• Nutrition Research and Practice
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• v.4 no.2
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• pp.114-120
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• 2010

The effects of grape seeds extract and grape peels extract prepared from grape pomace on the activity of antioxidant enzymes, degree of lipid peroxidation in serum and liver tissue were investigated in rabbits fed on high cholesterol diet. New Zealand white rabbits were divided as follows ; 1) NOR (normal group); 2) CHOL (cholesterol group); 3) GSH (cholesterol + grape seed extract group); 4) GPE (cholesterol + grape peel extract); 5) GSP (cholesterol + grape seed powder); 6) GPP (cholesterol + grape peel powder); 7) GE (cholesterol + grape seed and peel extract); 8) GP (cholesterol + grape seed and peel powder). Eight groups of rabbits were studied for 8 weeks. At the end of the experimental period, rabbits were sacrificed and the liver tissue were removed. Then, GSH, GPx, GST, CAT and MDA in the liver were measured. In liver tissues, total glutathione contents (GSH), glutathione peroxidase (GPx) and catalase (CAT) activity, which was significantly higher by grape seed extract supplementation. The level of malondialdehyde (MDA) was lower in the serum of rabbits fed grape seed extract or grape peel powder plus cholesterol than in the serum of rabbits fed cholesterol alone. It is therefore likely that grape seed extract prepared from grape pomace functioned as antioxidants in vivo, negating the effects of the oxidative stress induced by 1% cholesterol diet. The grape seed extract was found effective in converting the oxidized glutathione into reduced glutathione, and in removing $H_2O_2$ that is created by oxidative stress. The grape peel powder was found to have small influence on reduced glutathione content, CAT and GPX activity, but it increased GST activity in liver tissues, resulting in promoting the combination of lipid peroxide and glutathione (GSH), and further, lowering the formation of lipid peroxide in the serum. Therefore, grape pomace (grape seed extract and grape peel powder) supplementation is considered to activate the antioxidant enzyme system and prevent damage with hypercholesterolemia.

• Journal of Environmental Health Sciences
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• v.23 no.2
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• pp.83-88
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• 1997

To evaluate the effect of bromobenzene pretreatment on the bromobenzene metabolism, the animal group was induced the stage of slight liver damage with 7 times bromobenzene injection every two days (400 mg/kg body wt. i.p.). In the present experimental animal model, the single dose of bromobenzene(400 mg/kg body wt. i.p.) was injected to the bromobenzene-pretreated rats and the hepatic aniline hydroxylase(AH) activity, glutathione(GSH) content and glutathione S-transferase (GST) activity were determined at the intervals of 2, 4, 8, 24 hours throughout 24 hr. The activities of hepatic AH and GST were generally higher in bromobenzene-pretreated rats than those in normal group throughout the whole course of experiment. Furthermore, the decreasing rate of hepatic GSH content was also higher in bromobenzene pretreated rats than in normal rats. Moreover, the value of V$_{max}$ in hepatic GST was higher in bromobenzene pretreated rats than that in the normal rats. In conclusion, these results indicate that the pretreatment of bromobenzene may rather enhance the bromobenzene metabolism.

• Korean Journal of Acupuncture
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• v.20 no.1
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• pp.39-43
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• 2003

Sophorae Flos aqua-acupuncture solution(SFAS) was prepared and tested for the induction of quinone reductase and glutathione S-transferase activities and glutathione. SFAS significantly induced QR activity at the concentrations of $0.5{\times},\;1{\times}\;and\;3{\times}$ in cell culture. However, GST activity in murine Hepa 1c1c7 cells was slightly increased with SFAS. SFAS increased GSH levels.

• Environmental Analysis Health and Toxicology
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• v.24 no.1
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• pp.53-61
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• 2009

