Publications (64)131.63 Total impact
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Article: Oxidative damage of DNA induced by the reaction of methylglyoxal with lysine in the presence of ferritin.
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ABSTRACT: Methylglyoxal (MG) is an endogenous metabolite which is present in increased concentrations in diabetics and reacts with amino acids to form advanced glycation end products. In this study, we investigated whether ferritin enhances DNA cleavage by the reaction of MG with lysine. When plasmid DNA was incubated with MG and lysine in the presence of ferritin, DNA strand breakage was increased in a dose-dependent manner. The ferritin/MG/lysine system-mediated DNA cleavage was significantly inhibited by reactive oxygen species (ROS) scavengers. These results indicated that ROS might participate in the ferritin/MG/lysine system-mediated DNA cleavage. Incubation of ferritin with MG and lysine resulted in a time-dependent release of iron ions from the protein molecules. Our data suggest that DNA cleavage caused by the ferritin/MG/lysine system via the generation of ROS by the Fenton-like reaction of free iron ions released from oxidatively damaged ferritin. [BMB Reports 2013; 46(4): 225-229].BMB reports 04/2013; 46(4):225-9. · 1.72 Impact Factor -
Article: Oxidative modification of neurofilament-L and neuronal cell death induced by the catechol neurotoxin, tetrahydropapaveroline.
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ABSTRACT: Tetrahydropapaveroline (THP), which is an endogenous neurotoxin, has been suspected to be associated with dopaminergic neurotoxicity of L-DOPA. In this study, we examined oxidative modification of neurofilament-L (NF-L) and neuronal cell death induced by THP. When disassembled NF-L was incubated with THP, protein aggregation was increased in a time- and THP dose-dependent manner. The formation of carbonyl compounds and dityrosine were observed in the THP-mediated NF-L aggregates. Radical scavengers reduced THP-mediated NF-L modification. These results suggest that the modification of NF-L by THP may be due to oxidative damage resulting from the generation of reactive oxygen species (ROS). When THP exposed NF-L was subjected to amino acid analysis, glutamate, proline and lysine residues were found to be particularly sensitive. We also investigated the effects of copper ions on THP-mediated NF-L modification. At a low concentration of THP, copper ions enhanced the modification of NF-L. Treatment of C6 astrocyte cells with THP led to a concentration-dependent reduction in cell viability. When these cells were treated with 100μM THP, the levels of ROS increased 3.5 fold compared with control cells. Furthermore, treatment of cells with THP increased NF-L aggregate formation, suggesting the involvement of NF-L modification in THP-induced cell damage.Toxicology Letters 12/2012; · 3.23 Impact Factor -
Article: Oxidative modification of ferritin induced by methylglyoxal.
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ABSTRACT: Methylglyoxal (MG) was identified as an intermediate in non-enzymatic glycation and increased levels were reported in patients with diabetes. In this study, we evaluated the effects of MG on the modification of ferritin. When ferritin was incubated with MG, covalent crosslinking of the protein increased in a time- and MG dose-dependent manner. Reactive oxygen species (ROS) scavengers, N-acetyl-(L)-cysteine and thiourea suppressed the MG-mediated ferritin modification. The formation of dityrosine was observed in MG-mediated ferritin aggregates and ROS scavengers inhibited the formation of dityrosine. During the reaction between ferritin and MG, the generation of ROS was increased as a function of incubation time. These results suggest that ROS may play a role in the modification of ferritin by MG. The reaction between ferritin and MG led to the release of iron ions from the protein. Ferritin exposure to MG resulted in a loss of arginine, histidine and lysine residues. It was assumed that oxidative damage to ferritin caused by MG may induce an increase in the iron content in cells, which is deleterious to cells. This mechanism, in part, may provide an explanation or the deterioration of organs under diabetic conditions. [BMB reports 2012; 45(3): 147-152].BMB reports 03/2012; 45(3):147-52. · 1.72 Impact Factor -
Article: Oxidative modification of ferritin induced by hydrogen peroxide.
