• Journal of Life Science
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• v.13 no.2
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• pp.230-235
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• 2003

To investigate hepatoprotective activities of the root extract of Rosa davurica, the activities of hepatic enzymes, aminopyrine N-demethylase, aniline hydroxylase, glutathione S-transferase and epoxide hydrolase in rats intoxicated with bromobenzene were studied. Pretreatment with the methanol extract from the roots of Rosa davurica did not show any significant effects on the increases of the activities of aminopyrine N-demethylase and aniline hydroxylase, enzymes forming toxic epoxide by bromobenzene. There was no change in glutathione S-transferase activity by Rosa davurica. However, the activity of epoxide hydrolase, and epoxide-removing enzyme, was increased 33% by the administration of 500 mg/kg of the methanol extract. From the results, the protection of Rosa davurica against bromobenzene-induced hepatotoxicity is thought to be via enhancing the activity of epoxide hydrolase, an enzyme removing toxic epoxide rather than through epoxide-producing system.

• Bulletin of the Korean Chemical Society
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• v.28 no.5
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• pp.772-776
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• 2007

In order to study the role of residue in the active site of glutathione S-transferase (GST), Arg13 residue in human GST P1-1 was replaced with alanine, lysine and leucine by site-directed mutagenesis to obtain mutants R13A, R13K and R13L. These three mutant enzymes were expressed in Escherichia coli and purified to electrophoretic homogeneity by affinity chromatography on immobilized GSH. Mutation of Arg13 into Ala caused a substantial reduction of the specific activity by 10-fold. Km GSH, Km DCNB and Km EPNP values of R13A were approximately 2-3 fold larger than those of the wild type. Mutation of Arg13 into Ala also significantly affected I50 values of S-methyl-GSH that compete with GSH and ethacrynic acid, an electrophilic substrate-like compound. These results appeared that the substitution of Arg13 with Ala resulted in significant structural change of the active site. Mutation of Arg13 into Leu reduced the catalytic activity by approximately 2-fold, whereas substitution by Lys scarcely affected the activity, indicating the significance of a positively charged residue at position 13. Therefore, arginine 13 participates in catalytic activity as mainly involved in the construction of the proper electrostatic field and conformation of the active site in human GST P1-1.

• Preventive Nutrition and Food Science
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• v.5 no.3
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• pp.126-130
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• 2000

To enhance the antitumor activity of Chinese cabbage kimchi, four kinds of kimchi, which ere differently prepared in kinds and levels of sub-ingredients, were fermented at 15$^{\circ}C$ for 1 day and then at 5$^{\circ}C$ up to pH 4.3. The solid tumor formation, hepatic glutathione S-transferase activity and glutathione contents in the liver, and natural killer (NK) cell activity of spleen were determined from the sarcoma-180 cell injected Balb/c mice that were treated with methanol extracts of the kimchi samples. Kimchi IV, prepared with organically cultivated Chinese cabbage, red pepper powder, garlic, Chinese pepper powder mustard leaf and heat processed salt (Gueun salt), reduced the tumor formation by 39.3% compared to the sarcoma-180 cell treated group, resulting in the smallest tumor weight. Methanol extracts of the kimchi III and kimchi IV recovered the activities of hepatic glutathione S-transferase(GST) that was decreased by the transplantation of the sarcoma-180 cells to th mice. The injections of methanol extracts of kimchi II and kimchi IV increased glutathione contents in sarcoma-180 cells treated mice. The methanol extract of kimchi IV increased the natural killer (NK) cell activity of spleen lymphocytes a more effectively (p<0.05) than those the other kimchi samples. These results suggest that the anticancer activities of kimchi can be increased by changing the kinds and levels of sub-ingredients.

