• Korean Journal of Food Science and Technology
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• v.30 no.1
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• pp.206-212
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• 1998

This study was undertaken to explore the applicability of glutathione S-transferase (GST) activity as a predictable indicator to monitor chemical pollution in shells and fishes utilized for food. There were some variations in the basal level of GST activity depending on species tested. Ark shells, Anadara satowi, showed the highest normal enzyme activity, followed by catfish and marine mussels, Mytilus coruscus. White clams, Meretrix lusoria, Israeli carp and catfish had lower activity. When A. satowi was exposed to 3-methyl-cholanthrene (3-MC), a prototypic polycyclic aromatic hydrocarbon for 1 week, GST activity decreased by about 30%. This reduction in GST activity induced by 3-MC did not recover until two weeks after the cessation of exposure. GST activity increased in response to 3-MC in most of the other species studied. The GST elevation in M. coruscus attained its maxinum of about 200% at the termination of 3-MC exposure maintaining this level up to 2 weeks, and declined gradually thereafter. 3-MC also induced GST activity in lsraeli carp in a similar fashion to M. coruscus. Phenobarbital induced GST activity both in M. coruscus and lsraeil carp. Other chemicals. such as clofibrate, butylated hydroxyanisole. hexachlorobenzene, and oxolinic acid did not change the enzyme activity significantly in most speciel. Phenol depressed GST activity only in lsraeli carp. These results suggest that the basal level of GST activity is somewhat variable and that the direction of change in response to chemicals seems to be related to its normal activity. The change in enzyme activity can be a preditable indicator of some environmental chemicals such as PAHs and phenol.

• BMB Reports
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• v.38 no.2
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• pp.232-237
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• 2005

A glutathione S-transferase (GST) from Lactuca sativa was purified to electrophoretic homogeneity approximately 403-fold with a 9.6% activity yield by DEAE-Sephacel and glutathione (GSH)-Sepharose column chromatography. The molecular weight of the enzyme was determined to be approximately 23,000 by SDS-polyacrylamide gel electrophoresis and 48,000 by gel chromatography, indicating a homodimeric structure. The activity of the enzyme was significantly inhibited by S-hexylGSH and S-(2,4-dinitrophenyl) glutathione. The enzyme displayed activity towards 1-chloro-2,4-dinitrobenzene, a general GST substrate and high activities towards ethacrynic acid. It also exhibited glutathione peroxidase activity toward cumene hydroperoxide.

• 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.

• Journal of Nutrition and Health
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• v.30 no.7
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• pp.803-812
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• 1997

The influences of dietary supplements of vitamin E on hepatocellular chemical carcinogenesis have been studied, Placental glutathione S-transferase(GST-P) positive foci area, antioxidant enzymes(superoxide dismutase(SOD), catalase, glutathione reductase, glutathione peroxidase, glutathione S-transferase(GST)), glucose 6-phosphatase(G6Pase) activities, and lipid peroxidation of mecrosomes(thiobarbituric acid reactive substances(TBARS) contents) were investigated. For is purpose , we used the murine chemical hepatocardinogenic procedure induced by modified Ito model, which consists of 200mg/kg body weight diethylinitrosamine (DEN) injection, 0.01% 2-acethlaminoflurene(2-AAF) feeding for 6 weeks, and partial hepatectomy on week 3. Weanling Sprague-Dawley male rats were fed pulverized Purina rat chow with 15, 000IU/kg diet vitamin E from initiation or promotion stages. We found that vitamin E supplement decreased the area of GST-P positive foci. Catalase, glutathione peroxidase, glutathione reductase. GST activities, and TBARS contents were decreased. On the other hand G6Pase activities were increased by vitamin E supplement. It seemed that vitamin E supplements helped endogenous defense systems against carcinogenesis by decreasing TBARS contents, $H_2O$$_2$ and organic peroxides. So, vitamin E seemed to protect cell from free radical damage in carcinogenesis. Anticarcinogenic effects of vitamin E were more effective at intiation that at promotion stage. These results suggest that vitamin E has suppressive effects on hepatocellular chemical carcinogenesis, probably through antioxidant effects against TBARS contents $H_2O$$_2$ and orgainc peroxides.

• The Korean Journal of Pesticide Science
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• v.2 no.1
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• pp.97-103
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• 1998

Effects of safener fluxofenim was investigated for crop injury of acetanilide's upland herbicides and for enzyme activity of glutathione S-transferase (GST) in grain sorghum. Bioassay with etiolated grain sorghum [Sorghum bicolor (L.) Moench. cv. 'G522DR'] seedlings grown in agar containing metolachlor or alachlor showed that they are strong inhibitors on root growth of grain sorghum ($GI_{50}=4.5{\mu}M$ for metolachlor and $6.2{\mu}M$ for alachlor). The safener fluxofenim applied by seed soaking protected growth of grain sorghum from crop injury of metolachlor or alachlor at the concentrations of 1 to 10 ${\mu}M$. There was a significant increase in glutathione-herbicide conjugates in root tissues of fluxofenim-treated seedlings. Activities of $GST_{-metolachlor}$ and $GST_{-CDNB}$ were increased by 82% and 70%, respectively, in the cytosolic fraction of roots with fluxofenim treatment.

