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)

Lipid peroxidation of the cell membrane is one of the most important factors of reperfusion induced arrhythmia (RIA). To determine the role of lipid peroxidation in RIA, lipid peroxide (LPO) and superoxide dismutase (Total, Mn-SOD) were examined in this experiment. Thirty-four male Donryu strain rats (250-350 g body weight) were studied. After left thoracotomy and 5-minute ligature of LAD coronary artery, reperfusion was done under artificial ventilation with room air. The electrocardiogram (ECG) was recorded via standard limb leads. Twenty-four rats were divided into 5 groups and the heart tissue and blood samples were collected 1. preligature 2. after 1-minute ligature 3. after 4-minute ligature 4. 1-minute after declamping and 5. 10-minute after declamping. To examine the correlation between LPO and duration of RIA, samples from another 10 rats were collected as soon as RIA disappeared. LPO, SOD, CPK, and MDH (malate dehydrogenase) were measured in all samples. The total SOD level in heart tissue decreased after reperfusion (p less than 0.05). The heart tissue LPO (t-LPO) decreased after ligature (p less than 0.05), but each value in 2. to 5. was lower than 1., and no increase was found after reperfusion. A negative correlation of R = 0.87 (p less than 0.01) was found between t-LPO and RIA duration, but a positive correlation of R = 0.79 (p less than 0.01) was found between t-LPO and CPK. Moreover, the LPO level was lower in the RIA occurrence group than in the non-occurrence group (p less than 0.05).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Studies on the behavior of lipid peroxide in reperfusion induced arrhythmia]. 260 63

Two types of superoxide dismutase (SOD) have been found in Brucella abortus, a cytosolic Mn-SOD and a Cu/Zn-SOD of unknown location. We sought to determine the subcellular location of Cu/Zn-SOD in B. abortus ST 19. We report a modified spheroplasting procedure for the release of periplasmic contents from B. abortus cells using a dipolar ionic detergent, Zwittergent 316. This detergent, used in place of EDTA, destabilizes the outer membrane sufficiently to allow penetration of lysozyme and the subsequent selective release of periplasmic proteins by osmotic shock. Cytoplasmic cross-contamination of periplasmic fractions was assessed by assaying for malate dehydrogenase activity. Cyanide-sensitive and cyanide-insensitive SOD activity was measured by both the xanthine oxidase-cytochrome c method and a hematoxylin assay. Results suggest that B. abortus Cu/Zn-SOD activity is periplasmic. This zwittergent-lysozyme extraction procedure may be applicable to the separation, isolation and characterization of many other periplasmic proteins of B. abortus and other Gram-negative organisms especially when cytosolic contamination is undesirable.
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PMID:Periplasmic location of Brucella abortus Cu/Zn superoxide dismutase. 816 Mar 46

Using mouse hearts from Swiss Webster mice, calcineurin was immunoprecipitated using commercially available anti-calcineurin antibody and the resulting complex analyzed by using sodium dodecyl sulfate-gel electrophoresis with silver staining. Distinct proteins were observed and subjected to in situ trypsin digestion followed by extraction of the resulting peptides. Peptides from each protein band were loaded onto a target for matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and analyzed. The resulting peptide mass spectrum was compared with the Mascot and Protein Prospector databases and resulted in the specific identification of heart mitochondrial proteins, specifically Mn-superoxide dismutase (SOD), aconitase (ACN), and malate dehydrogenase (MDH). Each of the three mitochondrial enzymes was identified with approximately 15-25% sequence coverage and all with statistical significance (P < 0.05) according to the Mascot database search engine. Tandem mass spectrometry analysis of the peptide fragmentation spectra confirmed the identification of these protein partners and also yielded the identification of mitochondrial isocitrate dehydrogenase (ICDH) as another protein in the immunoprecipitated complex. Using antibody preparations against Mn-SOD, ACN, and ICDH showed the presence of calcineurin and each of the three proteins in the immunoprecipitated complex by Western slot blotting. The activity of ACN, but not MDH or ICDH, was enhanced after incubation with calcineurin indicating one possible regulatory function for the complex. The mitochondrial forms of Mn-SOD, ACN, MDH, and ICDH were identified as partner proteins of calcineurin with all the proteins present in a single multiprotein complex.
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PMID:Association of calcineurin with mitochondrial proteins. 1663 48

The activity of pea (Pisum sativum L.) Cu/Zn and Mn superoxide dismutase isoforms was evaluated across a range of temperatures from 10 to 45 degrees C. Maximal activity of the Cu/Zn and Mn superoxide dismutase isoforms was observed at 10 degrees C. Both cytoplasmic and chloroplast Cu/Zn superoxide dismutases exhibit a reduction in staining intensity with increasing temperatures. Mn superoxide dismutase, however, maintained a relatively constant staining intensity across the range of temperatures evaluated. An unrelated enzyme used as a control, malate dehydrogenase, exhibited the expected increase in staining activity with increasing temperatures. These results describe a unique response of a protection enzyme to temperature.
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PMID:Differential temperature sensitivity of pea superoxide dismutases. 1665 66

