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 basal levels of superoxide dismutase (SOD) activity and chromosome aberration (CA) and sister-chromatid exchange (SCE) frequencies were examined in cultured fibroblasts or Epstein-Barr virus (EBV)-transformed lymphoblastoid cell lines (LCLs). These cells were derived from patients with chromosome instability syndromes (CISs) including Bloom's syndrome (BS), Fanconi's anemia (FA) and ataxia telangiectasia (AT). Embryonal fibroblasts and LCLs from normal subjects served as controls. Although LCLs tended to exhibit a higher SOD level than fibroblasts due to an elevation of Cu/Zn-SOD activity, BS and FA fibroblasts with increased frequencies of CAs and/or SCEs showed abnormally elevated SOD activity due to the manifold increase of Mn-SOD levels compared with control cells. However, BS and AT LCLs with almost control levels of CA and SCE frequencies showed no, or a slightly elevated, SOD activity, suggesting a possible selection of such cells during EBV transformation. The observed parallelism between the SOD activity and the cytogenetic manifestation may imply an involvement of active oxygen species, especially superoxide radicals, in the increased chromosome damage of CIS cells.
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PMID:Superoxide dismutase activity and chromosome damage in cultured chromosome instability syndrome cells. 236 19

The cellular localization of copper-zinc superoxide dismutase (CuZn SOD) mRNA was determined in the human hippocampus by in situ hybridization with a 35S-labelled DNA probe complementary to human CuZn SOD mRNA. A positive hybridization signal was detected in pyramidal cell layers CA1-CA4 of Ammon's horn (CA), pyramidal cells of subiculum and in the granule cells of the dentate gyrus. The fact that CuZn SOD gene expression is important in neurones which are preferentially vulnerable in neurodegenerative processes such as Alzheimer's disease, suggests a role played by oxygen free radicals in the mechanism of nerve cell death.
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PMID:Localization of copper-zinc superoxide dismutase mRNA in human hippocampus by in situ hybridization. 248 84

Root resorbing of deciduous teeth is a general phenomenon during eruption of the permanent teeth. In the present study, we tried to clarify the active-oxygen metabolism of root resorped granulated tissues. Granulated tissues were obtained from two fresh mandibles of young bovine about 1 year old undergoing root resorption. Cu-Zn-Superoxide dismutase (SOD), Mn-SOD, Lactate dehydrogenase (LDH), and concentration of lipid-peroxidated products were determined on the supernatants from homogenized tissues. We obtained the following results. 1) Cytosolic Cu-Zn-SOD activity did not elevate as compared to control tissues. 2) Elevation of mitochondrial Mn-SOD activity was observed in granulated tissues. 3) LDH activity did not elevate as compared to control tissues. 4) Lipid-peroxidated products in granulated tissues showed high concentration as compared to control tissues. Based on the above, we specurated that the active-oxygen metabolism in the root resorped granulated tissues, at least in mitochondria, was elevated.
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PMID:[Oxygen metabolism in roots resorbing granulated tissue from bovine deciduous teeth, from the aspects of superoxide dismutase, lactate dehydrogenase, and lipid peroxidation]. 248 84

I have developed the new procedure for the preparation of experimental ischemic spinal cord from dog. Using this preparation, I have measured the enzymatic activities of superoxide dismutase (SOD), catalase, and glutathione peroxidase. The ischemic spinal cords, monitored by the evoked spinal cord potential, were obtained after clamping bilateral subclavian arteries and aorta distal to the origin of the left subclavian artery. Total SOD activity of the normal spinal cord was one ninth lower than that of the brain. But its catalase activity was eight times higher. Total SOD, Mn-SOD, and glutathione peroxidase activities of my experimental ischemic spinal cord didn't change as compared with those of the normal ones. The catalase activity was decreased after spinal cord ischemia. These results indicate that the catalase plays the main of protection against peroxidative damage in the spinal cord induced by reperfusion, Ca++-dependent protease system may be involved in the decrease for catalase activity in addition to the high turnover rate of this enzyme. In summary, ischemic injury of spinal cord could be induced from the active oxygen species as well as disorder of Ca++ in the tissue.
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PMID:[Experimental studies on the mechanism of spinal cord ischemia--the state of free radical scavengers]. 254 42