• Journal of Environmental Health Sciences
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• v.29 no.2
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• pp.80-86
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• 2003

To evaluate the effect of cyclohexane(CH) treatment on the serum levels of glutathion S-transferase(GST) activity in liver damaged animals, damaged liver was induced with pretreatment of 50% $CCl_4$ dissolved in olive oil (0.1 m1/100g body weight) intraperitoneally 17 times every other day. To $CCl_4$-treated rats, CH (1.56 g/kg body weight, i.p) was injected once and then the animals were sacrificed at 4 hours after injection of CH. The $CCl_4$-treated animals were identified as severe liver damage on the basis of liver functional findings, 1,e, increased serum levels of alanine aminotransferase(ALT), alkaline phosphate(ALP) and xanthine oxidase(XO) activities. On the other hand, $CCl_4$-treated animals injected with CH once($CCl_4$-pretreated animals) showed more decreased serum levels of ALT and XO, and more increased those of ALP rather than $CCl_4$-treated animals. In case of comparing the GST with ALT activity in liver, both $CCl_4$-treated and pretreated animals showed similar changing pattern of enzyme actvity. Especially $CCl_4$-pretreated animals showed significantly increased serum level of GST actvity compared with the $CCl_4$-treated those, whereas those of ALT showed reversed tendency. In aspects of GST enzyme kinetics, $CCl_4$-pretreated animals showed higher Vmax of liver GST enzyme than $CCl_4$-treated animals. In conclusion, injection of CH to the liver damaged rats led to enhanced liver damage and more increased activity of serum GST which may be chiefly caused by the enzyme induction.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.1
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• pp.15-18
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• 1993

To evaluate an effect of dietary protein on the intoxication of methanethiol in rats, the methanethiol was intraperitoneally injected to the rats fed a low or high protein diet and then the liver weight per body weight and seurm levels of alanine aminotransferase (ALT) activities were determined to investigate the differences in liver damage between the animal groups fed low protein diet and that fed high protein diet. On the other hand, the hepatic glutathione content and its conjugating enzyme, glutathione S-transferase (GST) activity were determined to clarify the cause of difference in liver function between the two groups. The increasing rate of liver weigh/body wt., serum levels of ALT to its control group were higher in methanethiol-treated rats fed low protein diet than those fed high protein diet. The hepatic content of glutathione and GST activity were higher in rats fed high protein diet than those fed low protein diet and the decreasing rate of hepatic glu-tathione content to its control group was higher in rats fed low protein diet than those fed high protein diet. Furthermore, the hepatic GST activity in methanethiol-treated rats was higher in rats fed high protein diet than those fed low protein diet. In case of control group, the GST activity was also higher in rats fed high protein diet than those fed low protein diet.

• Journal of Physiology & Pathology in Korean Medicine
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• v.20 no.6
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• pp.1572-1575
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• 2006

Water extract from Cnidii Rhizoma (CRW) was tested for colon cancer chemopreventive activity by measuring the induction of phase II detoxification enzyme activity [quinone reductase (QR) and glutathione S-transferase (GST)] and glutathion (GSH) levels and ornithine decarboxylase (ODC) activity in cultured human colorectal adenocarcinoma HT-29 cells. CRW inhibited cell proliferation in cultured HT-29 cells. CRW induced QR activity in a dose-dependent manner in a concentration range of 0.1${\sim}$5.0 $mg/m{\ell}$. GST activity was also induced with the treatment of CRW in HT-29 cells. In addition GSH levels was increased with CRW. CRW inhibited ODC activity, a key enzyme of polyamine biosynthesis, which is enhanced in tumor promotion. These results suggest that CRW has colon cancer chemopreventive activity by increasing phase II enzyme activity and GSH levels and inhibiting ODC activity in vitro.

• Journal of Physiology & Pathology in Korean Medicine
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• v.22 no.1
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• pp.126-130
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• 2008

Water extract from Prunella vulgaris L. (PVW) was tested for colon cancer chemopreventive activity by measuring the activities of cytochrome P450 1A1, phase Ⅱ detoxification enzyme [quinone reductase (QR) and glutathione S-transferase (GST)] and ornithine decarboxylase (ODC) and glutathione (GSH) levels in cultured human colorectal adenocarcinoma HT-29 cells. PVW significantly inhibited 7,12-dimethylbenz[a]anthracene (DMBA)-induced cytochrome P450 1A1 activity at 10 and 50 ${\mu}g/ml$. PVW induced QR activity in a dose-dependent manner over a concentration range of $1{\sim}50\;{\mu}g/ml$. GST activity was also induced with the treatment of PVW in HT-29 cells. In addition GSH levels were increased with PVW. PVW inhibited ODC activity, a key enzyme of polyamine biosynthesis, which is enhanced in tumor promotion. These results suggest that Prunella vulgaris L. has colon cancer chemopreventive activity by inhibiting cytochrome P450 1A1 and ODC activities and by increasing phase Ⅱ enzyme activity and GSH levels.

• Bulletin of the Korean Chemical Society
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• v.22 no.1
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• pp.77-83
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• 2001

To gain further insight into the relationship between structure and function of glutathione S-transferase (GST), the four cysteine mutants, C14S, C47S, C101S and C169S, of human GST P1-1 were expressed in Escherichia coli and purified to electrophoretic homogeneity by affinity chromatography on immobilized glutathione (GSH). The catalytic activities of the four mutant enzymes were characterized with five different substrates as well as by their binding to four different inhibitors. Cys14 seems to participate in the catalytic reaction of GST by stabilizing the conformation of the active-site loop, not in the GSH binding directly. The substitution of Cys47 with serine significantly reduces the affinity of GSH binding, although it does not prevent GSH binding. On the other hand, the substitution of Cys101 with serine appears to change the binding affinity of electrophilic substrate by inducing a conformational change of the $\alpha-helix$ D. Cys169 seems to be important for maintaining the stable conformation of the enzyme. In addition, all four cysteine residues are not needed for the steroid isomerase activity of human glutathione S-transferase P1-1.