• Korean Journal of Acupuncture
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• v.18 no.1
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• pp.1-9
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• 2001

Artemisia asiatica Nakai aqua-acupuncture solution (ANAS) was administered once daily for 10 days before the tumor implantation ($1{\times}10^6\;cells$). Body weight, spleen weight and the number of ascitic tumor cells were measured at 6 days after tumor implantation. The change of body weight and the survival rate of mice were observed for 21 days. It was used three biomarkers (quinone reductase, glutathione, glutathione S-transferase) to test chemopreventive potentials of ANAS. ANAS exerted antitumor activity by inhibiting the growth of Ehrlich ascites tumor cells in vivo. Mice given Ehrlich cells and ANAS at $CV_{12}$ and $BL_{18}$ had 57.1% to 49.2% survival after 21 days. Quinone reductase activity and glutathione levels were increased with ANAS. However, glutathione S-transferase level was 1.1-fold with ANAS. These results suggest that ANAS has chemopreventive potential by inducing QR activity and increasing GSH level.

• Bulletin of the Korean Chemical Society
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• v.25 no.9
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• pp.1366-1370
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• 2004

Controlled pore glass bead was modified with bovine serum albumin (BSA), and glutathione (GSH) was immobilized through three kinds of linkers on top of BSA. Bis(3-sulfo-N-hydroxysuccinimide suberate) sodium salt $(BS^3)$, N-hydroxysuccinimide 3-(2-pyridyldithio)propionate (SPDP), or N-hydroxysuccinimide 4-maleimidobutyrate (GMBS) was introduced into the BSA-bound matrix. Subsequently, GSH was immobilized by addition of thiol side chain into the maleimido moiety, replacing a disulfide group, or formation of an amide group upon releasing 3-sulfo-N-hydroxysuccimide group. It was observed that conjugation methodology played a critical role for activity of the immobilized GSH. SDS-PAGE chromatogram showed that the matrix of glutathione immobilized on BSA through GMBS manifested high selectivity towards glutathione-S-transferase (GST) in cell lysate.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.6
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• pp.678-684
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• 1993

To evaluate the role of xanthine oxidase in liver damage by CCl4, a group of rats were fed tungstate for a month, which suppressed the activities of xanthine oxidase in serum and liver. Control group of rats were fed standard diet without tungstate. Liver damage was induced both in tungstate fed and control groups by two intraperitoneal injections of CCl4 at the level of 0.1ml/100g body weight at intervals of 24 hours. Increases in the levels of serum alanine aminotransferase by CCl4 were significantly smaller in tungstate fed rats than in control rats. Concomitantly, histopathologic changes were less in tungstate fed rats than in control ones. In rats either treated with CCl4 or not, hepatic type O xanthine oxidase activities were remarkably reduced by tungstate feeding. Hepatic aniline hydroxylase activities were higher in rats fed tungstate than control rats when animals were not treated with CCl4, but the enzyme activities were lower in tungstate fed rats than control when they were treated with CCl4. Neither tungstate feeding nor CCl4 treatment caused any significant changes in hepatic glutathione contents, and activities of hepatic glutathione S-transferase, glutathione peroxidase and superoxide dismutase. It is concluded xanthine oxidase reaction augment CCl4 induced liver damage via oxygen free radical system.

• YAKHAK HOEJI
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• v.42 no.1
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• pp.108-113
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• 1998

G009, a polysaccharide isolated from the mycelia of Ganoderma lucidum IYO09, showed a hepatoprotective activity against $CCl_4$ induced cytotoxicity in primary cu ltured rat hepatocytes. Incubation of $CCl_4$-intoxicated hepatocytes with G009 significantly reduced the levels of glutamic pyruvic transaminase and sorbitol dehydrogenase released from hepatocytes in the medium. G009 showed antioxidative effect by elevating the activities of glutathione reductase and superoxide dismutase, and the content of glutathione in $CCl_4$-intoxidcated primary cultured rat hepatocytes. Furthermore, G009 significantly elevated glutathione-S-transferase activity in $CCl_4$-intoxicated primary cultured rat hepatocytes. G009 also reduced the production of malondialdehyde, a byproduct of lipid peroxidation. From these results, it could be concluded that G009 exerted hepatoprotective activity against $CCl_4$-induced cytotoxicity through antioxidation.

