• International Journal of Industrial Entomology and Biomaterials
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• v.13 no.1
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• pp.23-30
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• 2006

BmCu/Zn SOD was isolated from early embryo of Bombyx mori using microarray analysis. The BmCu/Zn SOD gene was observed during the early embryonic stage with the strongest signal found at the unfertilizaion, fertilization and blastoderm stages. The BmCu/Zn SOD gene encodes a protein of 154 amino acids with a calculated Mr of 15 kDa. The deduced amino acid sequence of BmCu/Zn SOD indicated that the residues that form on the Cu/Zn binding site are conserved and that the sequence is a 60% identity to that of M. domestica. In a phylogenetic tree, Bm SOD was also close to Drosophila SODs rather than other insect SODs. The BmCu/Zn SOD gene exists as a single copy in the genome. Transcripts of BmCu/Zn SOD cDNA were identified by northern blot analysis. The expression of the BmCu/Zn SOD gene was observed weakly in most of larvae, pre-pupae, pupae and adult tissues. Also, the BmCu/Zn SOD gene was observed in early embryonic stage. Although the roles of SODs remains to be further elucidated, the high expression of BmCu/Zn SOD gene at before 24 h post fertilization suggests that this gene is of general importance during early embryogenesis in the Bombyx mod.

• Korean Journal of Microbiology
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• v.30 no.6
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• pp.460-465
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• 1992

The effect of PSOD expression on lacZ-sodP fusion (pYK4) was explored in Escherichia coli sodA sodB mutants (QC774) under oxidative stress. In this system, although .betha.-galactosidase activity was not fully induced by isopropyl-1-thio-.betha.-galactosidase (IPTG) and was inhibited by glucose, functional PSOD was under lacZ promotor control and was induced by IPTC, lactose, PQ and copper isons, finally, the results show that higher PSOD expression leel was consistently importnat in defending against superoxide radicals.

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2003.10a
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• pp.71-74
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• 2003

Superoxide dismutase (SOD), one of the essential element of the antioxidant defense system, mainly removes $O^{-10}$ $_2$ and also prevents $O^{-10}$ $_2$ mediated reduction of iron and subsequent OH$^{-10}$ generation, which is highly toxic to the organism. Of these SOD enzymes, Cu, Zn-containing SOD (SODI) is an important component of the antioxidant defense system in eucaryotic cells. The SODI enzyme binds one copper and one zinc ion and displays the Greek Key $\beta$-barrel fuld. (omitted)

• Plant Resources
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• v.7 no.3
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• pp.163-169
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• 2004

To investigate the defense mechanism against the abiotic stress, a cDNA clone encoding a CuZn superoxide dismutase (CuZnSOD) protein was isolated from a cDNA library prepared from tabroot mRNAs of Codonopsis lanceolata. The eDNA, designated ClSODCc, is 799 nucleotides long and has an open reading frame of 459 bp with a deduced amino acid sequence of 152 residues. The deduced amino acid sequence of ClSODCc matched to the previously reported CuZnSODs. Consensus amino acid residues (His-45, -47, -62, -70, -79, -119 and Asp-82) were involved in Cu-, Cu/Zn-, and Zn- binding ligands. The deduced amino acid sequence of ClSODCc showed high homologies (82％-86％) regardless of species. Expression of ClSODCc by oxidative stress was increased up to 1 h after treatment and declined gradually. Much earlier and stronger expression of ClSODCc was observed in the cold stress treatment.

• Tuberculosis and Respiratory Diseases
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• v.41 no.3
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• pp.215-221
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• 1994

Background: It is well known that oxygen free radicals(OFR) play a vital role in the various type of acute lung injury. Among various antioxidant defense mechanisms, the superoxide dismutases(SOD) are thought to be the first line of antioxidant defense by catalyzing the dismutation of two superoxide radicals to yield hydrogen peroxide and oxygen. Eukaryotic cells contain two types of intracellular SOD : cytosolic, dimeric copper/zinc- containing enzyme(CuZnSOD) and mitochondrial, tetrameric manganese-containing enzyme(MnSOD). The purpose of this study is to evaluate the time-dependent gene expression of MnSOD and CuZnSOD in the endotoxin-treated rats, and to compare with the manifestations of LPS-induced acute lung injury in rats. Methods: Total RNA from rat lung was isolated using single step phenol extraction 0, 1, 2, 4, 6, 12, 18, 24 hours after E. coli endotoxin injection(n=3, respectively). RNA was separated by formaldehyde-containing 1.2% agarose gels elctrophoresis, transblotted, baked, prehybridized, and hybridized with $^{32}P$-labeled cDNA probes for rat MnSOD and CuZnSOD, which were kindly donated by Dr. Ho(Duke University, Durham, NC, USA). The probes were labeled by nick translation. Blots were washed and autoradiography were quantitated using laser densitometry. Equivalent amounts of total RNA/gel were assessed by monitoring 28S and 18S rRNA. Results: Endotoxin caused a rise in steady-state MnSOD mRNA levels by 4h with peak mRNA accumulation by 6h. Continued MnSOD mRNA expression was observed at 12h. CuZnSOD mRNA expression was observed from 1h to 24h with peak levels by 18h. Conclusion: These results suggest that SOD palys an important defensive role in the endotoxin-induced acute lung injury in rats.