사람 기관지상피세포주인 BEAS-2B에 담배연기농축액(CSC)을 처리하여 유도된 1198 세포주는 대조군 세포주인 1799에 비해 현저하게 낮은 glutathione 농도와 낮은 glutamate-cysteine ligase(GCL), glutathione peroxidase(GPx), glucose-6-phosphate dehydrogenase(G6PD), catalase 효소활성을 보였다. 두 세포주를 포도당 존재 하에서 4시간 hypoxia 처리 후 reoxygenation 하면서 시간에 따른 세포의 항산화계 활성을 측정한 결과, 1799 세포주에서는 의미 있는 변화가 관찰되지 않은 반면, 1198 세포주에서는 hypoxia 처리에 의해 glutathione의 농도 및 GSH/GSSG 비와 G6PD 활성이 감소되었고, reoxygenation 기에는 GPx, glutathione reductase(GRd), G6PD, superoxide dismutase 활성이 감소되었다. 그러나 reoxygenation 2시간 이후에는 GRd와 G6PD 활성의 회복이 관찰되었으며, 그 결과 GSH/GSSG 비율이 회복되었다. 이 실험 결과는 CSC가 능력을 현저히 저하시킬 수 있음을 보여준다. Glutathione은 hypoxia-reoxygenation에 의한 산화적 스트레스 하에서 항산화제로서의 역할뿐 아니라, 세포 내 GSH/GSSG 비의 변화를 통해 산화적 스트레스에 대한 항산화계의 적응 반응 여부를 결정하는 중요한 인자로 작용할 것으로 보여진다.

• Development and Reproduction
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• v.10 no.2
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• pp.115-125
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• 2006

The present experiment was performed to confirm the effects of selenium on maturation and viability of mouse oocyte. Maturation of oocytes was observed by microscope, Germinal vesicle breakdown(GVBD) and polar body formation(PB) were confirmed at 2.5, 13 hours after in vitro culture. Viability of oocytes was observed by microscope. Normal and abnormal oocytes were distinguished by morphological change in vitro culture for 72 hours. Glutathione(GSH) content of collected oocytes from individual stage also was measured by glutathione assay using spectrophotometer. The results obtained were as follows; The low concentration of selenium($0.005\;{\mu}g/mL{\sim}0.5\;{\mu}g/mL$) increased the maturation rate of germinal vesicle(GV) oocytes to GVBD and PB oocytes. The high concentration of selenium($5\;{\mu}g/mL$) decreased the maturation rate. The low concentration of selenium increased the viability rate of PB oocytes. The high concentration of selenium did not affect the viability rate. The low concentration of selenium increased the GSH content in PB oocytes. The high concentration of selenium decreased GSH content. GSH content in PB oocyte was much higher than that in GVBD oocyte. The results indicate that the low concentration of selenium increases the maturation rate by helping quality elevation of oocyte and minimizing damages of oxidative stress generated from metabolism process. The low concentration of selenium also increases the viability rate by increasing GSH content.

• Herbal Formula Science
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• v.11 no.2
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• pp.135-146
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• 2003

Objectives : Wolguk-whan has been used as a prescription of natural drug for the treatment of stress digestive system disease. Recently, we reported that Wolguk-whan methnol extract (WGWM) exerted a significant protective effect against oxidative damage to the liver of ICR mice. This study was purposed to investigate the effects of Wolguk-whan water extract (WGWW) on liver injury induced by oxidative stress. Methods : In order to investigate the effects of WGWW on acute liver injury, ICR mice were pretreated with WGWW for 6days, starved for 24hrs, and administerated acetamirtophen(500mg/kg, i.p.). In the liver homogenates, lipid peroxide and glutathione(GSH) levels were measured. In addition, activities of hepatic enzyme, such as catalase, glutathione peroxidase(GSH-Px), glutathione S-transferase(GST) were measured in the hepatic mitochondrial and cytosolic fractions. Results : In vivo administeration of WGWW showed effective inhibition of acetaminophen induced lipid peroxidation, and showed elevations of GSH level, catalase, GSH-Px, GST activities. Conclusions : These results suggested that WGWW might suppress the formation of oxidative metabolites, and prevent acetaminophen induced hepatotoxicity.

• Archives of Pharmacal Research
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• v.28 no.9
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• pp.1065-1072
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• 2005

The nascent thyroglobulin (Tg) multimer molecule, which is generated during the initial fate of Tg in ER, undergoes the rapid reductive depolymerization. In an attempt to determine the depolymerization process, various types of Tg multimers, which were generated from deoxy­cholate-treated/reduced Tg, partially unfolded Tg or partially unfolded/reduced Tg, were subjected to various GSH (reduced glutathione) reducing systems using protein disulfide isomerase (PDI), glutathione reductase (GR), glutaredoxin or thioredoxin reductase. The Tg multimers generated from deoxycholate-treated/reduced Tg were depolymerized readily by the PDI/GSH system, which is consistent with the reductase activity of PDI. The PDI/GSH-induced depolymerization of the Tg multimers, which were generated from either partially unfolded Tg or partially unfolded/reduced Tg, required the simultaneous inclusion of glutathione reductase, which is capable of reducing glutathionylated mixed disulfide (PSSG). This suggests that PSSG was generated during the Tg multimerization stage or its depolymerization stage. In particular, the thioredoxin/thioredoxin reductase system or glutaredoxin system was also effective in depolymerizing the Tg multimers generated from the unfolded Tg. Overall, under the net GSH condition, the depolymerization of Tg multimers might be mediated by PDI, which is assisted by other reductive enzymes, and the mechanism for depolymerizing the Tg multimers differs according to the type of Tg multimer containing different degrees and types of disulfide linkages.

