Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.15.1.1 (superoxide dismutase)
 58,858 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

26 specimens of Presbytis entellus were examined for a variety of blood proteins. In contrast to previous studies of other species of leaf monkeys, our P.entellus sample proved to be very heterogeneous. Polymorphisms were found in the third component of complement, group-specific component, glycine-rich beta-glycoprotein, alpha1-antitrypsin, phosphoglucomutase, 6-phosphogluconate dehydrogenase, adenylate kinase, superoxide dismutase, malate dehydrogenase, and phosphohexose isomerase. Variable band strengths that might represent polymorphism were found in acid phosphatase and lactate dehydrogenase. Further analyses of the P. cristatus sample studied by Barnicot and Hewett-Emmett failed to disclose variation. The interpretation of blood protein variability in relation to sample collection and population structure is discussed.
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PMID:Protein polymorphism in the Hanuman langur (Presbytis entellus). 5 13

Biochemical studies were performed on blood and lung tissue of squirrel monkeys (Saimiri sciureus) following acute exposure to 0.75 ppm ozone (O3) for 4 h/d for 4 consecutive days. One group of animals was sacrificed at the end of the last exposure day and another group was sacrificed 4 d later after the last exposure. Evidence was sought for oxidation-induced changes known to occur in rodents when high levels of O3 are inhaled. A significant increase in red blood cell membrane fragility was observed, as well as significant decreases in red blood cell glutathione and erythrocyte acetylcholinesterase; however, the red blood cell enzymes, lactic acid dehydrogenase (LDH), and glucose-6-phosphate dehydrogenase (G6PDH) were not changed significantly. Lung tissue analysis showed that lipid peroxidation was markedly increased and tissue vitamin E levels were significantly decreased. The tissue enzymes G6PDH, glutathione reductase, and LDH significantly increased in activity. No significant changes were seen in either superoxide dismutase or malic acid dehydrogenase. The results of this experiment indicate that O3, or reaction products resulting from O3-tissue interaction in the lung, pass the air-blood barrier and are capable of producing biochemical changes in blood as well as in lung tissue.
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PMID:Biochemical response of squirrel monkeys to ozone. 10 43

1. Employing starch gel electrophoresis at pH 8.6, a single anodal band of L(+)-lactate dehydrogenase activity was found in skeletal muscle of Birgus latro. 2. Two anodal malate dehydrogenase isozymes were observed in heart, skeletal muscle and pericardial gland tissue. Lung and gill exhibited the faster moving band only. 3. Multiple bands of esterase activity were detected in all tissues examined employing alpha-naphthylacetate or alpha-butyrate as substrate. 4. Multiple molecular forms of superoxide dismutase were observed in all tissues examined. 5. Lung exhibited a single cathodal band of carbonic anhydrase activity.
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PMID:An electrophoretic analysis of selected enzymes of the coconut crab, Birgus latro. 31 28

The erythrocytes of 350 pigtailed macaques (Macaca nemestrina) were examined for electrophoretic variation of hemoglobin and 26 enzymes. Seven enzymes showed variation in more than 1% of individuals: phosphoglucose isomerase, phosphoglucomutase-1, soluble NADP-dependent isocitric dehydrogenase, peptidase A, peptidase C, 2,3-diphosphoglycerate mutase, and acid phosphatase. Variation with lesser frequency was found in soluble glutamic-oxalacetic transaminase, phosphoglycerate kinase, lactic dehydrogenase, and hemoglobin. Only eight samples were tested for esterase D, and one of these had a variant phenotype. Enzymes with no clear variation were adenylate kinase, adenosine deaminase, phosphofructokinase, hexokinase, pyruvate kinase, glyceraldehyde 3-phosphate dehydrogenase, aldolase, phosphoglycerate mutase, phosphopyruvate hydratase (enolase), phosphoglucomutase-3, and superoxide dismutase. There was father-to-son transmission of PGI, PGM-1, peptidase C, 6PGD, 2,3-DPGAM, NADP-ICD, and acid phosphatase variants, suggesting that these loci are autosomal as in man.
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PMID:Intraspecific red cell enzyme variation in the pigtailed macaque (Macaca nemestrina). 114 87

