Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P04179 (MnSOD)
2,777 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The superoxide dismutating activity of the D-penicillamine copper complex was determined and compared with the activities of Cu-Zn and Mn superoxide dismutase in four O2 ground negative earth generating systems. I. Nitrite formation from hydroxylamine. II. Crocin destruction by xanthine/xanthine oxidase. III. Ethylene production by isolated chloroplasts. IV. Nitrite formation from hydroxylamine by chloroplasts in the presence of diquat (1, 1'-dimethylene-2,2'-bipyridylium dibromide). In all four test systems a high dismutative activity of the complex was found, which is not sensitive to KCN as demonstrated with test system III. The results are discussed with regard to the antiinflammatory activity of D-penicillamine.
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PMID:Determination of the superoxide dismutating activity of D-penicillamine copper. 66 84

The lung activity of the antioxidant enzymes (AOEs) copper, zinc superoxide dismutase (Cu,Zn SOD), catalase (CAT), and glutathione peroxidase (GP), but not manganese superoxide dismutase (Mn SOD), increases in rats during late gestation; the concentrations of Cu,Zn SOD mRNA and CAT mRNA also rise. During early postnatal exposure to > 95% O2, the lung activity of Cu,Zn SOD, CAT, and GP increases. We now show 1) the lung concentration of Mn SOD mRNA and GP mRNA does not increase in late gestation; 2) Mn SOD activity and the concentration of its mRNA and of GP mRNA increase during exposure of neonatal rats to > 95% O2; and 3) as previously shown for CAT mRNA, the increase in lung concentration of the mRNAs for Cu,Zn SOD, Mn SOD, and GP during early postnatal hyperoxia occurs with a 70-80% prolongation of the half-life of these mRNAs. We conclude that 1) in late gestation the level at which lung AOE gene expression is regulated differs among the enzymes, 2) the level at which lung AOE gene expression is regulated shortly after birth in response to > 95% O2 is uniform among the enzymes, and 3) the lung's AOE response to neonatal hyperoxia is not merely a step-up of its prenatal regulation but involves different regulatory mechanisms based on increased stability of AOE mRNAs.
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PMID:Rat lung antioxidant enzymes: differences in perinatal gene expression and regulation. 141 24

We investigated the developmental profile of copper-zinc and manganese superoxide dismutase (CuZnSOD and MnSOD) in tissue sections obtained from fetal (Day 12 to 21 of gestation) and neonatal (Day 0 and 6) rats. Tissues were stained immunohistochemically with specific antisera against the respective rat SODs. There was a general trend towards richness of SODs in the epithelial linings and metabolically active sites, although differential distribution between the two SODs also existed. At Day 12 of gestation, immunoreactivity for both SODs was detected in the cardiomyocytes but not in other tissues. Hepatocytes expressed CuZnSOD at Day 14 and MnSOD at Day 17. By Day 18 CuZnSOD was detected in the epithelial cells of the gastrointestinal tract, respiratory tract, pancreatic islets, kidneys, and adrenals. These tissues exhibited MnSOD staining at Day 19. CuZnSOD occurred in the epithelia of the thyroid, thymus, and salivary glands at Day 19, while MnSOD was seen at Day 21. The increase in intensity of the staining for SODs occurred no later than postnatal Day 0, indicating that most tissues accumulated SODs during late gestation. Breathing atmospheric oxygen during early extrauterine life did not appreciably intensify the SOD staining. These results suggest that perinatal increase in SODs occurs as a general mechanism of preparation for birth.
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PMID:Immunohistochemical localization of superoxide dismutases in fetal and neonatal rat tissues. 143 Oct 59