Superoxide dismutase (SOD) is an essential enzyme protecting cells against oxidative stress. However, its specific role under different conditions is not clear. To study the possible role of SOD in the cell during respiration, Saccharomyces cerevisiae single and double mutants with inactivated SOD1 and/or SOD2 genes growing on ethanol as an energy and carbon source were used. Activities of antioxidant and associated enzymes as well as the level of protein carbonyls were measured. SOD activity was significantly higher in a Mn-SOD deficient strain than that in the wild-type parental strain, but significantly lower in a Cu, Zn-SOD mutant. A strong positive correlation between SOD and catalase activities (R(2) = 0.99) shows possible protection of catalase by SOD from inactivation in vivo and/or decrease in catalase activity because of lower H(2)O(2) formation in the mutant cells. SOD deficiency resulted in a malate dehydrogenase activity increase, whereas glucose-6-phosphate dehydrogenase (G6PDH) activity was lower in SOD-deficient strains. Linear and non-linear positive correlations between SOD and isocitrate dehydrogenase activities are discussed. No changes in the activity of glutathione reductase and protein carbonyl levels support the idea that SOD-deficient cells are not exposed to strong oxidative stress during exponential growth of yeast cultures on ethanol.
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PMID:Growth on ethanol results in co-ordinated Saccharomyces cerevisiae response to inactivation of genes encoding superoxide dismutases. 1770 88

Oxidative damage to mitochondria caused by reactive oxygen species (ROS) has been implicated in the process of senescence as well as a number of senescence-related disorders in a variety of organisms. Whereas mitochondrial DNA was shown to be oxidatively modified during cellular senescence, mitochondrial protein oxidation is not well-understood. With the use of high-resolution, two-dimensional gel electrophoresis coupled with immunoblotting, we show here that protein carbonylation, a widely used marker of protein oxidation, increased in mitochondria during the senescence of peach fruit. Specific mitochondrial proteins including outer membrane transporter (voltage-dependent anion-selective channel, VDAC), tricarboxylic acid cycle enzymes (malate dehydrogenase and aconitase), and antioxidant proteins (manganese superoxide dismutase, MnSOD) were found as the targets. The oxidative modification was concomitant with a change of VDAC function and loss of catalytic activity of malate dehydrogenase and MnSOD, which in turn facilitated the release of superoxide radicals in mitochondria. Reduction of ROS content by lowering the environmental temperature prevented the accumulation of protein carbonylation in mitochondria and retarded fruit senescence, whereas treatment of fruit with H2O2 had the opposite effect. Our data suggest that oxidative damage of specific mitochondrial proteins may be responsible for impairment of mitochondrial function, thus, leading to fruit senescence. Proteomics analysis of mitochondrial redox proteins provides considerable information on the molecular mechanisms involved in the progression of fruit senescence.
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PMID:Oxidative damage of mitochondrial proteins contributes to fruit senescence: a redox proteomics analysis. 1923 64

Experiments were conducted to identify the differentially expressed proteins in rice (Oryza sativa L.) plants after treatment with the glycoprotein elicitor CSB I, purified from ZC(13), a race of the rice blast fungus Magnaporthe grisea. The interactions of two near isogenic lines of rice, C101A51 and CO39, with ZC(13) resulted in completely incompatible and compatible types, respectively. Proteins were extracted from rice leaves at 12 and 24 h after treatment with CSB I. Temporal changes in total proteins were examined using 2-DE. Among more than 900 protein spots reproducibly detected on each gel, 11 were up-regulated, three were down-regulated and seven were newly induced during, at a minimum, one time point. Twenty-one differentially expressed proteins were identified by linear ion trap quadrupole (LTQ)-MS/MS. The identified proteins were classified into six categories based on their putative function reported: (i) defense proteins (PR-10a, PR-5 and putative salt-induced protein), (ii) signal transduction (nucleoside diphosphate kinase and putative profilin), (iii) ROS (Mn-SOD, Cu/Zn-SOD, GST and CAT), (iv) programmed cell death (translationally controlled tumor protein), (v) molecule biosynthesis (putative ribosomal protein S5, putative ribosomal protein L12, putative translational elongation factor Tu and putative chaperonin 21 precursor) and (vi) metabolism (putative fructose-bisphosphate aldolase class-I, putative malate dehydrogenase, cytoplasmic malate dehydrogenase, putative acid phosphatase, putative transketolase1 and gamma hydroxybutyrate dehydrogenase-like protein). All of these proteins (except Cu/Zn-SOD, putative acid phosphatase and translationally controlled tumor protein) were induced faster and to a higher degree in C101A51 than in CO39. These data suggest that the incompatible rice line may possess a more sensitive recognition system that can identify and react to specific chemical, biological or physical triggers in a more efficient manner, thus eliciting an early and fast defense response.
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PMID:Identification of elicitor-responsive proteins in rice leaves by a proteomic approach. 1940 28