The effect of carboxyethylgermanium sesquioxide (Ge-132) on cultured neonatal rat myocytes and isoproterenol injured myocytes was studied. The results showed that Ge-132 (0.01 mmol.L-1 and 1 mmol.L-1) increased the incorporation of both [3H]-TdR and [14C]-UR, reduced the membrane lipid fluidity and inhibited the release of the cytoplasmic enzyme lactate dehydrogenase (LDH). Exposure of the myocytes to isoproterenol 0.5 mmol.L-1 for 6 hours resulted in 5-fold release of LDH compared with the control. All myocytes ceased beating. Ultrastructurally, severe sarcolemmal and mitochondrial damage was evident. When the cells were pretreated with Ge-132 before the addition of isoproterenol, the increased LDH release was inhibited significantly, and preservation of beat and ultrastructure of myocytes was observed. In addition, the activity of superoxide dismutase (SOD) was elevated by Ge-132. All the effects of Ge-132 were dose-related. The results indicate that Ge-132 may improve the metabolism of cultured neonatal rat myocytes and protect myocytes from isoproterenol-induced injury.
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PMID:[Effect of carboxyethylgermanium sesquioxide on cultured normal neonatal rat myocardial cells and cells injured by isoproterenol]. 127 37

Isolated pancreatic acini were incubated with either a combination of xanthine and xanthine oxidase which generates superoxide (O2), or hydrogen peroxide (H2O2), and the direct cytotoxic effect of active oxygen species on the pancreatic acini was examined in vitro in the isolated pancreatic acini system of the rat. Both amylase secretion and lactic dehydrogenase discharge were increased dose-dependently by the addition of xanthine and xanthine oxidase, and suppressed by the addition of a superoxide scavenger, superoxide dismutase. In addition, amylase and lectate dehydrogenase discharge was increased dose-dependently by hydrogen peroxide and decreased by catalase. These results suggest that superoxide and hydrogen peroxide directly injure pancreatic acinar cells and that active oxygen species are involved in the pathogenesis of acute pancreatitis.
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PMID:Toxic effects of oxygen-derived free radicals on rat pancreatic acini; an in vitro study. 128 95

The protective effects of cyproheptadine, an antiserotonin-antihistaminic agent with calcium channel blocker activity, on calcium paradox in isolated Langendorff's heart in rats were studied. After a 5 min of calcium-free perfusion [standard Krebs-Henseleit (K-H) buffer without calcium, gassed with 95% O2 and 5% CO2] followed by a 20 min of normal K-H buffer (Ca2+ 2.5 mmol/L) perfusion, extensive and rapid myocardial injury was observed: release of massive cellular enzymes such as lactic dehydrogenase (LDH) and creatine phosphokinase (CPK), significant decrease of myocardial anti-oxygen free radical enzymes such as superoxide dismutase (SOD) and glutathione peroxidase (GSH-Px) activities but no obvious change of myocardial lipid peroxides such as malondialdehyde (MDA) content was observed. The loss of normal colour and mechanical activity, even contracture, was also observed in the injured hearts. Cyproheptadine (2.5-5 mumol/L) was shown to effectively antagonize the damage. The results suggest that the protective effects of cyproheptadine on the calcium paradox may be related to its actions of blocking calcium channel, protecting anti-oxygen free radical enzymes and scavenging oxygen free radicals in the myocardial tissues.
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PMID:[Protective effects of cyproheptadine on calcium paradox in isolated rat hearts]. 130 23

