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 expression of manganese-containing superoxide dismutase (sodA) in Escherichia coli using sodA::lacZ gene fusion was found to be stimulated by DNA gyrase inhibitors, nalidixic acid, or coumermycin A1. Aerobically, the gyrase inhibitors increased the expression of sodA::lacZ in the presence or absence of either paraquat or the iron chelator 2,2'-dipyridyl. The concentrations of the inhibitors used were found to reduce DNA supercoiling. Treatment of wild-type cells (sodA+) with nalidixic acid increased the transcription of MnSOD mRNA. Anaerobically, the expression of sodA::lacZ in wild-type cells was not affected by nalidixic acid. However, nalidixic acid had a stimulatory effect on the anaerobic expression of sodA::lacZ in cells preinduced by the iron chelator as well as in mutants derepressed in sodA expression by virtue of their lacking the trans-acting repressor proteins or the cis-acting regulatory elements needed for sodA regulation. The results indicate that the effect of DNA gyrase inhibitors is secondary to the cis- and trans-regulatory elements of sodA and suggest that changes in DNA topology may affect transcriptional regulation of sodA.
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PMID:Transcriptional regulation of Mn-superoxide dismutase gene (sodA) of Escherichia coli is stimulated by DNA gyrase inhibitors. 133 15

Evidence is reported that liver manganese deficiency, whether artificially produced by the administration of a Mn-deficient diet, or physiologically occurring in the neonatal life, in mice and rats respectively, causes the down-regulation of the manganese-containing superoxide dismutase at (pre)-transcriptional level. These observations, in addition to previous data concerning Mn-deficiency and the low level of expression of MnSOD in Morris hepatomas, strongly support the role played by the metal ion in the control of the MnSOD by a mechanism of gene activation. While the molecular events taking place in such regulation are not yet identified, the involvement of reactive oxygen species (ROS) as second messengers in the activation of specific transcription factors is suggested.
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PMID:Transcriptional regulation of MnSOD by manganese in the liver of manganese-deficient mice and during rat development. 148 98

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

Serum concentrations of manganese-containing superoxide dismutase (Mn-SOD; EC 1.15.1.1), a mitochondrial enzyme present in high concentrations in the heart, were measured successively by enzyme immunoassay in 18 patients with acute myocardial infarction (AMI) and in eight with angina pectoris. Results were compared with creatine kinase (EC 2.7.3.2) isoenzyme MB (CK-MB) concentrations in the same specimens. The mean (and SD) serum Mn-SOD concentration in 120 healthy adults was 77.5 (18) micrograms/L. Mn-SOD concentrations exceeding 150 micrograms/L (greater than mean + 4 SD) were considered above-normal. In patients with AMI, the Mn-SOD concentration was 80 (16.8) micrograms/L on admission and increased gradually after the first hospital day. The peak, 260 (109) microgram/L, occurred on the fourth hospital day, at which time the Mn-SOD concentrations in all AMI patients were above normal. Thereafter the Mn-SOD concentration decreased slowly, but still was above normal in 14 of 18 patients on the seventh hospital day. On the other hand, in patients with angina pectoris, the Mn-SOD concentration was 78 (11) micrograms/L on admission and did not increase significantly [peak value 97.5 (42) micrograms/L on the fourth hospital day]. The serum concentration of Mn-SOD is a potentially useful marker for estimating cardiac mitochondrial damage and for diagnosing AMI, especially in the late phase.
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PMID:Concentration of Mn-superoxide dismutase in serum in acute myocardial infarction. 200 57

cDNAs coding for human manganese-containing superoxide dismutase (Mn SOD) have been isolated from a human liver and a dibutyryl cyclic AMP differentiated U937 cDNA library constructed in vector lambda gtll. The nucleotide sequences of the insert cDNAs had an opening reading frame coding for 222 amino acid residues. The first 24 amino acids of the primarily translated polypeptide might constitute the leader peptide for transport of the precursors to the mitochondria. Differentiation of the U937 cells with dibutyryl cyclic AMP resulted in a 70% decrease in Mn SOD mRNA. The amino acid sequences of the mature Mn SODs of human, rat and mouse are highly conserved, while the sequences of the leader peptides of these species are moderately conserved.
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PMID:Isolation and characterization of complementary DNAs encoding human manganese-containing superoxide dismutase. 283 Oct 93

