• Korean Journal of Plant Resources
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• v.10 no.2
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• pp.188-193
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• 1997

Panax ginseng C.A.Meyer,1 to 5 years old were electrophored and were stained for SOD activity. The result indicated a total of 13 distinct form of the enzyme and the pattern of achromatic bands were not different according to ages. Nine of the enzyme activities were eliminated with cyanide or peroxide treatment and were resistant to treatment of chloroform plus ethanol. It suggested that they may be cupro-zinc containing SOD, whereas four were cyanide or peroxide resistant and were eliminated with cholroform plus ethanol treatment. They may be manganese containing SOD. Ginseng roos. 1 to 5 years old were analyzed for their SOD measurement of SOD activities of all extracts, the significant difference of SOD activities were not shown according to ages. All ginseng extracts had the total SOD activities of all extracts, the significant difference of SOD activities were not shown according to ages. All ginseng extracts had the total SOD activities of about 700-800 unit/g of fresh weight. Therefore, the SOD activities from SOD-mimic compounds were higher than one from SOD. The ratio between the SOD activity from SOD-mimic compounds and one from true SOD was approximately 2:1 to 3:1.

• Korean Journal of Plant Resources
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• v.12 no.3
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• pp.234-239
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• 1999

The isoenzyme patterns and activities of superoxide dismutase(SOD) were investigated from leaves of Araliaceae plants. Of the eight isoenzymes, two isoenzymes(SOD 4 and SOD 6) were prevalent to leaves of Araliaceae plants. The patterns of these two isoenzymes were most various in the leaves of Acanthopanax senticosus for. inermis, while their activity was highest in the leaves of A. koreanum. These two isoenzymes were respectively identified as Fe-SOD and CuZn-SOD, based on selective inhibition with KCN or$H_2O_2$. The SOD isoenzyme patterns did not differed among stem barks, root barks and leaves of A. koreanum. However, the activities of Fe-SOD and CuZn-SOD were higher in the root bark and in leaves, respectively. Both of Fe-SOD and CuZn-SOD were stable for 1 hr at 30-4$0^{\circ}C$, while unstable above 5$0^{\circ}C$.

• Korean Journal of Environmental Agriculture
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• v.29 no.1
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• pp.77-85
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• 2010

Reactive oxygen species (ROS) are very harmful to living organisms due to the potential oxidation of membrane lipids, DNA, proteins, and carbohydrates. transformed E.coli strain QC 871, superoxide dismutase (SOD) double-mutant, with three sequence variant MnSOD1, MnSOD2, and MnSOD3 manganese superoxide dismutase (MnSOD) gene isolated from wheat. Although all QC 871 transformants grown at $37^{\circ}C$ expressed mRNA of MnSOD variants, only MnSOD2 transformant had functional SOD activity. MnSOD3 expressed active protein when grown at $22^{\circ}C$, however, MnSOD1 did not express functional protein at any growing and induction conditions. The sequence comparison of the wheat MnSOD variants revealed that the only amino acid difference between the sequence MnSOD2 and sequences MnSOD1 and 3 is phenylalanine/serine at position 58 amino acid. We made MnSOD2S58F gene, which was made by altering the phenylalaine to serine at position 58 in MnSOD2. The expressed MnSOD2S58F protein had functional SOD activity, even at higher levels than the original MnSOD2 at all observed temperatures. These data suggest that amino acid variation can result in highly active forms of MnSOD and the MnSOD2S58F gene can be an ideal target used for transforming crops to increase tolerance to environmental stresses.

• Journal of Crop Science and Biotechnology
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• v.10 no.1
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• pp.8-12
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• 2007

All accessions of Rehmannia glutinosa show the unique characteristic of intrinsic tolerance to paraquat. The higher level of endogenous superoxide dismutase(SOD) activity and its increase upon paraquat treatment indicated the involvement of SOD in the tolerance mechanism to paraquat in R. glutinosa. In this study, we examined the isoform-specific response of SOD to oxidative stresses and hormones. Six SOD isoforms were found in the leaf, and they were identified as two MnSODs(named MnSOD I and MnSOD II, in order of increasing mobility), one FeSOD and three Cu/ZnSODs(named Cu/ZnSOD I, Cu/ZnSOD II, and Cu/ZnSOD III, in order of increasing mobility). MnSOD I, MnSOD II, FeSOD, Cu/ZnSOD I, Cu/ZnSOD II, and Cu/ZnSOD III, contributed to 4, 11, 7, 15, 30, and 32% of the total SOD activity, respectively. Total SOD activity levels in the leaf were increased by 4, 24, and 21% by paraquat, salicylic acid(SA), and yeast extract(YE), respectively, but little by ethephon. Six SOD isoforms responded differentially to these stresses and hormones. The activities of all the isoforms were increased by YE and SA except that of MnSOD I which was decreased by SA. The activities of MnSOD I, FeSOD, and CuZnSOD I were increased by paraquat. These results suggest that amelioration of oxidative stresses by SOD is fine-tuned by the differential expression of isoforms in R. glutinosa.

