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)

Antioxidant enzyme levels were determined in kidneys during estrogen-induced cortical renal tumorigenesis in male Syrian hamsters. The activity of these enzymes in renal tumors were compared to those in the kidney cortex of untreated male castrated hamsters of different ages and in age-matched animals treated with diethylstilbestrol (DES) for varying periods. A transient increase in kidney Mn superoxide dismutase (MnSOD) and total SOD activity was seen after 1.5 and 3.1 months of DES treatment compared to untreated controls. However, after 4.4 months of DES exposure the activities of these antioxidant enzymes fell below untreated levels. The level of MnSOD and CuZnSOD was 3- to 10-fold lower compared to castrated male renal cortical values in DES-induced primary, serially transplanted and in autonomous renal tumour variants. Catalase activity declined steadily at 1.5 to 4.4 months of DES treatment. Low levels of catalase activity were found in all tumors examined. In general, Western blot analysis of immunoreactive proteins confirmed these findings, indicating that the low enzyme activities were due to low levels of enzyme proteins. Immunohistochemistry of the earliest tumor foci exhibited negligible antioxidant enzyme activity. The levels of these antioxidant enzymes were similar in all tumors surveyed, both primary and autonomous variants and in newborn kidneys, and they were about 10-fold lower than in normal kidney cortex or isolated proximal tubules.
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PMID:Superoxide dismutase and catalase levels during estrogen-induced renal tumorigenesis, in renal tumors and their autonomous variants in the Syrian hamster. 204 4

The influence of an animal's copper (Cu) and manganese (Mn) status on its response to ozone was investigated in weanling mice. Control, Cu-deficient and Mn-deficient mice were exposed continuously to 1.2 ppm O3 or filtered air for 7 days. In control mice, ozone exposure resulted in higher lung activities of CuZnSOD, MnSOD and GPx. In contrast, Mn-deficient mice did not display increases in lung MnSOD, CuZnSOD or GPx activities following ozone exposure. Similarly, ozone-induced increases in lung CuZn-SOD and MnSOD activities were not observed in Cu-deficient mice, although lung GPx activity was increased in these mice relative to their air-breathing controls. These results show that an animal's Cu and Mn status can influence its response to ozone, and the data suggest that Cu- and Mn-deprived animals may be more susceptible to long-term or repetitive ozone exposure.
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PMID:Influence of dietary-induced copper and manganese deficiency on ozone-induced changes in lung and liver antioxidant systems. 204 64

The immunohistochemical localization of manganese (Mn)-superoxide dismutase (Mn-SOD) was studied in the rat basal forebrain using polyclonal antibodies to Mn-SOD. Neurons of the basal forebrain exhibit a high density of Mn-SOD immunoreactivity. Double immunostaining with a monoclonal antibody to choline acetyltransferase demonstrated that both cholinergic and non-cholinergic neurons in the basal forebrain are intensely immunoreactive for Mn-SOD.
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PMID:Intense immunoreactivity for Mn-superoxide dismutase (Mn-SOD) in cholinergic and non-cholinergic neurons in the rat basal forebrain. 205 47

Bacterial lipopolysaccharide (LPS) was shown to produce an induction of manganese superoxide dismutase (Mn SOD) mRNA levels in porcine pulmonary artery endothelial cells (PAEC). Additional studies in porcine PAEC also demonstrated induction of Mn SOD mRNA in response to the inflammatory mediators interleukin 1 and tumor necrosis factor. On the other hand, we observed no change in Mn SOD mRNA within 24 h of a hyperoxic exposure. The induction of Mn SOD by LPS was blocked by both a RNA synthesis inhibitor, actinomycin D, and a protein synthesis inhibitor, cycloheximide. The data implicate the involvement of Mn SOD in the acute phase response of pulmonary endothelial cells.
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PMID:Regulation of manganese superoxide dismutase in porcine pulmonary artery endothelial cells. 205 89

The distribution of cells containing copper-zinc superoxide dismutase (CuZn SOD) protein and mRNA was studied in hippocampi from normal humans and patients with Alzheimer's disease (AD) by using immunohistochemistry and in situ hybridization. Using antisera against native and denatured CuZn SOD protein, we have determined that immunostaining was intense in pyramidal neurons of the cornu ammonis, in granule cells of the dentate gyrus and very weak in other cells. In the hippocampus of an Alzheimer's patient, successive immunostaining of the same tissue section by antiCuZn SOD and antipaired helical filaments antisera show that both normal and degenerating cells were labeled by the antiCuZn SOD antiserum. Thus, large pyramidal neurons which are susceptible to degenerative processes in AD have the property to contain high amount of CuZn SOD protein. In situ hybridization was performed on paraformaldehyde-fixed hippocampus sections of normal human brains and AD brains with a 35 S labeled DNA probe homologous to human CuZn SOD mRNA. Our results show that CuZn SOD transcripts are present at high abundance in pyramidal neurons of the CA1-CA4 fields, subiculum, and in granule cells of the dentate gyrus. This cellular distribution is similar to that obtained with the antiCuZn SOD antiserum. This might indicate that biochemical pathways leading to superoxide radicals generation are specially active in these neurons, requiring an active transcription of CuZn-SOD gene.
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PMID:Neuronal localization of copper-zinc superoxide dismutase protein and mRNA within the human hippocampus from control and Alzheimer's disease brains. 206 Aug 34