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ABSTRACT: Excess free iron generates oxidative stress that may contribute to the pathogenesis of various causes of neurodegenerative diseases. In this study, we assessed the modification of ferritin induced by H(2)O(2). When ferritin was incubated with H(2)O(2), the degradation of ferritin L-chain increased with the H(2)O(2) concentration whereas ferritin H-chain was remained. Free radical scavengers, azide, thiourea, and N-acetyl-(L)-cysteine suppressed the H(2)O(2)-mediated ferritin modification. The iron specific chelator, deferoxamine, effectively prevented H(2)O(2)-mediated ferritin degradation in modified ferritin. The release of iron ions from ferritin was increased in H(2)O(2) concentration-dependent manner. The present results suggest that free radicals may play a role in the modification and iron releasing of ferritin by H(2)O(2). It is assumed that oxidative damage of ferritin by H(2)O(2) may induce the increase of iron content in cells and subsequently lead to the deleterious condition.BMB reports 03/2011; 44(3):165-9. · 1.72 Impact Factor -
Article: Vitamin C increases the apoptosis via up-regulation p53 during cisplatin treatment in human colon cancer cells.
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ABSTRACT: Vitamin C (VC) is an important antioxidant and enzyme co-factor that works by stimulating the immune system and protecting against infections. It is well known that melanoma cells are more susceptible to VC than any other tumor cells. However, the role of VC in the treatment of colon cancer has not been studied. Cisplatin (CDDP) is a DNA damaging agent and is widely used for treating cancer, while the role of p53 in CDDP-induced cell death has been stressed. Using cell growth assays, morphological methods, Western blotting, flow cytometry, and DNA fragmentation analysis, we measured the expression of p53 level involved in the effect of VC on CDDP-induced apoptosis of HCT116, a human colon cancer cell line. CDDP plus VC treatment resulted in significantly increased apoptosis along with upregulation of p53 compared to untreated cells and/or CDDP-treated cells. These results suggest that VC enhanced CDDP sensitivity and apoptosis via upregulation of p53.BMB reports 03/2011; 44(3):211-6. · 1.72 Impact Factor -
Article: Oxidative Modification of Neurofilament-L Induced by Endogenous Neurotoxin, Salsolinol
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ABSTRACT: 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 this study, we examined oxidative modification of neurofilament-L (NF-L) induced by salsolinol. When disassembled NF-L was incubated with salsolinol, the aggregation of protein was increased with the concentration of sasolinol. The formation of carbonyl compound was obtained in salsolinol-mediated NF-L aggregates. This process was protected by free radical scavengers, such as N-acetyl-L-cysteine and glutathione. These results suggest that the aggregation of NF-L is mediated by salsolinol via the generation of free radicals. We also investigated the effects of copper ion on salsolinol-mediated NF-L modification. In the presence of copper ions, salsolinol enhanced the modification of NF-L. We suggest that salsolinol might be related to abnormal aggregation of NF-L which may be involved in the pathogenesis of neurodegenerative diseases and related disorders.Bull. Korean Chem. Soc. 01/2011; 32329. -
Article: Protective effects of carnosine and homocarnosine on ferritin and hydrogen peroxide-mediated DNA damage.
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ABSTRACT: Previous studies have shown that one of the primary causes of increased iron content in the brain may be the release of excess iron from intracellular iron storage molecules such as ferritin. Free iron generates ROS that cause oxidative cell damage. Carnosine and related compounds such as endogenous histidine dipetides have antioxidant activities. We have investigated the protective effects of carnosine and homocarnosine against oxidative damage of DNA induced by reaction of ferritin with H(2)O(2). The results show that carnosine and homocarnosine prevented ferritin/H(2)O(2)-mediated DNA strand breakage. These compounds effectively inhibited ferritin/H(2)O(2)-mediated hydroxyl radical generation and decreased the mutagenicity of DNA induced by the ferritin÷H(2)O(2) reaction. Our results suggest that carnosine and related compounds might have antioxidant effects on DNA under pathophysiological conditions leading to degenerative damage such as neurodegenerative disorders.BMB reports 10/2010; 43(10):683-7. · 1.72 Impact Factor -
Article: Salsolinol, a catechol neurotoxin, induces modification of ferritin: Protection by histidine dipeptide.
