• Title, Summary, Keyword: CuZn-SOD

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Salsolinol, a Tetrahydroisoquinoline Catechol Neurotoxin, Induces Human Cu,Zn-superoxidie Dismutase Modificaiton

  • Kang, Jung-Hoon
    • BMB Reports
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    • v.40 no.5
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    • pp.684-689
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    • 2007
  • The endogenous neurotoxin, 1-methyl-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline (salsolinol), has been considered a potential causative factor for the pathogenesis of Parkinson's disease (PD). In the present study, we examined the pattern of human Cu,Zn-superoxide dismutase (SOD) modification elicited by salsolinol. When Cu,Zn-SOD was incubated with salsolinol, some protein fragmentation and some higher molecular weight aggregates were occurred. Salsolinol led to inactivation of Cu,Zn-SOD in a concentration-dependent manner. Free radical scavengers and catalase inhibited the salsolinol-mediated Cu,Zn-SOD modificaiton. Exposure of Cu,Zn-SOD to salsolinol led also to the generation of protein carbonyl compounds. The deoxyribose assay showed that hydroxyl radicals were generated during the oxidation of salsolinol in the presence of Cu,Zn-SOD. Therefore, the results indicate that free radical may play a role in the modification and inactivation of Cu,Zn-SOD by salsolinol.

Copper, Zinc-Superoxide Dismutase (Cu/Zn SOD) Gene During Embryogenesis of Bombyx mori: Molecular Cloning, Characterization and Expression

  • Hong, Sun-Mee;Kang, Seok-Woo;Goo, Tae-Won;Kim, Nam-Soon;Lee, Jin-Sung;Nho, Si-Kab
    • International Journal of Industrial Entomology
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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.

Expression of a Cu-Zn Superoxide Dismutase Gene in Response to Stresses and Phytohormones in Rehmannia Glutinosa

  • Park, Myoung-Ryoul;Ryu, Sang-Soo;Yoo, Nam-Hee;Yu, Chang-Yeon;Yun, Song-Joong
    • Korean Journal of Medicinal Crop Science
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    • v.13 no.5
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    • pp.270-275
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    • 2005
  • Superoxide dismutases (SOD) are metalloenzymes that convert $O_2^-\;to\;H_2O_2$. Rehmannia glutinosa is highly tolerant to paraquat-induced oxidative stress. The primary objective of this study was to characterize regulation of SOD gene expression in R. glutinosa in response to oxidative stresses and hormones. A full-length putative SOD clone (RgCu-ZnSOD1) was isolated from the leaf cDNA library of R. glutinosa using an expressed sequence tag clone as a probe. RgCu-ZnSOD1 cDNA is 777 bp in length and contains an open reading frame for a polypeptide consisted of 152 amino acid residues. The deduced amino acid sequence of the clone shows highest sequence similarity to the cytosolic Cu-ZnSODs. The two to three major bands with several minor ones on the Southern blots indicate that RgCu-ZnSOD1 is a member of a small multi-gene family. RgCuZnSOD1 mRNA was constitutively expressed in the leaf, flower and root. The expression of RgCu-ZnSOD1 mRNA was increased about 20% by wounding and paraquat, but decreased over 50% by ethylene and $GA_3$. This result indicates that the RgCu-ZnSOD1 expression is regulated differentially by different stresses and phytohormones at the transcription level. The RgCu-ZnSOD1 sequence and information on its regulation will be useful in investigating the role of SOD in the paraquat tolerance of R. glutinosa.

Isoform-Specific Responses of Superoxide Dismutase to Oxidative Stresses and Hormones in Parquat-Tolerant Rehmannia glutinosa

  • Jamal, Arshad;Yoo, Nam-Hee;Yun, Song-Joong
    • 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.

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Modification and inactivation of Cu,Zn-superoxide dismutase by the lipid peroxidation product, acrolein

  • Kang, Jung Hoon
    • BMB Reports
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    • v.46 no.11
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    • pp.555-560
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    • 2013
  • Acrolein is the most reactive aldehydic product of lipid peroxidation and is found to be elevated in the brain when oxidative stress is high. The effects of acrolein on the structure and function of human Cu,Zn-superoxide dismutase (SOD) were examined. When Cu,Zn-SOD was incubated with acrolein, the covalent crosslinking of the protein was increased, and the loss of enzymatic activity was increased in a dose-dependent manner. Reactive oxygen species (ROS) scavengers and copper chelators inhibited the acrolein-mediated Cu,Zn-SOD modification and the formation of carbonyl compound. The present study shows that ROS may play a critical role in acrolein-induced Cu,Zn-SOD modification and inactivation. When Cu,Zn-SOD that has been exposed to acrolein was subsequently analyzed by amino acid analysis, serine, histidine, arginine, threonine and lysine residues were particularly sensitive. It is suggested that the modification and inactivation of Cu,Zn-SOD by acrolein could be produced by more oxidative cell environments.