In the skin ulcer or severely inflamed and erosive lesions induced due to burn, wounds and other dermatitides, lipid peroxides were markedly increased, with resultant cytotoxic effects in situ. Generally, superoxide dismutase (SOD), which scavenges oxygen radicals or inhibits lipid peroxidation, is adapted to be induced (increased) under oxygen toxicity. For the treatment of not only systemic inflammatory diseases but also skin ulcer lesions, especially due to burn and wounds, liposomal-encapsulated SOD injection was effective. Topical application of free Mn-SOD or Cu, Zn-SOD extracted from bovine, bacterial and other species except for human was also dramatically effective in skin lesions; a burnt patient who was advised to undergo skin transplantation showed complete healing with free SOD cream. In addition, topical application of low molecular weight antioxidants, AOA or Bio-harmony, also showed remarkable effectiveness in these skin lesions. However, SOD dissolved in the vehicle containing greater amounts of vaselinum album (white petrolatum) rapidly lost its activity, and that dissolved in the vehicle with large quantities of water lost its activity within 3 months. In conclusion, SOD should be dissolved in the vehicle before use, however, low molecular weight antioxidant cream can be commercially sold because it does not lose its activity for long periods.
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PMID:Lipid peroxides and superoxide dismutase (SOD) induction in skin inflammatory diseases, and treatment with SOD preparations. 267 51

Superoxide-mediated oxidative stress initiates a chain of events resulting in numerous cellular injuries. We have used genetics and E. coli to investigate the role and regulation of superoxide dismutase (SOD) and its relationship with the other constituents of the oxygen toxicity defence system. Structural SOD genes have been cloned and sequenced, permitting us to refine structural analysis and to isolate SOD-deficient mutants. The conditional oxygen sensitivity of these mutants, together with their increased mutation rate, demonstrated the essential biological role of SOD. Furthermore the complementation of SOD-lacking E. coli deficiencies by introducing a plasmid containing the gene encoding the human SOD supported the proposal that superoxide dismutation is the physiological function of SOD. Regulation of the MnSOD, through which the global SOD level in E. coli is modulated, has been studied using operon and protein fusions with the lactose operon, and led to the conclusion of a multicontrol of MnSOD. Isolation and characterization of regulation mutants are in progress, with the aim of identifying effectors and targets involved in the response to superoxide-mediated oxidative stress.
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PMID:The molecular genetics of superoxide dismutase in E. coli. An approach to understanding the biological role and regulation of SODS in relation to other elements of the defence system against oxygen toxicity. 268 1