• Tuberculosis and Respiratory Diseases
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• v.42 no.4
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• pp.522-534
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• 1995

Background: In the pathogenesis of acute lung injury induced by lipopolysaccharide(LPS), oxygen radiclls are known to be involved in one part. Superoxide dismutase(SOD) protects oxygen radical-induced tissue damage by dismutating superoxide to hydrogen peroxide. In eukaryotic cells, two forms of SOD exist intracellularly as a cytosolic, dimeric copper/zinc-containing SOD(CuZnSOD) and a mitochondrial, tetrameric manganese-containing SOD(MnSOD). But there has been little information about SOD gene expression and its regulation in pulmonary alveolar macrophages(PAMs). The objective of this study is to evaluate the SOD gene expression induced by LPS and its regulation in PAMs of rat. Method: In Sprague-Dawley rats, PAMs obtained by broncholaveolar lavage were purified by adherence to plastic plate. To study the effect of LPS on the SOD gene expression of PAMs, they were stimulated with different doses of LPS($0.01{\mu}g/ml{\sim}10{\mu}g/ml$) and for different intervals(0, 2, 4, 8, 24hrs). Also for evaluating the level of SOD gene regulation actinomycin D(AD) or cycloheximide(CHX) were added respectively. To assess whether LPS altered SOD mRNA stability, the rate of mRNA decay was determined in control group and LPS-treated group. Total cellular RNA extraction by guanidinium thiocyanate/phenolfchlorofonn method and Northern blot analysis by using a $^{32}P$-labelled rat MnSOD and CuZnSOD cDNAs were performed. Results: The expression of mRNA in MnSOD increased dose-dependently, but not in CuZnSOD. MnSOD mRNA expression peaked at 8 hours after LPS treatment. Upregulation of MnSOD mRNA expression induced by LPS was suppressed by adding AD or CHX respectively. MnSOD mRNA stability was not altered by LPS. Conclusion: These findings show that PAMs of rat could be an important source of SOD in response to LPS, and suggest that their MnSOD mRNA expression may be regulated transcriptionally and require de novo protein synthesis without affecting mRNA stability.

• Journal of Microbiology and Biotechnology
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• v.17 no.8
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• pp.1399-1402
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• 2007

The virulence of superoxide dismutase (SOD) mutants of Vibrio vulnificus, as tested by intraperitoneal injection into mice, decreases in the order of sodC mutant, sodA mutant, and sodB mutant lacking CuZnSOD, MnSOD, and FeSOD, respectively. The survival of SOD mutants under superoxide stress also decreases in the same order. The virulence of soxR mutant, which is unable to induce MnSOD in response to superoxide, is similar to that of the sodA mutant, as the survival of the soxR mutant under superoxide stress is similar to that of the sodA mutant. Consistently, the lowered survival of the soxR mutant is complemented not only with soxR but also with sodA. Thus, the virulence of V. vulnificus is significantly affected by the cellular level of SOD activity, and an increase in SOD level through MnSOD induction by SoxR under superoxide stress is essential for virulence.

• Journal of Microbiology and Biotechnology
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• v.9 no.6
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• pp.732-736
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• 1999

The superoxide dismutase (SOD) in Lactococcus lactis was measured quantitatively and qualitatively under various culture conditions. The L. lactis SOD was induced by oxidative stress. As the concentration of paraquat to produce superoxide radicals increased, the growth of L. lactis decreased with concomitant increase of SOD activity. The SOD activity was found to be growth-phase dependent: when aerobically grown cells entered to the stationary phase, the activity increased gradually until the late stationary phase. From inhibition studies, L. lactis SOD was found to be insensitive to KCN and $H_2O_2$ which are known to inhibit Cu/ZnSOD and FeSOD, respectively. Moreover, as the concentration of manganese in the medium increased, the activity of SOD also increased. These data strongly suggested that L. lactis possessed a single manganese-containing SOD (MnSOD). Finally, a putative sod gene fragment of 510 bp was identified in L. lactis using a polymerase chain reaction (PCR) with degenerate primers designed from the deduced DNA sequences of known SOD genes.