Modification of Cu,Zn-Superoxide Dismutase by Oxidized Catecholamines

  • Kang, Jung-Hoon
    • BMB Reports
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    • v.37 no.3
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    • pp.325-329
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    • 2004
  • Oxidation of catecholamines may contribute to the pathogenesis of Parkinson's disease (PD). The effect of the oxidized products of catecholamines on the modification of Cu,Zn-superoxide dismutase (SOD) was investigated. When Cu,Zn-SOD was incubated with the oxidized 3,4-dihydroxyphenylalanine (DOPA) or dopamine, the protein was induced to be aggregated. The deoxyribose assay showed that hydroxyl radicals were generated during the oxidation of catecholamines in the presence of copper ion. Radical scavengers, azide, N-acetylcysteine, and catalase inhibited the oxidized catecholamine-mediated Cu,Zn-SOD aggregation. Therefore, the results indicate that free radicals may play a role in the aggregation of Cu,Zn-SOD. When Cu,Zn-SOD that had been exposed to catecholamines was subsequently analyzed by an amino acid analysis, the glycine and histidine residues were particularly sensitive. These results suggest that the modification of Cu,Zn-SOD by oxidized catecholamines might induce the perturbation of cellular antioxidant systems and led to a deleterious cell condition.

DNA Cleavage Induced by the Reaction of Salsolinol with Cu,Zn-Superoxide Dismutase

  • Kang, Jung-Hoon
    • Bulletin of the Korean Chemical Society
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    • v.28 no.12
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    • pp.2329-2332
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    • 2007
  • Salsolinol, endogenous neurotoxin, is known to be involved in the pathogenesis of Parkinson's disease (PD). In the present study, we have investigated the oxidative damage of DNA induced by the reaction of salsolinol with Cu,Zn-SOD. When plasmid DNA incubated with salsolinol and Cu,Zn-SOD, DNA cleavage was proportional to the concentrations of salsolinol and Cu,Zn-SOD. The salsolinol/Cu,Zn-SOD system-mediated DNA cleavage was significantly inhibited by radical scavengers such as mannitol, ethanol and thiourea. These results indicated that free radicals might participate in DNA cleavage by the salsolinol/Cu,Zn-SOD system. Spectrophotometric study using a thiobarbituric acid showed that hydroxyl radical formation was proportional to the concentration of salsolinol and was inhibited by radical scavengers. These results indicated that hydroxyl radical generated in the reaction of salsolinol with Cu,Zn-SOD was implicated in the DNA cleavage. Catalase and copper chelators inhibited DNA cleavage and the production of hydroxyl radicals. These results suggest that DNA cleavage is mediated in the reaction of salsolinol with Cu,Zn-SOD via the generation of hydroxyl radical by a combination of the oxidation reaction of salsolinol and Fenton-like reaction of free copper ions released from oxidatively damaged SOD.

Identification and Characterization of SOD Isoenzymes in Acanthopanax koreanum Plants (섬오갈피나무에서 SOD Isoenzyme의 식별 및 특성규명)

  • 오순자;박영철;김응식;고석찬
    • 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$0^{\circ}C$.

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Molecular Phylogenetic Analyses of Scyliorhinus torazame (Carcharhiniformes) Inferred from Cu,Zn Superoxide Dismutase (두툽상어(Scyliorhinus torazame) Cu,Zn-SOD의 분자 계통학적 분석)

  • Kim, Keun-Yong;Nam, Yoon Kwon
    • Korean Journal of Ichthyology
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    • v.18 no.4
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    • pp.293-299
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    • 2006
  • Copper,zinc superoxide dismutase (Cu,Zn-SOD) plays a key role to the first antioxidant defense system against oxidative stress in diverse aerobic organisms. Due to the housekeeping action of Cu,Zn-SOD, it was reported that the structure and function have been conserved during evolution. In this study Cu,Zn-SOD from cloudy catshark Scyliorhinus torazame was subjected to phylogenetic analyses to know its evolutionary relationship in the vertebrate lineage. Molecular phylogenetic trees inferred by NJ, MP, ML and/or Bayesian analyses showed two shark species, Prionace glauca and S. torazame grouped together with high statistical supports. In general, they placed at the separated position from bony vertebrates. Thereafter, bony vertebrates composed of teleosts and birds/mammals (amniotes) formed a monophyletic group. Each teleost and amniote clade was also supported by relatively high statistical values. These phylogenetic relationships are well congruent with the phylogenetic hypothesis of the ancestral position of cartilaginous fishes to bony vertebrates.

Inactivation of Copper, Zinc Superoxide Dismutase by the Lipid Peroxidation Products Malondialdehyde and 4-Hydroxynonenal

  • Koh, Young-Ho;Yoon, Seon-Joo;Park, Jeen-Woo
    • BMB Reports
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    • v.32 no.5
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    • pp.440-444
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    • 1999
  • Membrane lipid peroxidation processes yield reactive aldehydes that may react with copper,zinc superoxide dismutase (Cu,Zn SOD), one of the key antioxidant enzymes against oxidative stress. We investigated this possibility and found that exposing Cu,Zn SOD to malondialdehyde (MDA) or 4-hydroxynonenal (HNE) caused the loss of dismutase activity, cross-linking of peptides, and an increase in protein oxidation, reflected by the increased level of carbonyl groups. When Cu,Zn SOD that had been exposed to MDA or HNE was subsequently analyzed by amino acid analysis, histidine content was found to be significantly lost. Both MDA-and HNE-treated Cu,Zn SOD were resistant to proteolysis, which may imply that damaged proteins exist in vivo for a longer period of time than the native enzyme. The lipid peroxidation-mediated damage to Cu,Zn SOD may result in the perturbation of cellular antioxidant defense mechanisms, and subsequently lead to a pro-oxidant condition.

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