• Nutrition Research and Practice
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• v.11 no.3
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• pp.214-222
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• 2017

BACKGROUND/OBJECTIVES: Glutathione S-transferase (GST) forms a multigene family of phase II detoxification enzymes which are involved in the detoxification of xenobiotics by conjugating substances with glutathione. The aim of this study is to assess the antioxidative status and the degree of DNA damage in the subclinical hypertensive patients in Korea using glutathione S-transferase polymorphisms. SUBJECTS/METHODS: We examined whether DNA damage and antioxidative status show a difference between GSTM1 or GSTT1 genotype in 227 newly diagnosed, untreated (systolic blood pressure $(BP){\geq}130mmHg$ or diastolic $BP{\geq}85mmHg$) subclinical hypertensive patients and 130 normotensive subjects (systolic BP < 120 mmHg and diastolic BP < 80 mmHg). From the blood of the subjects, the degree of the DNA damage in lymphocyte, the activities of erythrocyte superoxide dismutase, the catalase, and the glutathione peroxidase, the level of glutathione, plasma total radical-trapping antioxidant potential (TRAP), anti-oxidative vitamins, as well as plasma lipid profiles and conjugated diene (CD) were analyzed. RESULTS: Of the 227 subjects studied, 68.3% were GSTM1 null genotype and 66.5% were GSTT1 null genotype. GSTM1 null genotype had an increased risk of hypertension (OR: 2.104, CI: 1.38-3.35), but no significant association in GSTT1 null genotype (OR 0.982, CI: 0.62-1.55). No difference in erythrocyte activities of superoxide dismutase, catalase, or glutathione peroxidase, and plasma TRAP, CD, lipid profiles, and GSH levels were observed between GSTM1 or GSTT1 genotype. Plasma levels of ${\alpha}-tocopherol$ increased significantly in GSTT1 wild genotype (P < 0.05); however, plasma level of ${\beta}-carotene$ increased significantly in GSTT1 null genotype (P < 0.01). DNA damage assessed by the Comet assay was significantly higher in GSTM1 null genotype than wild genotype (P < 0.05). CONCLUSIONS: These results confirm the association between GSTM1 null genotype and risk of hypertension as they suggest that GSTM1 null genotype leads to an increased oxidative stress compared with wild genotype.

• The Journal of Korean Medicine
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• v.25 no.4
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• pp.36-42
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• 2004

Objective : Glutathione S-transferase polymorphism (GST) were examined in 120 cases with ischemic cerebrovascular disease (ICVD) to test the hyperthesis that GST polymorphisms confer a risk to an individual to develop ICVD. Tobacco smoking is a major cause of both cancer and vascular disease. Methods : therefore We were stratified the subjects with ICVD for smoking status, and then examined whether polymorphisms in this detoxification enzyme gene, GST, influence risk of ICVD Results : Neither GSTM1 nor GSTT1 genotypes in the ICVD group was significantly different from the control group (n=207), even in smokers. We attempted the combined analyses for GSTM1 and GSTT1 genotypes in ICVD for smoking status. No significant association observed between the combined genotypes and ICVD Conclusion : Our observation do not confirm the effect of the GSTM1 and GSTT1 genotypes as a risk factor for ICVD, even in smokers.

• Bulletin of the Korean Chemical Society
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• v.24 no.8
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• pp.1188-1192
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• 2003

In order to study the role of residue in the active site of glutathione S-transferase (GST), Tyr 108 residue in human GST P1-1 was replaced with alanine, phenylalanine and tryptophan by site-directed mutagenesis to obtain mutants Y108A, Y108F and Y108W. These three mutant enzymes were expressed in Escherichia coli and purified to electrophoretic homogeneity by affinity chromatography on immobilized GSH. The substitutions of Tyr108 significantly affected $K_m^{CDNB}$ and $K_m^{ETA}$, whereas scarcely affected $K_m^{GSH}$. The substitutions of Tyr108 also significantly affected $I_{50}$ of ETA, an electrophilic substrate-like compound. The effect of these substitutions on kinetic parameters and the response to inhibition suggests that tyrosine 108 in hGST P1-1 contributes to the binding of the electrophilic substrate and a major determinant in the binding of CDNB is the aromatic ring of Tyr108, not its hydroxyl group.