In vitro synthesis of Escherichia coli manganese-containing superoxide dismutase, directed by the plasmid pDT1-5, has been achieved. The Mn superoxide dismutase polypeptide was identified by electrophoresis on polyacrylamide gels, immunoprecipitation, and the competitive immunoprecipitation effect of pure, active E. coli Mn superoxide dismutase. Dithiothreitol and glutathione, but not cysteine, suppressed in vitro synthesis of Mn superoxide dismutase. The parallel syntheses of beta-lactamase and of another unidentified polypeptide were not suppressed by thiols. In vitro transcription of the E. coli Mn superoxide dismutase gene was similarly suppressed by glutathione, dithiothreitol, and beta-mercaptoethanol; but not by L-cysteine or thioglycolate. Compounds, such as diamide, 1-chloro-2,4-dinitrobenzene, potassium ferricyanide, and methylene blue, which are expected to deplete intracellular glutathione, caused the induction of Mn superoxide dismutase in anaerobic E. coli.
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PMID:Controls on the biosynthesis of the manganese-containing superoxide dismutase of Escherichia coli. Effects of thiols. 332 44

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

Activities of the copper-zinc- and manganese-containing superoxide dismutase enzymes (CuSOD and MnSOD) were studied in tissues of the sheep to determine the dependence of these activities on sheep age, and their relationship to tissue and dietary mineral concentrations. Tissue samples were obtained from day-old through 16-week-old lambs from flocks grazing pastures normal or high in copper and manganese, and from adult sheep. In liver, lung, heart, kidney and skeletal muscle, activities of CuSOD and MnSOD in day-old and week-old lambs were only half those measured in 16-week-old and adult sheep. Activities in 4-week-old lambs were intermediate between these two groups except for heart tissue, in which activities were not increased until lambs were 16 weeks old. For all age groups, heart and skeletal muscle had low activities of CuSOD. Minimal age-related changes were observed for CuSOD activities in erythrocyte and brain tissues. The low enzyme activities evident in most tissues of day-old lambs, occurred in the presence of apparently adequate tissue copper and manganese concentrations. Concentrations of these minerals in lamb tissues were equal to or greater than those observed in older sheep and although these concentrations increased considerably with increased pasture mineral concentrations, enzyme activities were unchanged. Age-related increases in tissue CuSOD and MnSOD activities, occurring as normal developmental processes, may be important factors in diseases attributed to uncontrolled tissue peroxidation in sheep.
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PMID:Age-related changes in activities of the superoxide dismutase enzymes in tissues of the sheep and the effect of dietary copper and manganese on these changes. 648 83

Superoxide dismutases might conceivably protect against both ionizing radiation and free radical-producing antibiotic antitumor drugs. Copper- and zinc-containing superoxide dismutase (CuZn superoxide dismutase) and manganese-containing superoxide dismutase (Mn superoxide dismutase) were specifically assayed in human malignant tumors and for comparison in human tissues. The tumors possessed less CuZn superoxide dismutase than did the more metabolically active tissues, but there was a large overlap between the tissue and the tumor levels. Mn superoxide dismutase was found in all tumors, and the ratio between the activities of CuZn superoxide dismutase and Mn superoxide dismutase was not different from that of the normal tissues. Human tumors are thus different from tumors from other species which have been reported to be deficient or very low in Mn superoxide dismutase. There was no obvious relation between sensitivity to ionizing radiation and content of the enzymes among the tumors and the tissues, nor did tumor types known to be responsive to radical-producing drugs possess less CuZn superoxide dismutase or Mn superoxide dismutase than other tumors.
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PMID:Copper- and zinc-containing superoxide dismutase and manganese-containing superoxide dismutase in human tissues and human malignant tumors. 724 54

A genomic clone encoding manganese-containing superoxide dismutase (SOD; EC 1.15.1.1) was isolated from a Hevea brasiliensis genomic library made in lambda phage EMBL3 by using a heterologous cDNA probe of MnSOD from Nicotiana plumbaginifolia. The nucleotide sequence of 4968 bp from the genomic clone was determined. Based on the putative translation initiation codon and stop codon, PCR primers were designed and utilized for cloning the full-length cDNA from total mRNA. Of the two distinct cDNAs of MnSOD isolated, MnSOD-A has a perfect match with exons of the nuclear gene, while MnSOD-B has a 90.2% homology and is 6 nucleotides longer than MnSOD-A in the putative transit peptide region. The nuclear gene comprises 6 exons and 5 introns, giving a total length of 3211 bp. The sequences of 1400 bp upstream of the initiation codon and 320 bp downstream of the stop codon were also determined. Southern analysis of genomic DNA from Hevea probed with a genomic fragment indicated there are at least two genes of MnSOD in Hevea. Northern blot analysis showed that MnSOD transcripts were present in all tissues examined (leaf, petiole, root, latex, callus) with young leaves showing the highest levels in intact plants. The transcript level in embryogenic callus was nearly 50-fold higher than in mature leaves. In addition, transcripts of MnSOD could be induced 3- to 5-fold in response to sucrose, ethephon and Murashige-Skoog salts.
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PMID:Molecular cloning, characterization and expression of Mn-superoxide dismutase from the rubber tree (Hevea brasiliensis). 821 64


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