies using [3H]arginine showed that an increase in new protein synthesis occurred during the time period of the second peak, but did not occur during the first peak. These results are consistent with the hypothesis that MnSOD induction occurs in two peaks with the first peak due to a preformed MnSOD protein or mRNA for MnSOD and the second peak due to an increase in new protein synthesis.
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PMID:Increase in manganese superoxide dismutase activity in the mouse heart after X-irradiation. 357 7

[14C]Acetyl-CoA was found to react spontaneously with dithiothreitol to give a relatively apolar product which was readily extractable into a butanol-toluene scintillant. This technique was used in rapid, reproducible assay for rat brain ATP:citrate lyase using [1,5-14C]citrate as substrate. The tissue extract, a 14,000 g supernatant, exhibited a lyase activity of approximately 7 nmol acetyl-CoA produced/min per mg supernatant protein, and was inhibited greater than or equal to 79% by alpha-ketoglutaric acid (10 mM), Cu2+ (1 mM) and Zn2+ (1 mM). [14C]Oxaloacetate, [14C]malate and endogenous citrate synthase were found not to interfere significantly with lyase estimations, but NADH was required in the reaction mixture to inhibit acetyl-CoA hydrolase activity.
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PMID:The interaction of dithiothreitol and acetyl coenzyme A in a radiochemical assay for rat brain ATP:citrate oxaloacetate lyase. 725 96

Similarities in morphology between copper-deficient cartilage and abnormal cartilage associated with tibial dyschondroplasis (TD) led to studies dealing with copper metabolism and its possible relation to TD. Abnormal cartilage and copper deficient cartilage cells both oxidize significantly less glucose to CO2 and water when compared to normal epiphyseal and day-old hypertrophic cartilage cells. Plasma ceruloplasmin levels and cartilage copper content were not different between normal birds and those affected wth TD, which seemed to rule out a genetic defect in copper metabolism as being partly responsible for the abnormal cartilage occurrence. Mitochondrial marker enzyme activities were investigated, and abnormal cartilage showed a significant decrease in activity of both cytochrome oxidase and citrate synthase. The yield of mitochondria on a percent of total activity basis was quite low from both normal and abnormal cartilages, and, thus, an absolute conclusion with regard to mitochondrial impairment cannot be made at this time.
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PMID:Metabolism of abnormal cartilage cells associated with tibial dyschondroplasia. 741 92

Amyotrophic lateral sclerosis is a fatal paralytic disorder of unknown cause. Recent evidence implicated the role of free radicals in the death of motor neurons in this disease. To investigate this hypothesis further, we measured the activity of the main free radical scavenging enzymes copper/zinc superoxide dismutase, manganese superoxide dismutase, catalase, and glutathione peroxidase in postmortem brain samples from 9 patients with sporadic amyotrophic lateral sclerosis and from 9 control subjects. We examined samples from the precentral gyrus of the cerebral cortex, a region affected in amyotrophic lateral sclerosis, and from the cerebellar cortex, a region not affected. The two groups did not differ in age or postmortem delay. In the precentral gyrus from amyotrophic lateral sclerosis samples, glutathione peroxidase activity as measured by spectrophotometric assay (13.8 +/- 2.6 nmol/min/mg protein [mean +/- standard error of mean]) was reduced significantly compared to the activity in the precentral gyrus from control samples (22.7 +/- 0.5 nmol/min/mg protein). In contrast, glutathione peroxidase activity was not significantly altered in the cerebellar cortex from amyotrophic lateral sclerosis patients compared to controls. Copper/zinc superoxide dismutase, manganese superoxide dismutase (corrected or not corrected for citrate synthase), and catalase were not significantly altered in the precentral gyrus or cerebellar cortex in the patient samples. This study indicated that glutathione peroxidase activity is reduced in a brain region affected in amyotrophic lateral sclerosis, thus suggesting that free radicals may be implicated in the pathogenesis of the disease.
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PMID:Brain superoxide dismutase, catalase, and glutathione peroxidase activities in amyotrophic lateral sclerosis. 896 46

The biological effects of the HIV-1 accessory protein, Vpr, have been studied in yeast expression systems. In our previous study [1], employing the pCUP1-vpr copper-inducible expression cassette, Vpr was shown to cause growth arrest and structural defects. In this study yeast constitutively expressing vpr, through elevated copy number and/or elevated transcription levels, displayed no growth arrest in fermentative growth conditions while Vpr was produced at much lower levels than in the inducible expression system. However, such cells were respiratory deficient and unable to utilise ethanol or glycerol as the sole carbon source. They exhibited gross mitochondrial dysfunction displayed in the loss of respiratory chain complex I, II, III, IV and citrate synthase activities. The effects on mitochondria required a C-terminal domain of Vpr that contains a conserved amino acid sequence motif HFRIGCRHSRIG. These results suggest that the widely observed phenomenon of 'Vpr-induced growth arrest' in human cells could be due to mitochondrial dysfunction.
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PMID:HIV-1 protein Vpr causes gross mitochondrial dysfunction in the yeast Saccharomyces cerevisiae. 923 18