The effect of micronutrient stress (either deficiency or toxicity) on the expression of different superoxide dismutase isoenzymes in plants is reviewed. The induction of Fe-SOD and Mn-SOD by different metals and the potential use of the metalloenzyme system SOD for the appraisal of the micronutrient status of plants, is examined. At subcellular level, evidence for the participation of peroxisomal SOD in the molecular mechanism of plant tolerance to Cu is presented, and the activated oxygen-dependent toxicity of a xenobiotic (clofibrate) in plant peroxisomes is examined.
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PMID:Nutritional effect and expression of SODs: induction and gene expression; diagnostics; prospective protection against oxygen toxicity. 206 Aug 54

Cu,Zn.superoxide dismutase (SOD) enhanced the toxicity of 3-hydroxyanthranilic acid (3-HAT) to Salmonella typhimurium strain TA 102, evaluated as ability to form colonies. MnSOD showed the same effect. Inactivated Cu.ZnSOD had no effect. SODs accelerated the oxidation of 3-HAT, but inactivated Cu.ZnSOD caused little acceleration. It is proposed that the acceleration of 3-HAT oxidation leads to the enhancement of the 3-HAT toxicity. Catalase protected the bacteria from the toxicity of 3-HAT enhanced by Cu,ZnSOD, indicating that hydrogen peroxide generated in the oxidation of 3-HAT is involved in the toxicity. SODs accelerate the oxidation of 3-HAT and generate more hydrogen peroxide, that causes the enhancement of the 3-HAT toxicity to the bacteria. However, hydrogen peroxide alone was not so toxic. Hydrogen peroxide with 3-HAT was more toxic to the bacteria.
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PMID:Superoxide dismutase enhances the toxicity of 3-hydroxyanthranilic acid to bacteria. 206 Aug 64

Monoclonal antibodies against human Cu,Zn-superoxide dismutase (SOD) and Mn-SOD were used to stain frozen sections of normal and abnormal human skin. In normal human epidermis, the Cu,Zn-SOD antibody almost exclusively stained the basal cells. Mn-SOD antibody weakly stained the whole of the epidermis but more predominantly the basal cell layer. In psoriasis, Cu,Zn-SOD antibody mainly stained the basal cells of the lowest parts of the elongated rete ridges. Basal cells corresponding to the tip of the dermal papillae were weakly stained. Mn-SOD staining was considerably decreased in the psoriatic epidermis. In squamous cell carcinoma, staining with both Cu,Zn-SOD and Mn-SOD antibodies was decreased, and single cells positive for Cu,Zn-SOD were scattered throughout the tumour nests. In basal cell epithelioma, Cu,Zn-SOD staining was intense and diffusely distributed throughout the tumour nests, while Mn-SOD staining was absent.
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PMID:Superoxide dismutase in psoriasis, squamous cell carcinoma and basal cell epithelioma: an immunohistochemical study. 206 38

Bacteroides fragilis, an obligate anaerobe, synthesizes an azide-inhibitable iron-containing superoxide dismutase when grown in complex medium. Cells grown anaerobically in complex media containing desferrioxamine (Desferal, Ciba-Geigy) and graded concentrations of Mn synthesize the azide-resistant manganese-containing SOD. The fraction of MnSOD activity in dialyzed cell extracts increased progressively as the Mn concentration in the medium increased. The fraction of MnSOD activity also increased in extracts of cells grown in the medium with 1 mM Mn but with graded concentrations of desferrioxamine (0-10 micromolar). The SOD activity in the cells grown under the various conditions varied but not in a causal relationship with either Mn or desferrioxamine concentration. Electrophoresis revealed that the SOD activity in cells grown in the absence or presence of 1 mM Mn migrated with the same relative mobility and exhibited identical activity patterns when examined separately or as a mixture. These data are consistent with substitution of Mn for Fe in the B. fragilis apoprotein under anaerobic conditions and support the model of a single protein binding either Fe or Mn.
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PMID:In vivo metal substitution in Bacteroides fragilis superoxide dismutase. 207 Oct 36

The biological role and the regulation of superoxide dismutase (SOD) in E. coli have been investigated using genetics. Cloning of both E. coli SOD genes permitted construction of mutants completely lacking SOD. The conditional oxygen sensitivity of those mutants, together with their increased mutation rate, demonstrated the essential biological role of SOD. SOD-deficient mutants constitute a powerful tool to assess a possible role of O-2 or SOD in biological processes. Complementation of their deficiencies by the expression of SOD originating from a different organism is used for screening libraries for SOD genes of other species. Regulation of MnSOD has been studied using protein and operon fusions with the lactose operon, and isolating regulation mutants. These studies reveal multiregulation of MnSOD including response to the superoxide mediated oxidative stress and response to variations of the intracellular redox state induced by metabolic changes.
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PMID:The molecular genetics of superoxide dismutase in E. coli. 207 Oct 41


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