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ABSTRACT: 1-Methyl-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline (salsolinol), an endogenous neurotoxin present in the mammalian brain, is known to perform a role in the pathogenesis of Parkinson's disease. In this study, we evaluated oxidative modifications of ferritin occurring after incubation with salsolinol. When ferritin was incubated with salsolinol, protein aggregation increased in a time-dependent manner. Free radical scavengers inhibited this salsolinol-mediated ferritin modification. The exposure of ferritin to salsolinol also results in the generation of protein carbonyl compounds and the formation of dityrosine. The results of this study show that free radicals may perform a pivotal role in salsolinol-mediated ferritin modification. Histidine dipeptides, such as carnosine, have been proposed to function as antioxidant agents in vivo. In this study, we also attempted to determine whether the histidine dipeptides, carnosine and N-acetyl-carnosine, could prevent salsolinol-mediated oxidative modification of ferritin. Our results showed that both carnosine and N-acetyl-carnosine significantly reduced ferritin aggregation. Both compounds effectively inhibited the formation of both carbonyl compounds and dityrosine. These results suggest that carnosine derivatives can, indeed, protect against salsolinol-mediated ferritin modification, as the consequence of free radical-scavenging activity.Environmental toxicology and pharmacology. 05/2010; 29(3):246-51. -
Article: Reaction of ferritin with hydrogen peroxide induces lipid peroxidation.
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ABSTRACT: Lipid peroxidation is known to be an important factor in the pathologies of many diseases associated with oxidative stress. We assessed the lipid peroxidation induced by the reaction of ferritin with H2O2. When linoleic acid micelles or phosphatidyl choline liposomes were incubated with ferritin and H2O2, lipid peroxidation increased in the presence of ferritin and H2O2 in a concentration-dependent manner. The hydroxyl radical scavengers, azide and thiourea, prevented lipid peroxidation induced by the ferritin/H2O2 system. The iron specific chelator desferoxamine also prevented ferritin/H2O2 systemmediated lipid peroxidation. These results demonstrate the possible role of iron in ferritin/H2O2 system-mediated lipid peroxidation. Carnosine is involved in many cellular defense processes, including free radical detoxification. In this study, carnosine, homocarnosine, and anserine were shown to significantly prevent ferritin/H2O2 system-mediated lipid peroxidation and also inhibited the free radical-generation activity of ferritin. These results indicated that carnosine and related compounds may prevent ferritin/H2O2 system-mediated lipid peroxidation via free radical scavenging.BMB reports 03/2010; 43(3):219-24. · 1.72 Impact Factor -
Article: Oxidative Damage of DNA Induced by Ferritin and Hydrogen Peroxide
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ABSTRACT: Excess free iron generates oxidative stress that may contribute to the pathogenesis of various causes of neurodegenera-tive diseases. Previous studies have shown that one of the primary causes of increased brain iron may be the release of excess iron from intracellular iron storage molecules. In this study, we attempted to characterize the oxidative damage of DNA induced by the reaction of ferritin with H2O2. When DNA was incubated with ferritin and H2O2, DNA strand breakage increased in a time-dependent manner. Hydroxyl radical scavengers strongly inhibited the ferritin/H2O2 system-induced DNA cleavage. We investigated the generation of hydroxyl radical in the reaction of ferritin with H2O2 using a chromogen, 2,2'-azinobis-(2-ethylbenzthiazoline-6-sulfonate) (ABTS), which reacted with ·OH to form ABTS + • . The initial rate of ABTS + • formation increased as a function of incubation time. These results suggest that DNA strand breakage is mediated in the reaction of ferritin with H2O2 via the generation of hydroxyl radicals. The iron-specific chelator, deferoxamine, also inhibited DNA cleavage. Spectrophotometric study using a color reagent showed that the release of iron from H2O2-treated ferritin increased in a time-dependent manner. Ferritin enhanced mutation of the lacZ' gene in the presence of H2O2 when measured as a loss of α-comple-mentation. These results indicate that ferritin/H2O2 system-mediated DNA cleavage and mutation may be attributable to hydroxyl radical generation via a Fenton-like reaction of free iron ions released from oxidatively damaged ferritin.Bull. Korean Chem. Soc. 01/2010; 31. -
Article: Ferritin enhances salsolinol-mediated DNA strand breakage: protection by carnosine and related compounds.