The activity of antioxidant enzymes were measured in alveolar type II cells isolated from control and 85% oxygen-exposed rats to determine if type II cells, an oxygen-resistant lung cell type had constitutively high enzyme activities and to measure the effect of hyperoxia on these antioxidant enzyme. Type II cells were isolated from lungs of control rats and rats exposed to 85% O2 for 7 days. In whole lungs of rats exposed to 85% oxygen there is an increase in activity (per lung or per mg lung DNA) in the antioxidant enzymes CuZn superoxide dismutase, Mn superoxide dismutase, catalase, glutathione peroxidase and glucose-6-phosphate dehydrogenase. Oxygen exposure significantly increased (p less than 0.05) all type II cell antioxidant enzyme activities when expressed per mg DNA. The protein content of oxygen exposed type II cells increased 25% from (63.9 +/- 4.8 micrograms/10(6) cells to 79.6 +/- 4.2 micrograms/10(6) cells, p less than 0.05). When type II cell enzyme activities were expressed in U/mg cell protein, only CuZn superoxide dismutase and Mn superoxide dismutase increased in activity following oxygen exposure (by 43% and 28% relative to air exposed lung type II cells, respectively, p less than 0.05). This suggested that most lung cell antioxidant enzymes increased in activity following oxidant stress in proportion to increased cell mass. CuZn and Mn superoxide dismutase increased activity to an extent greater than the increase in type II cell protein content after oxygen exposure. Alveolar macrophages lavaged from control and oxygen-exposed rats were also evaluated, and they had no significant change in CuZn and Mn superoxide dismutase activities. Type II cells accounted for 10% and 17% of alveolar cells in control and oxygen treated rats. By knowing the antioxidant enzyme activities in type II cells, the total enzyme activity of whole lung and the number of type II cells in control and oxygen exposed rats from morphometric data, we calculated the percent of whole lung enzyme activity accounted for by type II cells. Type II cells accounted for a high percentage of lung glucose-6-phosphate dehydrogenase (58% in control rats, 65% in oxygen exposed rats) but a low percentage of Mn superoxide dismutase (4% in control rats, 6% in oxygen exposed rats).
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PMID:Antioxidant enzyme activity in alveolar type II cells after exposure of rats to hyperoxia. 300 82

An Escherichia coli double mutant, sodAsodB, that is deficient in both bacterial superoxide dismutases (Mn superoxide dismutase and iron superoxide dismutase) is unable to grow on minimal medium in the presence of oxygen and exhibits increased sensitivity to paraquat and hydrogen peroxide. Expression of the evolutionarily unrelated eukaryotic CuZn superoxide dismutase in the sodAsodB E. coli mutant results in a wild-type phenotype with respect to aerobic growth on minimal medium and in resistance to paraquat and hydrogen peroxide. This supports the hypothesis that superoxide dismutation is the in vivo function of these proteins. Analysis of the growth of sodAsodB cells containing plasmids encoding partially active CuZn superoxide dismutases, produced by in vitro mutagenesis, shows a correlation between cell growth and enzyme activity. Thus, the sodAsodB strain provides a controlled selection for varying levels of superoxide dismutase activity.
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PMID:Human copper-zinc superoxide dismutase complements superoxide dismutase-deficient Escherichia coli mutants. 331 94

The nuclear gene for manganese-containing superoxide dismutase (MnSOD; superoxide:superoxide oxidoreductase, EC 1.15.1.1) of yeast mitochondria was mapped on chromosome VIII and inactivated by gene disruption. The resulting mutant lacked any protein cross-reacting with anti-MnSOD antibodies, and its mitochondria exhibited less than 1% of the cyanide-insensitive superoxide dismutase activity found in mitochondria of the wild-type parent strain. In the absence of oxygen, the mutant grew as rapidly as the wild-type parent. However, increasing concentrations of oxygen led to a progressive inhibition of growth. The properties of this mutant provide direct evidence that MnSOD contributes to the natural protection of cells against oxygen toxicity.
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PMID:A yeast mutant lacking mitochondrial manganese-superoxide dismutase is hypersensitive to oxygen. 352 May 57

Levels of Cu, Zn superoxide dismutase (CuSOD), Mn superoxide dismutase (MnSOD), catalase, and glutathione peroxidase (GPx) were assessed in the rat brain cortex. The concentrations of Cu- and MnSOD were found to increase linearly with the logarithm of the age of the animal from 3 days before birth to 30 months, both in the whole cortex tissue and in its cytoplasmic fraction. Catalase and GPx levels showed different trends; in particular, GPx, which appears to play a key role in detoxification of hydrogen peroxide, after an initial fall increases steadily with age. The enhancement of the levels of SOD and GPx could be related to protection against an increased production of reactive oxygen species in the aging process.
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PMID:Age dependence of the level of the enzymes involved in the protection against active oxygen species in the rat brain. 357 30


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