• Journal of the East Asian Society of Dietary Life
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• v.3 no.2
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• pp.121-128
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• 1993

This study was intended to clarify the protective mechanism of diallyl disulfide on the carbon tetrachloride-induced hepatotoxicity in mice. It was observed that a powerfully increment of serum alanine aminotransferase activity and hepatic lipid peroxide content after carbon tetrachloride injection were markedly inhibited by the pretreatment of diallyl disulfide (20mg/kg) for 5 days. It was also observed that hepatic aminopyrine demethylase and xanthine ocidase as free radical generating enzymes as well as superoxide dismutase and catalase activities as free frdical scavenging enzymes and hepatic glutathione content were not changed by the pretreatment with diallyl disulfide. But, treatment with diallyl disulfide did signifiantly increase cytosolic glutathione S-transferase activity. However, glutathione S-transferase activity in the presence of diallyl disulfide was not affected in vitro. Therefore, it is concluded that mechanism for the observed preventive effect ofdiallyl disulfide against the carbon tetrachloride-induced hepatotoxicity can be due to the engancement of glutathione S-transferase activity.

• Archives of Pharmacal Research
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• v.10 no.3
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• pp.149-152
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• 1987

The present work was undertaken to investigate the effect of diallyl disulfide on ethacrynic acid toxicity. Ethacrynic acid-induced morality and formation of lipid peroxide were inhibited by diallyl disulfide. Furthermore, decreasing effect of glutathione S-transferase and glutathione level in the liver by ethacrynic acid were reduced by diallyl disulfide. These results suggested that the inducing effect of diallyl disulfide on the ethacrynic acid metabolizing enzyme, glutathione S-transferase, is believed to be a possible detoxication mechanism for the ethacrynic acid toxicity in mice.

• BMB Reports
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• v.56 no.8
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• pp.457-462
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• 2023

Glutathione S-transferase omega 1 (GstO1) is closely associated with various human diseases, including obesity and diabetes, but its functional mechanism is not fully understood. In the present study, we found that the GstO1-specific inhibitor C1-27 effectively suppressed the adipocyte differentiation of 3T3-L1 preadipocytes. GstO1 expression was immediately upregulated upon the induction of adipocyte differentiation, and barely altered by C1-27. However, C1-27 significantly decreased the stability of GstO1. Moreover, GstO1 catalyzed the deglutathionylation of cellular proteins during the early phase of adipocyte differentiation, and C1-27 inhibited this activity. These results demonstrate that GstO1 is involved in adipocyte differentiation by catalyzing the deglutathionylation of proteins critical for the early phase of adipocyte differentiation.

• Analytical Science and Technology
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• v.10 no.5
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• pp.378-385
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• 1997

In order to clarify the functional role of Tyr7 in human glutathione S-transferase P1-1, we extensively investigated the effect of mutation of Tyr7 on the substrate specificity and inhibition characteristics. The mutational replacement of Tyr7 with phenylalanine lowered the specific activities with 1,2-dichloro-4-nitrobenzene and 1,2-epoxy-3-(p-nitrophenoxy) propane for GSH-conjugation reaction to 3~5% of the values for the wild-type enzyme. The pKa of the thiol group of GSH bound in Y7F was about 2.4 pK units higher than that in the wild-type enzyme. The $I_{50}$ of hematin for Y7F was similar to that for the wild-type enzyme and those of benastatin A and S-(2,4-dinitrophenyl)glutathione were only moderately decreased. These results suggest that Tyr7 is considered to be important the catalytic activities not only for GSH-chloronitrobenzene derivatives but also for GSH-epoxide conjugation reaction, rather than to binding of the substrates.

• Preventive Nutrition and Food Science
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• v.4 no.2
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• pp.134-138
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• 1999

The effects of dietary Coix(lacryma-jobi) water extract on the antioxidant enzyme activity in the liver and kidney of Sprague-Dawley rats were studied. Forty-five rats were fed for 3 weeks with either control diet or experimental diets that contain either Coix water extract or Coix water residue. Twenty percent of the carbohydrate was replaced with Coix water residue by dry weight in the water residue diet, while distilled water was replaced by Coix water extract to make a pellet-form diet in the Coix water extract diet. The levels of glutathione, glutathione-peroxidase, and glutathione-S-transferase activities in liver and kidney were measured . It has been found that glutathione, glutathione peroxidase, and glutathione-S-transferase enzyme activities from activities from liver and kidneyof the rats were enhanced in the group fed with Coix water extract.

• Bulletin of the Korean Chemical Society
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• v.32 no.10
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• pp.3756-3759
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• 2011

• Journal of the Korean Applied Science and Technology
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• v.36 no.1
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• pp.341-347
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• 2019

In this study, the following is the result of measuring the quality characteristics of herbal wine and the active inhibition of Glutathione S-transferase in order to measure the release of physiological active substances according to the concentration of extracts. The pH level of herbal wine was 4.4, up from 3.9 before fermentation. These changes are attributed to fermentation and organic acids during alcoholic fermentation. The acidity of herbal wine was 0.55%, about six times higher than the pre-fermentation control of 0.09%. These results show that organic acids are used for flavor formation, ether, in combination with alcohol. The inhibitory activity of glutathione S-transferase were $5.1{\pm}0.31$ in herbal wine 15%, $6.5{\pm}0.6$ in herbal wine 20%, $7.6{\pm}0.6$ in herbal wine 25%, $8.4{\pm}0.2$ in herbal wine 30% and $9.7{\pm}0.7$ in herbal wine 35%. As the extract concentration was increased the inhibitory activity of glutathione S-transferase were significantly increased (<0.05).

• 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 applied entomology
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• v.43 no.4 s.137
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• pp.317-322
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• 2004

Insecticidal activity, systemic and residual effects, and effects on enzyme activities (esterase, acetylcholinesterase, glutathione S-transferase) of indoxcarb were evaluated against Plutella xylostella. The insecticide was very effective against larvae of P. xylostella. Also, indoxacarb showed only residual effect to P. xylostella when applied to vegetable leaves. It inhibited acetylcholinesterase activity, but didn't do esterase and glutathione S-transferase activities.

• Journal of Microbiology and Biotechnology
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• v.15 no.1
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• pp.183-187
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• 2005

Abstract The cancer chemopreventive potential of chitosanoligosaccharides was investigated by measuring the induction of quinone reductase and glutathione S-transferase activities and inhibition of cytochrome P450 1A1, 2B1, and 2E1 activities. Chitosanoligosaccharide I (1-${\kappa}$Da${\kappa}$Da) significantly induced glutathione S-transferase activity with a maximal 1.5-fold increase at 500 ${\mu}$g/ml, while chitosanoligosaccharide II (3-${\kappa}$Da${\kappa}$Da) (500 ${\mu}$g/ml) strongly induced quinone reductase (p<0.01) and glutathione S-transferase (p<0.005) activities. The in vitro incubation of rat liver microsomes with chitosanoligosaccharides I and II (2.5, 5, 50, and 500 ${\mu}$g/ml) showed a dose-dependent inhibiton of cytochrome P450 1A1, 2B1, and 2E1 activities. Chitosanoligosaccharide II was a more potent inhibitor of cytochrome P450 2B1 activity than chitosanoligosaccharide I. Accordingly, these findings suggest that chitosanoligosaccharides are potential chemopreventive agents.