• Journal of Life Science
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• v.16 no.5
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• pp.716-722
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• 2006

Superoxide dismutase (SOD) is physiologically important in regulating cellular homeostasis and apoptotic cell death, and its mutations are the cause of familial amyotrophic lateral sclerosis (FALS). Mitochondrial serine protease HtrA2 has a pro-apoptotic function and has known to be associated with neurodegenerative disorders. To investigate the relationship between genes associated with apoptotic cell death, such as HtrA2 and SOD1, we utilized the pGEX expression system to develop a simple and rapid method for purifying wild-type and ALS-associated mutant SOD1 proteins in a suitable form for biochemical studies. We purified SOD1 and SOD1 (G93A) proteins to approximately 90% purity with relatively high yields (3 mg per liter of culture). Consistent with the result in mammalian cells, SOD1 (G93A) was more insoluble than wild-type SOD1 in E. coli, indicating that research on the aggregate formation of SOD1 may be possible using this pGEX expression system in E. coli. We investigated the HtrA2 serine protease activity on SOD1 to assess the relationship between two proteins. Not only wild-type SOD1 but also ALS-associated mutant SOD1 (G93A) were cleaved by HtrA2, resulting in the production of the 19 kDa and 21 kDa fragments that were specific for anti-SOD1 antibody. Using protein gel electrophoresis and immunoblot assay, we compared the relative molecular masses of thrombin-cleaved GST-SOD1 and HtrA2-cleaved SOD1 fragments and can predict that the HtrA2-cleavage sites within SOD1 are the peptide bonds between leucine 9-lysine 10 (L9-K10) and glutamine 23-lysine 24 (Q23-K24). Our study indicates that SOD1 is one of the substrate for HtrA2, suggesting that both HtrA2 and SOD1 may be important for modulating the HtrA2-SOD1-mediated apopotic cell death that is associated with the pathogenesis of neurodegenerative disorder.

• Asian Pacific Journal of Cancer Prevention
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• v.13 no.6
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• pp.2571-2576
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• 2012

Breast cancer is the first of the most common ten cancers in Iraq. Its etiology is multifactorial, oxidative stress and lipid peroxidation being suggested to play important roles in carcinogenesis. The purpose of this study was to investigate the oxidant-antioxidant status in breast cancer patients, by measuring SOD isoenzyme activities (total SOD, CuZn-SOD, Mn-SOD and EC-SOD) in plasma and breast tumors, and by estimating thiobarbituric reactive substances (TBRS) in tissue homogenates. General increase in total SOD activity was observed in plasma and tissue samples of breast tumors, greater in the malignant when compared to benign group (p<0.05). Mn-SOD showed a significant decrease in tissue malignant samples (p<0.05), and insignificant decrease in plasma malignant samples compared with control and benign samples. Plasma EC-SOD activity in both patient benign and malignant breast tumors demonstrated 3.5% and 22.8% increase, respectively. However, there was a decrease in tissue EC-SOD activity in malignant breast tumors when compared with benign. A similar tendency was noted for TBRS. We suggest that elevated total SOD might reflect a response to oxidative stress, and then may predict a state of excess reactive oxygen species in the carcinogenesis process. If there is proteolytic removal of the heparin binding domain, EC-SOD will lose its affinity for the extracellular matrix and diffuse out of the tissue. This will result in a decreased EC-SOD activity, thus leading to an increase in the steady-state concentration of $O^{2-}$ in this domain, and increase in EC-SOD activity in the extracellular fluid. This might explain the results recorded here concerning the decrease in tissue EC-SOD activity and increase in plasma of breast cancer patients.

• Journal of Life Science
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• v.13 no.5
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• pp.658-667
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• 2003

Antioxidative enzymes (superoxide dismutase; SOD, ascorbate peroxidase; APX, glutathione reductase; GR) play major roles in scavenging mechanism of reactive oxygen species which were involved in various stress conditions including salt. In order to investigate the relation between their growth responses (dry weight) and the changes of antioxidative enzymes activity, salt-tolerant spinach beet having 15cm of shoot length were treated with various salt levels (0, 50, 200, 1000 mM NaCl) for 24 hours. Spinach beet exhibited an increase in the activity of antioxidative enzymes by salt, the maximal activity at 200 mM NaCl and the lowest activity at 50 mM NaCl in 2 hrs. after treatments. As a result of PAGE, it has been confirmed that spinach beet contained 3 isoforms (Fe-SOD, CuZn-SOD and Mn-SOD) of SOD and main isoform was CuZn- SOD form. In case of APX, isoforms of the low molecular weight(No. 7, 8) were showed strong expression especially at 200 and 400 mM NaCl treatment. Meanwhile, GR did not show specific pattern of isoforms among the salt treatments. Especially, in case of 50 mM treatment, plant showed the lowest activity of SOD with the best growth, a low enzyme activity was induced by inactivation of the Mn-SOD. Therefore, we suggested that the decrease of SOD activity at a low salt level (50 mM NaCl) or the increase of enzyme activity at a high salt level (200 mM NaCl) may be related to expression of the Mn-SOD isoform. These antioxidative enzymes showed the increase of activity in a short time by salt addition. So, it is considered that spinach beet copes effectively with a stressful condition such as salt by operating effective antioxidative defense mechanism rapidly under high salt level.