• Tuberculosis and Respiratory Diseases
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• v.50 no.5
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• pp.579-590
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• 2001

Background : The aging process may be induced, at least in part, by reactive oxygen species(ROS). It has been thought that the lung could be a good source of ROS because it has a high oxygen tension. In the present study, we invetigated the inducibility of the first and last lines against oxidative stress, superoxide dismutases(CujZn-SOD and Mn-SOD) as a scavenger of ${O_2}^-\;{\cdot}$ and metallothionein(MT) as a scavenger of $OH{\cdot}$, respectively, in mouse lungs with age. Methods : Oxidative stress was induced by paraquat, an intracellular superoxide generator, at 1, 4, 8, and 12 months of age and then SODs and MT mRNAs were determined by RT-PCR method. Results : The steady-state level of Mn-SOD mRNA increased from 1 to 8 months but decreased thereafter. However, Mn-SOD mRNA was not induced by paraquat after 1 month. On the other hand, there was no change in the steady-state level of Cu/Zn-SOD mRNA, which decreased abruptly at 12 months of age. Additionally, Cu/Zn-SOD mRNA was not induced by paraquat at any age. There was no change in the steady-state level of MT mRNA with age whereas its inducibility by paraquat was intact at all ages. Conclusion : These results indicate that lack of induction of SODs with age may be one of the causative factors in the aging process while induction of MT may play an important role in the defense against oxidative stress. It is therefore implicated that the tissue antioxidant/prooxidant balance could be one of determinants of mean life span.

• International Journal of Industrial Entomology and Biomaterials
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• v.10 no.1
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• pp.73-77
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• 2005

A Cu,Zn superoxide dismutase (SOD1) cDNA was cloned from the spider, Araneus ventricosus. The A. ventricosus SOD1 (AvSOD1) cDNA contains an open reading frame of 495 bp encoding 165 amino acid polypeptide with a predicted molecular mass of 17,114 Da and pI of 6.55, and possesses the typical metal binding ligands of six histidines and one aspartic acid common to SOD1s. The deduced amino acid sequence of the AvSOD1 cDNA showed $51\%$ identity to Ceratitis capitata SOD1, and $50\%$ to SOD1 sequences of both Drosophila melanogaster and Chymomyza amoena. Northern blot analysis revealed the presence of AvSOD1 transcripts in all tissues examined.

• Proceedings of the Microbiological Society of Korea Conference
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• 2004.05a
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• pp.47-50
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• 2004

The defenses against free radical damage include specialized repair enzymes that correct oxidative damages in DNA, and detoxification systems such as superoxide dismutases. These defenses may be coordinated genetically as global responses. We hypothesized that the expression of the SOD and the DNA repair genes would inhibit DNA damage under oxidative stress. Therefore, the protection of E. coli mutants deficient in SOD and DNA repair genes $(sod^-\;xth^-\;and\;nfo^-)$ was demonstrated by transforming the mutant strain with a plasmid pYK9 which encoded Photobacterium leiognathi CuZnSOD and human AP endonuclease. The results show that survival rates were increased in $sod^+\;xth^-\;nfo^+$ cells compared to $sod^-\;xth^-\;ap^+,\;sod^-\;xth^-\;ap^-,\;and\;sod^+\;xth^-\;ap^-$ cells under oxidative stress generated from 0.1 mM Paraquat or 3 mM $H_2O_2$. The data suggested that, at least, SOD and DNA repair enzymes may have collaborate protection and repair of the damaged DNA. Additionally, both enzymes are required for protection against free radicals.

• Journal of Ginseng Research
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• v.23 no.1 s.53
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• pp.44-49
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• 1999

Cu/Zn superoxide dismutase (SOD1) is a protective enzyme responsible for the dismutat ion of superoxide radicals within the cell by converting superoxide radicals to oxygen and hydrogen peroxide, which is in turn changed to oxygen and water by catalase. Previously, we reported that the panaxadiol (PD) and its ginsenoside $Rb_2$ induced the expression of SOD1 gene through AP2 binding site and its induction. Here, we examined the effect of subfractions of panaxadiol ginsenosides, which were extracted from different parts of ginseng root that possess various ratios of panaxadiol to panaxatriol, on the induction of SOD1 gene expression. To explore this possibility, the upstream regulatory region of SOD1 was linked to the chloramphenicol acetyl transferase (CAT) structural gene and introduced into human hepatoma HepG2 cells. We observed that the transcriptional activation of SOD1 was proportional to the contents ratio of panaxadiol ginsensides. Consistent with this results, the total extract portion prepared from the finely-hairy root, which contains the higher ratio of panaxadiol to panaxatriol about 2.6, increased the SODl transcription about 3 fold. This results suggest that the panaxadiol fraction could induce the SOD1 and total extract of the ginseng finely-hairy root would be a useful material as a functional food for the SOD1 inducer.

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2003.10a
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• pp.66-70
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• 2003

The first line of antioxidant defense against reactive oxygen species includes the enzymatic activity of the superoxide dismutase (SOD) that catalyzes the disproportionation of superoxide to hydrogen peroxide and water. The SOD mainly removes highly toxic $O_2$$^{[-10]}$ and also prevents $O_2$$^{[-10]}$ mediated reduction of iron and subsequent OH$^{[-10]}$ generation. Along with an interest in SOD as a first line of defense against damage mediated by the superoxide anion, the SOD1 enzyme has been subjected to investigation in the molecular and cellular level. (omitted)