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ABSTRACT: Salsolinol is an endogenous neurotoxin, known to be involved in the pathogenesis of neurodegenerative disorders. In this present study, we have attempted to characterize the oxidative damage of DNA induced by the reaction of salsolinol with ferritin. When DNA was incubated with salsolinol and ferritin, DNA strand breakage occurred. Hydroxyl radical scavengers and catalase reduced salsolinol/ferritin system-mediated DNA cleavage, whereas Cu,Zn-superoxide dismutase did not inhibit DNA cleavage. The reaction of salsolinol with ferritin resulted in a time-dependent increase in the release of free iron ions. A strong iron chelator, ferrozine, effectively inhibited the salsolinol/ferritin system-mediated DNA cleavage. Ferritin enhanced a mutation of the lacZ' gene in the presence of salsolinol when measured as a loss of alpha-complementation. These results indicate that salsolinol/ferritin system-mediated DNA cleavage and mutation may be attributable to hydroxyl radical generation via the Fenton-like reaction of free iron ions released from oxidatively damaged ferritin. The endogenous dipeptides, carnosine and related compounds, are naturally occurring compounds with a multiplicity of neuroprotective properties. Carnosine, homocarnosine and anserine significantly inhibited salsolinol/ferritin system-mediated DNA strand breakage and mutation. These results indicate that carnosine and related compounds effectively suppressed the salsolinol/ferritin system-mediated DNA strand breakage via hydroxyl radical scavenging.Toxicology Letters 08/2009; 188(1):20-5. · 3.23 Impact Factor -
Article: Transduced HSP27 protein protects neuronal cell death by enhancing FALS-associated SOD1 mutant activity.
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ABSTRACT: Familial Amyotrophic lateral sclerosis (FALS) is a progressive neurodegenetative disorder induced by mutations of the SOD1 gene. Heat shock protein 27 (HSP27) is well-defined as a stress-inducible protein, however the its role in ALS protection has not yet been established. To investigate the role HSP27 may have in SOD1 mutant-mediated apoptosis, human SOD1 or HSP27 genes were fused with a PEP-1 peptide in a bacterial expression vector to produce a genetic in-frame fusion protein, which was then transduced into cells. We found the purified PEP-1-HSP27 fusion proteins can be transduced efficiently into neuronal cells and protect against cell death by enhancing mutant SOD1 activity. Moreover, transduced PEP-1-HSP27 efficiently prevents protein aggregation produced by oxidative stress. These results suggest that transduced HSP27 fusion protein may be explored as a potential therapeutic agent for FALS patients.BMB reports 04/2009; 42(3):136-41. · 1.72 Impact Factor -
Article: Acrolein, the toxic endogenous aldehyde, induces neurofilament-L aggregation.
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ABSTRACT: Acrolein is a highly reactive by product of lipid peroxidation and individuals with neurodegenerative disorders have been shown to contain elevated concentrations of this molecule in the brain. In the present study, we examined the pattern of neurofilament-L (NF-L) modification elicited by acrolein. When NF-L was incubated with acrolein, protein aggregation occurred in a acrolein concentration-dependent manner. Exposure of NF-L to acrolein also led to the generation of protein carbonyl compounds. Through the addition of free radical scavengers we observed a significant decrease in acrolein-mediated NF-L aggregation. These results indicate that free radicals may be involved in the modification of NF-L by acrolein. In addition, dityrosine crosslink formation was observed in acrolein-mediated NF-L aggregates and these aggregates displayed thioflavin T reactivity, reminiscent of amyloid. This study suggests that acrolein-mediated NF-L aggregation might be closely related to oxidative reactions, thus these reactions may play a critical role in neurodegenerative diseases.BMB reports 10/2008; 41(9):635-9. · 1.72 Impact Factor -
Article: Transduction of familial amyotrophic lateral sclerosis-related mutant PEP-1-SOD proteins into neuronal cells.