Indapamide, a nonthiazide chlorosulfamoyl diuretic, which possesses well-known antihypertensive properties, is able to scavenge free radical intermediates involved in lipid peroxidation. In this respect, it has almost the same level of action as alpha-tocopherol. Using an isolated working rat heart preparation, we investigated the effect of indapamide on the myocardial resistance to global total normothermic ischemia followed by reperfusion. The heart, isolated at the end of chronic oral pretreatment (7 day at 3 mg/kg body weight/day), was submitted to ischemia for 15 min and then reperfused. The main results were as follows: in the indapamide-treated group, 1) postischemic recovery of cardiac function was significantly better as compared to the untreated control group; 2) lactate dehydrogenase (LDH) release measured after 15 min of reperfusion was significantly reduced; 3) the myocardial content of organic hydroperoxides (HPO), taken as an index of lipid peroxidation, was significantly lowered, whereas the activity of superoxide dismutase (SOD) and glutathione peroxidase (GPx) remained unchanged; and 4) electron spin resonance (ESR) analysis of coronary effluents, collected during the first minutes of reperfusion in the presence of the spin-trap 5,5-dimethyl-1-pyrroline N-oxide (DMPO), revealed a significant modification in the treated group. These findings suggest that indapamide treatment is able to afford some protective effect to cardiac tissue during the early stage of postischemic reperfusion, and that this effect might be related to the antioxidant properties of inadapamide.
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PMID:Beneficial effect of indapamide in experimental myocardial ischemia. 131 Jun 2

Reactive oxygen metabolites have been reported to be important in the pathogenesis of ischemia/reperfusion-induced and alcohol- and drug-induced liver injuries. We investigated the role of superoxide dismutase, cellular and extracellular, in preventing reactive oxygen metabolite-induced cytotoxicity in cultured rate hepatocytes. Cells were exposed to reactive oxygen metabolites enzymatically generated by hypoxanthine-xanthine oxidase. Cytotoxicity was quantified by measuring 51Cr release from prelabeled cells and lactate dehydrogenase release. Reactive oxygen metabolites caused dose-dependent cytotoxicity. Good correlation was found between the values for 51Cr and lactate dehydrogenase release. Reactive oxygen metabolite-induced cell damage was reduced by catalase but not by superoxide dismutase. Cellular superoxide dismutase and catalase activities were not increased after incubation with exogenous superoxide dismutase and catalase for up to 5 hr. Pretreatment with diethyldithiocarbamate inhibited cellular superoxide dismutase activity without inhibiting other antioxidants such as catalase, glutathione, glutathione reductase and glutathione peroxidase and sensitized cells to reactive oxygen metabolite-induced cytotoxicity. We conclude that hydrogen peroxide is an important mediator in hypoxanthine-xanthine oxidase-induced cell damage and that superoxide dismutase plays a critical role in cellular antioxidant defenses against hypoxanthine-xanthine oxidase-induced cytotoxicity in cultured rat hepatocytes in vitro.
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PMID:Role of cellular superoxide dismutase against reactive oxygen metabolite-induced cell damage in cultured rat hepatocytes. 131 53

The effect of age on the toxicity of diquat, a redox cycling compound, was investigated in hepatocytes isolated from mature (6 months) and old (24-29 months) male Fischer 344 rats. Hepatocytes of old rats were more sensitive than those of mature rats to diquat-induced cytotoxicity (lactate dehydrogenase release into the medium). Cell death was preceded by glutathione disappearance, and rates of glutathione depletion were similar in mature and old hepatocytes. In contrast, diquat-induced formation of thiobarbituric acid-reactive substances was much greater in the hepatocytes from old rats, suggesting that increased lipid peroxidation caused the enhanced cytotoxicity. Further experiments revealed that: 1) hepatocytes of mature and old rats were equally sensitive to iron-induced lipid peroxidation; 2) diquat-stimulated production of superoxide anion radical in liver microsomes did not increase with age, but decreased 43%; 3) superoxide dismutase activity was similar in hepatocytes of mature and old rats; 4) inhibition of catalase activity (which diminishes with age in male rats) did not increase diquat toxicity; and 5) malondialdehyde disappearance in intact hepatocytes decreased (33%) with age, but the toxicological significance of the decline in metabolism was uncertain. Thus, the results demonstrated that diquat-induced lipid peroxidation and cytotoxicity increase with age in male rat hepatocytes, but the enhanced sensitivity to diquat poisoning remains unexplained.
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PMID:Age-associated enhancement of diquat-induced lipid peroxidation and cytotoxicity in isolated rat hepatocytes. 132 Jun 87


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