Enzymes from extreme halophiles have potential as catalysts in biotransformations. We have developed methods for the expression in Escherichia coli and purification of two enzymes from Haloferax volcanii: dihydrolipoamide dehydrogenase and citrate synthase. Both enzymes were expressed in E. coli using the cytoplasmic expression vectors, pET3a and pET3d. Citrate synthase was soluble and inactive, whereas dihydrolipoamide dehydrogenase was expressed as inclusion bodies. Citrate synthase was reactivated following overnight incubation in 2 M KCl, and dihydrolipoamide dehydrogenase was refolded by solubilisation in 8 M urea followed by dilution into a buffer containing 2 M KCl, 10 microM FAD, 1 mM NAD, and 0.3 mM GSSG/3 mM GSH. Maximal activity was obtained after 3 days incubation at 4 degrees C. Purification of the two active enzymes was carried out using high-resolution methods. Dihydrolipoamide dehydrogenase was purified using copper-based metal ion affinity chromatography in the presence of 2 M KCl. Citrate synthase was recovered using dye-affinity chromatography in the presence of salt. A high yield of active enzyme was obtained in both cases. Following purification, characterisation of both recombinant proteins showed that their kinetics and salt-dependence were comparable to those of the native enzymes. Expression of active protein was attempted both by growth of E. coli in the presence of salt and betaine, and also by using periplasmic expression vectors in combination with a high salt growth media. Neither strategy was successful.
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PMID:Expression, reactivation, and purification of enzymes from Haloferax volcanii in Escherichia coli. 1039 37

Copper and cadmium inhibited the growth as well as citric acid production (depending on the heavy metal concentrations) by citric-acid-producing Aspergillus niger. Activity of citrate synthase was connected with citrate synthesis in the absence as well as in the presence of heavy metals. The activity of aconitase, and both NAD- and NADP-isocitrate dehydrogenases was strongly inhibited by copper. The contents of DNA and proteins in the cells decreased but the contents of lipids and polysaccharides increased considerably in the presence of both heavy metals.
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PMID:Effect of cadmium and copper on the production of citric acid by Aspergillus niger. 1134 55

Eighteen lakes studied near Sudbury and across Northeastern Ontario (Canada) over a five-year period provided a wide contamination gradient of cadmium (Cd), copper (Cu) and other metals such as nickel (Ni) and zinc (Zn). All were inhabited by yellow perch (Perca flavescens), which was sometimes the only species present. Liver Cd and Cu concentrations were monitored in these lakes, in some cases for several consecutive years and for multiple seasons. This data suggests that yellow perch from clean to mildly-contaminated environments loosely control their hepatic Cu concentrations between 7 and 50 microg g dry weight(-1), and a threshold of 50 microg g dry weight(-1) is suggested as the normal range of homeostatic control. Similar data collected by others support this value. Liver Cd concentrations appeared more variable among lake samples, but consistently remained below 10 microg g dry weight(-1) in clean to mildly-contaminated lakes, also supported by data collected elsewhere. Condition factors allowed the discrimination between clean and polluted yellow perch, a conclusion consistent with data for the same species collected in the Rouyn-Noranda area (Quebec, Canada). Values of weight-to-length scaling coefficient lower than 3.0 also discriminated between clean and metal-polluted yellow perch. Finally, three studies indicated that chronic metal exposure can lead to an impairment of aerobic capacities in wild yellow perch, as indicated by lower muscle activity of citrate synthase (CS), aerobic swim performance and respiration rate. We propose that the combination of liver metal concentrations, scaling coefficient, condition factor and an indicator of physiological impairment such as muscle CS activity can provide a suitable range of parameters to adequately assess the effects of metal contamination on the health of yellow perch. Although yellow perch are ubiquitous in North America, this approach can potentially be applied to other small fish species more suitable to other study areas.
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PMID:Morphometric and metabolic indicators of metal stress in wild yellow perch (Perca flavescens) from Sudbury, Ontario: a review. 1272 57

Activities of several metabolic enzymes show distinct patterns of zonation along the intestinal tract of tilapia (Oreochromis niloticus), rainbow trout (Oncorhynchus mykiss) and copper rockfish (Sebastes caurinus). Zonation is species and enzyme specific, with different metabolic activities concentrated in specific areas, and few generalizations can be made. The rockfish show the smallest degree of zonation, with highest activities in the third quarter of the intestine, and shallow gradients to either side, and a general upswing in activity towards the distal end. In the trout, mitochondrial enzyme activities (citrate synthase, glutamate dehydrogenase, malate dehydrogenase) are highest in the pyloric caeca and decrease along the length of the small intestine. This pattern is accentuated for malic enzyme and glucose 6-phosphate dehydrogenase. These enzymes drop precipitously in activity after the first few sections of the small intestine, while other NADP-linked dehydrogenases (isocitrate dehydrogenase, and 6-phosphogluconate dehydrogenase) show moderate activity in pyloric caeca and peak toward the distal section of the small intestine. In tilapia, glutamate dehydrogenase shows a similar decrease as in trout, but citrate synthase peaks towards the distal sections. NADP-dependent dehydrogenases reveal distinct patterns, peaking in different sections of the intestine-malic enzyme in the proximal midsection, glucose 6-phosphate dehydrogenase in the distal mid-section, and isocitrate dehydrogenase in the anal section. Enzyme activities in the stomach of trout and tilapia also show zonation, with the midsection generally displaying the highest activities. A 5-day treatment of tilapia with an intraperitoneal cortisol deposit (25 mg kg(-1) wet mass) drastically alters metabolic performance along the gut in enzyme specific patterns, generally increasing enzyme activities in site-specific arrangements. Cortisol treatment also leads to the expected increases in activities of phosphoenolpyruvate carboxykinase, pyruvate kinase and aspartate aminotransferase in liver, but not in kidney. Aspartate aminotransferase is the only enzyme in brain significantly increased by cortisol treatment. Short-term food deprivation changes enzyme patterns, often resembling those observed after cortisol administration. We conclude that brain, liver and intestinal amino acid metabolism is an important target for cortisol action in fish and that metabolic zonation is a key factor to be reckoned with when analyzing physiological phenomena in the fish intestine.
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PMID:Metabolic zonation in teleost gastrointestinal tract. Effects of fasting and cortisol in tilapia. 1278 63


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