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ABSTRACT: Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disorder characterized by the selective death of motor neurons. Mutations in the SOD1 gene are responsible for a familial form of ALS (FALS). Although many studies suggest that mutant SOD1 proteins are cytotoxic, the mechanism is not fully understood. To investigate the role of mutant SOD1 in FALS, human SOD1 genes were fused with a PEP-1 peptide in a bacterial expression vector to produce in-frame PEP-1-SOD fusion proteins (wild type and mutants). The expressed and purified PEP-1-SOD fusion proteins were efficiently transduced into neuronal cells. Neurones harboring the A4V, G93A, G85R, and D90A mutants of PEP-1-SOD were more vulnerable to oxidative stress induced by paraquat than those harboring wild-type proteins. Moreover, neurones harboring the mutant SOD proteins had lower heat shock protein (Hsp) expression levels than those harboring wild-type SOD. The effects of the transduced SOD1 fusion proteins may provide an explanation for the association of SOD1 with FALS, and Hsps could be candidate agents for the treatment of ALS.Molecules and Cells 03/2008; 25(1):55-63. · 2.18 Impact Factor -
Article: Salsolinol, a tetrahydroisoquinoline catechol neurotoxin, induces human Cu,Zn-superoxidie dismutase modificaiton.
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ABSTRACT: 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 Parkinsonos 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 salsolinolmediated 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.Journal of biochemistry and molecular biology 10/2007; 40(5):684-9. · 2.02 Impact Factor -
Article: Protective effects of histidine dipeptides on the modification of neurofilament-L by the cytochrome c/hydrogen peroxide system.
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ABSTRACT: Neurofilament-L (NF-L) is a major element of the neuronal cytoskeleton and is essential for neuronal survival. Moreover, abnormalities in NF-L result in neurodegenerative disorders. Carnosine and the related endogeneous histidine dipeptides prevent protein modifications such as oxidation and glycation. In the present study, we investigated whether histidine dipeptides, carnosine, homocarnosine, or anserine protect NF-L against oxidative modification during reaction between cytochrome c and H(2)O(2). Carnosine, homocarnosine and anserine all prevented cytochrome c/H(2)O(2)-mediated NF-L aggregation. In addition, these compounds also effectively inhibited the formation of dityrosine, and this inhibition was found to be associated with the reduced formations of oxidatively modified proteins. Our results suggest that carnosine and histidine dipeptides have antioxidant effects on brain proteins under pathophysiological conditions leading to degenerative damage, such as, those caused by neurodegenerative disorders.Journal of biochemistry and molecular biology 02/2007; 40(1):125-9. · 2.02 Impact Factor -
Article: Oxidative modification of cytochrome c by hydrogen peroxide.
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ABSTRACT: Oxidative alteration of mitochondrial cytochrome c has been linked to disease and is one of the causes of pro-apoptotic events. We have investigated the modification of cytochrome c by H2O2. When cytochrome c was incubated with H2O2, oligomerization of the protein increased and the formation of carbonyl derivatives and dityrosine was stimulated. Radical scavengers prevented these effects suggesting that free radicals are implicated in the H2O2-mediated oligomerization. Oligomerization was significantly inhibited by the iron chelator, deferoxamine. During incubation of deoxyribose with cytochrome c and H2O2, damage to the deoxyribose occurred in parallel with the release of iron from cytochrome c. When cytochrome c that had been exposed to H2O2 was analyzed by amino acid analysis, the tyrosine, histidine and methionine residues proved to be particularly sensitive. These results suggest that H2O2-mediated cytochrome c oligomerization is due to oxidative damage resulting from free radicals generated by a combination of the peroxidase activity of cytochrome c and the Fenton reaction of free iron released from the oxidatively-damaged protein.Molecules and Cells 11/2006; 22(2):220-7. · 2.18 Impact Factor -
Article: PEP-1-SOD fusion protein efficiently protects against paraquat-induced dopaminergic neuron damage in a Parkinson disease mouse model.