Four experiments were done to characterize the interactions of copper, iron, and ascorbic acid with manganese in rats. All experiments were factorially arranged Dietary Mn concentrations were less than 1 micrograms/g (Mn0) and 50 micrograms/g (Mn+). Dietary Cu was less than 1 mg/g (Cu0) and 5 micrograms/g (Cu+); dietary Fe was 10 micrograms/g (Fe10) and 140 micrograms/g (Fe140). Ascorbic acid (Asc) was not added to the diet or added at a concentration of 10 g/kg diet. Experiment 1 had two variables, Mn and Cu; in Experiment 2, the variables were Mn and Asc. In Experiment 3, the variables were Mn, Cu, and Asc; in Experiment 4, they were Mn, Cu, and Fe. Definite interactions between Mn and Cu were observed, but they tended to be less pronounced than interactions between Mn and Fe. Cu depressed absorption of 54Mn and accelerated its turnover. In addition, adequate Cu (Cu+), compared with Cu0, depressed liver, plasma, and whole blood Mn of rats. Absorption of 67Cu was higher in animals fed Mn0 diets than in those fed Mn+. Ascorbic acid depressed Mn superoxide dismutase activity and increased Cu superoxide dismutase activity in the heart. The addition of ascorbic acid to the diet did not affect Mn concentration in the liver or blood. Absorption of 54Mn was depressed in rats fed Fe140 compared with those fed Fe10. Interactions among Fe, Cu, and Mn resulted in a tendency for Mn superoxide dismutase activity to be lower in rats fed Fe140 than in rats fed Fe10. Within the physiologic range of dietary concentrations, Mn and Cu have opposite effects on many factors that tend to balance one another. The effects of ascorbic acid on Mn metabolism are much less pronounced than effects of dietary Cu, which in turn affects Mn metabolism less than does Fe.
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PMID:Effects of copper, iron, and ascorbic acid on manganese availability to rats. 154 27

Human retinal pigment epithelium (RPE) contains two genetically distinct forms of superoxide dismutase (SOD) enzymes that scavenge harmful superoxide anions. Biochemical and immunochemical techniques were used to compare levels of copper-zinc- and manganese-containing forms of SOD (CuZn-SOD and Mn-SOD) in human adult and fetal RPE cells. It was found that Mn-SOD activity was higher in adult than fetal RPE cells, both in vivo and in vitro. Immunolocalization of Mn-SOD in cultured RPE cells showed a greater reactivity in the mitochondria of the adult cells. Primary cultures of adult RPE contained cells with various patterns of mitochondria as shown by immunolabeling for Mn-SOD. Adult RPE cells were more resistant to the effects of a superoxide generator, paraquat, which appeared to disrupt mitochondrial integrity as judged by staining with rhodamine 123. These results suggest that high levels of Mn-SOD protect mitochondria from oxidative damage that probably occurs with aging in the RPE.
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PMID:Mitochondrial superoxide dismutase in mature and developing human retinal pigment epithelium. 158 97

Eucaryotes have two major forms of superoxide dismutase (SOD), Cu,ZnSOD and MnSOD; in most tissues Cu,ZnSOD is present in higher amounts than MnSOD. To assay MnSOD, Cu,ZnSOD can be inhibited selectively by millimolar concentrations of cyanide ion. However, calculation of MnSOD activity from the differential cyanide inhibition assay is complex and small experimental errors can cause large errors in the calculated MnSOD activity. We have assessed how interaction of cyanide and hydrogen peroxide with cytochrome c can lead to further errors in the xanthine oxidase-cytochrome c assay for SOD. Alternatively, Cu,ZnSOD can be completely inactivated by 50 mM diethyldithiocarbamate (DDC) at 30 degrees C for 1 h without affecting the activity of MnSOD. Since DDC reduces cytochrome c, the treated samples must be thoroughly dialyzed or desalted before assay. In the case of lung homogenates, dialysis is not an extra step since fresh, untreated samples must also be dialyzed or desalted before assaying by the cytochrome c method. Cu,ZnSOD activity is equal to the activity in the untreated sample minus the activity in the DDC-treated portion of the sample. Another copper chelator, triethylenetetramine, did not inactivate Cu,ZnSOD and could not be used instead of DDC. For accurate measurement of both enzymes in samples where MnSOD contributes only a small fraction of the total SOD activity, the DDC method has the advantage that it provides a direct measure of the MnSOD activity without interference by Cu,ZnSOD.
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PMID:Use of cyanide and diethyldithiocarbamate in the assay of superoxide dismutases. 164 52

A method for copper- and manganese-containing superoxide dismutase (Cu- and MnSOD) assay in tissue homogenates such as liver and brain, based on the measurement of the longitudinal nuclear relaxation time (T1) of F-, has been developed as a preliminary approach to in vivo measurement of these enzymes. The relaxation rate of F-, which increases linearly with the SOD concentration, also depends on the oxidation state of the metal ion present in the active site of the enzyme. The relaxivity values of the oxidized, reduced and turnovering CuSOD were found to be 9.6 x 10(6), much less than 1 x 10(2) and 5.2 x 10(6) M-1 s-1, respectively, while for MnSOD the corresponding values were 2.9 x 10(6), 4.2 x 10(6) and 3.6 x 10(6) M-1 s-1, respectively. These high relaxivity values allow the detection of SODs in brain and liver homogenates where, under aerobic conditions, these enzymes appear in the steady-state. The contribution of the two types of SOD to the F- relaxation rate in the homogenates was measured by addition of either diethyldithiocarbamate or cyanide, both of which selectively inhibit the CuSOD. The comparison between NMR and activity data confirmed the possibility of carrying out accurate and precise measurements of SODs in homogenates by NMR.
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PMID:NMR method for superoxide dismutase assay in brain and liver homogenates. 164 13