• BMB Reports
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• v.44 no.3
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• pp.170-175
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• 2011

We identified a bovine $B_{12}$ trafficking chaperone bCblC in Bos taurus that showed 88% amino acid sequence identity with a human homologue. The protein bCblC was purified from E. coli by over-expression of the encoding gene. bCblC bound cyanocobalamin (CNCbl), methylcobalamin (MeCbl) and adenosylcobalamin (AdoCbl) in the base-off states and eliminated the upper axial ligands forming aquo/hydroxocobalamin ($OH_2$/OHCbl) under aerobic conditions. A transition of $OH_2$/OHCbl was induced upon binding to bCblC. Interestingly, bCblC-bound $OH_2$/OHCbl did not react with reduced glutathione (GSH), while the reaction of free$OH_2$/OHCbl with GSH resulted in the formation of glutathionylcobalamin (GSCbl) and glutathione disulfide (GSSG). Furthermore we found that bCblC eliminates the GSH ligand of GSCbl forming $OH_2$/OHCbl. The results demonstrated that bCblC is a $B_{12}$ trafficking chaperone that binds cobalamins and protects $OH_2$/OHCbl from GSH, which could be oxidized to GSSG by free $OH_2$/OHCbl.

• Korean Journal of Acupuncture
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• v.20 no.4
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• pp.41-52
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• 2003

Objectives : Circii Herba has been used as a natural drug for the treatment of stress digestive system disease. The aim of this study is to investigate the role of Circii Herba aqua-acupuncture solution (CHAS) in experimental oxidative liver injury. Methods : In order to investigate the effects of CHAS on acute liver injury, male ICR mice were pretreated with CHAS(0.2 ml/mouse/day) at the loci of BL18 and CV12 for 6days, starved for 24hrs, and administerated acetaminophen(500 mg/kg, i.p.). After acetaminophen administeration, mice were sacrificed, and the liver was removed, rinsed with ice-cold $1.15{\%}$ KCI buffer, and homogenized at $4^{\circ}C$. Fractions(fraction Ⅰ, Ⅱ, Ⅲ) were isolated by differential centrifugation. Lipidperoxide, total SH, and glutathione(GSH) levels were measured in the Fraction Ⅰ. In addition, activities of hepatic enzyme, such as catalase, glutathione peroxidase(GSH-Px) were measured in the Fraction Ⅱ, and glutathione S-transferase(GST) was measured in the Fraction Ⅲ. Results : In vivo treatment of CHAS(BL18 and CV12) showed effective inhibition of acetaminophen induced lipid peroxidation, and showed elevations of total SH, GSH level, catalase, GSH-Px, GST activities. Conclusions : These results suggested that CHAS might suppress the formation of oxidative metabolites, and prevent acetaminophen induced hepatotoxicity.

• Molecules and Cells
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• v.19 no.1
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• pp.131-136
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• 2005

The ETV6-NTRK3 gene fusion, first identified in the chromosomal translocation in congenital fibrosarcoma, encodes a chimeric protein tyrosine kinase with potent transforming activity. ETV6-NTRK3-dependent transformation involves the joint action of NTRK3 signaling pathways, and aberrant cell cycle progression resulting from activation of Mek1 and Akt. The level of glutathione (GSH) was found to be markedly increased in ETV6-NTRK3-transformed NIH3T3 cells. The activities of the two GSH biosynthetic enzymes as well as of glutathione peroxidase, together with their mRNAs, were also higher in the transformed cells. The transformed cells were able to grow in the presence of GSH-depleting agents, whereas the control cells were not. L-Buthionine-(S,R)-sulfoximine (BSO) inhibited activation of Mek1 and Akt in the transformed NIH3T3 cells. These observations imply that up-regulation of GSH biosynthesis plays a central role in ETV6-NTRK3-induced transformation.