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ABSTRACT: Parkinson disease (PD) is a common neurodegenerative disorder characterized by the progressive loss of dopaminergic neurons in the substantia nigra (SN). However, the mechanism of the pathology of PD still remains poorly understood. Because the administration of the herbicide paraquat triggers selective dopaminergic neuronal cell death, exposure of mice to this herbicide is one valuable model for studying the pathological aspects of PD. In this study, we investigated the protective effects of PEP-1-SOD in vitro and in vivo under exposure to the herbicide paraquat. The viability of neuronal cells treated with paraquat was markedly increased by transduced PEP-1-SOD. When the PEP-1-SOD fusion protein was injected intraperitoneally into mice, a completely protective effect against dopaminergic neuronal cell death in the SN was observed. This protective effect was synergistically increased when the PEP-1-SOD was cotransduced with Tat-alpha-synuclein. These results suggest that PEP-1-SOD provides a strategy for therapeutic delivery in various human diseases related to reactive oxygen species, including PD.Free Radical Biology and Medicine 11/2006; 41(7):1058-68. · 5.42 Impact Factor -
Article: Oxidative damage of DNA induced by the cytochrome C and hydrogen peroxide system.
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ABSTRACT: To elaborate the peroxidase activity of cytochrome c in the generation of free radicals from H2O2, the mechanism of DNA cleavage mediated by the cytochrome c/H2O2 system was investigated. When plasmid DNA was incubated with cytochrome c and H2O2, the cleavage of DNA was proportional to the cytochrome c and H2O2 concentrations. Radical scavengers, such as azide, mannitol, and ethanol, significantly inhibited the cytochrome c/H2O2 system-mediated DNA cleavage. These results indicated that free radicals might participate in the DNA cleavage by the cytochrome c and H2O2 system. Incubation of cytochrome c with H2O2 resulted in a time-dependent release of iron ions from the cytochrome c molecule. During the incubation of deoxyribose with cytochrome c and H2O2, the damage to deoxyribose increased in a time-dependent manner, suggesting that the released iron ions may participate in a Fenton-like reaction to produce dOH radicals that may cause the DNA cleavage. Evidence that the iron-specific chelator, desferoxamine (DFX), prevented the DNA cleavage induced by the cytochrome c/H2O2 system supports this mechanism. Thus we suggest that DNA cleavage is mediated via the generation of dOH by a combination of the peroxidase reaction of cytochrome c and the Fenton-like reaction of free iron ions released from oxidatively damaged cytochrome c in the cytochrome c/H2O2 system.Journal of biochemistry and molecular biology 08/2006; 39(4):452-6. · 2.02 Impact Factor -
Article: Transduced Tat-alpha-synuclein protects against oxidative stress in vitro and in vivo.
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ABSTRACT: Parkinson's disease (PD) is a common neurodegenerative disorder and is characterized by the progressive loss of dopaminergic neurons in the substantia nigra. Although many studies showed that the aggregation of alpha-synuclein might be involved in the pathogenesis of PD, its protective properties against oxidative stress remain to be elucidated. In this study, human wild type and mutant alpha-synuclein genes were fused with a gene fragment encoding the nine amino acid transactivator of transcription (Tat) protein transduction domain of HIV-1 in a bacterial expression vector to produce a genetic in-frame WT Tat-alpha-synuclein (wild type) and mutant Tat-alpha-synucleins (mutants; A30P and A53T), respectively, and we investigated the protective effects of wild type and mutant Tat-alpha-synucleins in vitro and in vivo. WT Tat-alpha-synuclein rapidly transduced into an astrocyte cells and protected the cells against paraquat induced cell death. However, mutant Tat-alpha-synucleins did not protect at all. In the mice models exposed to the herbicide paraquat, the WT Tat-alpha-synuclein completely protected against dopaminergic neuronal cell death, whereas mutants failed in protecting against oxidative stress. We found that these protective effects were characterized by increasing the expression level of heat shock protein 70 (HSP70) in the neuronal cells and this expression level was dependent on the concentration of transduced WT Tat-alpha-synuclein. These results suggest that transduced Tat-alpha-synuclein might protect cell death from oxidative stress by increasing the expression level of HSP70 in vitro and in vivo and this may be of potential therapeutic benefit in the pathogenesis of PD.Journal of biochemistry and molecular biology 06/2006; 39(3):253-62. · 2.02 Impact Factor
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Institutions
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1732–2012
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Cheongju University
Tyundyu, North Chungcheong, South Korea
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2002–2009
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Hallym University
- • Department of Biomedical Science
- • College of Medicine
Seoul, Seoul, South Korea
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