The antioxidant responses of human cell differentiation and membrane fusion are not known and may be important in understanding cellular response to injury in the human placenta. We studied the regulation of antioxidant enzymes in human trophoblasts which differentiate from mononucleated cellular trophoblasts to synctium in vivo and in culture. We characterized morphological and biochemical differentiation of cultured trophoblasts from term placenta in the presence or absence of serum, on different growth surfaces, and with a range of plating densities. Culture of cellular trophoblasts consistently and transiently induced the mRNAs of the mitochondrial antioxidant manganese superoxide dismutase (Mn SOD) but not the mRNAs for the antioxidant enzymes copper zinc SOD or catalase. Fibrin and type I collagen substrates modulated only the expression of the placental specific proteins, human chorionic gonadotropin, and human placental lactogen. Both Mn SOD induction and terminal differentiation, as reflected by human chorionic gonadotropin expression, were dependent on trophoblastic plating density. Increased levels of a smaller Mn SOD mRNA species correlated temporally with an increase in Mn SOD enzyme activity in cultured trophoblasts. These results demonstrate that Mn SOD gene expression and enzyme activity precede or are coordinately regulated with morphological and biochemical trophoblastic differentiation.
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PMID:Induction of manganese superoxide dismutase in cultured human trophoblast during in vitro differentiation. 172 88

An acute dose of ethanol was used to investigate the biochemical response of tissues with a compromised antioxidant defense system to a surge of oxygen radical production. The copper (Cu)-deficient rat served as the animal model for this study based on its compromised antioxidant defense system. Rats were fed control (10 micrograms Cu/g) or Cu-deficient (0.2 microgram Cu/g) diet for 14 days. In order to minimize secondary effects associated with chronic Cu deficiency, the chelator triethylenetetramine was added to the Cu-deficient diet to shorten the time required for the induction of Cu deficiency. On day 14, rats were gavaged with ethanol (4.5 g/kg b.wt.) or saline and killed 9 hours postgavage. Rats fed the Cu-deficient diets had lower liver superoxide dismutase (SOD) and glutathione peroxidase (GPx) activities than controls. Ethanol treatment had no effect on liver CuZnSOD or Gpx activity, while MnSOD activity was higher than saline control levels following EtOH treatment. Despite low GPx and SOD activity, Cu-deficient rats did not exhibit higher hepatic thiobarbituric acid reacting substances (TBARS) than controls; in fact, hepatic microsomal TBARS were lower in saline-treated Cu-deficient rats relative to Cu-sufficient rats. Ethanol treatment resulted in higher whole homogenate and mitochondrial TBARS than in saline-gavaged rats. Copper status did not influence hepatic TBARS production in response to an acute EtOH load. These data suggest that compensatory mechanisms contribute to the protection of the liver from excessive free radical production in this model of Cu deficiency.
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PMID:Influence of copper status on the response to acute ethanol exposure in rats. 178 25

Superoxide dismutases (SODs) are metalloproteins that catalyze the dismutation of superoxide radicals to hydrogen peroxide and oxygen. The enzyme is ubiquitous in aerobic organisms where it plays a major role in defense against oxygen radical-mediated toxicity. In plants, environmental adversity often leads to the increased generation of reduced oxygen species and, consequently, SOD has been proposed to be important in plant stress tolerance. Here we describe the isolation of a cDNA clone encoding a cytosolic copper/zinc SOD from Nicotiana plumbaginifolia. Using this, together with previously isolated cDNAs encoding the mitochondrial manganese SOD and the chloroplastic iron SOD as probes in RNA gel blot analyses, we have studied SOD transcript abundance during different stress conditions: in response to light, during photoinhibitory conditions (light combined with high or low temperatures), and in response to a xenobiotic stress imposed by the herbicide paraquat. Evidence is presented that iron SOD mRNA abundance increases whenever there is a chloroplast-localized oxidative stress, similar to the previous finding that manganese SOD responds to mitochondria-localized events. The diverse effects of the different stress conditions on SOD mRNA abundance thus might provide an insight into the way that each treatment affects the different subcellular compartments.
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PMID:Differential regulation of superoxide dismutases in plants exposed to environmental stress. 182 Aug 18


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