• 동아시아식생활학회지
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• 제3권2호
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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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• 제10권3호
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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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• 제56권8호
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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.

• 분석과학
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• 제10권5호
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• pp.378-385
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• 1997

본 실험은 human glutathione S-transferase P1-1의 tyrosine 7 잔기에 대한 변이체를 작성하고, 기질특이성과 저해제의 효과를 조사하여, 이 잔기의 기능을 분석한 것이다. 1,2-dichloro-4-nitrobenzene과 1,2-epoxy-3-(p-nitrophenoxy)propane에 대한 GSH 포합반응에 대한 활성은 야생형에 비해 변이체 Y7F에서는 3~5%로 크게 저하하였으며, 효소에 결합한 GSH의 thiol기의 pKa는 2.4 pK 높았다. 저해제 hematin에 대한 $I^{50}$값은 야생형과 변이체 Y7F에서 비슷하게 나타났으며, 저해제 benastatin A와 S-(2,4-dinitrophenyl) glutathione에 대한 $I^{50}$값들은 다소 감소하였다. 이러한 결과들로부터 tyrosine 7 잔기는 기질의 결합에 관여하기보다 GSH-chloronitrobenzene 유도체와 GSH-epoxide 포함반응에 대한 촉매활성에 중요하다고 생각된다.

• Preventive Nutrition and Food Science
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• 제4권2호
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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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• 제32권10호
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• pp.3756-3759
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• 2011

• 한국응용과학기술학회지
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• 제36권1호
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• pp.341-347
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• 2019

본 연구에서는 한약재의 활용도를 높이기 위한 연구로 추출물 농도에 따른 생리활성물질의 용출량을 측정하기 위해 한방약술의 품질 특성과 Glutathione S-transferase의 활성 저해능을 측정한 결과는 다음과 같다. 한방약술의 pH결과는 4.4로 발효 전의 대조구 3.9보다 증가하였다. 이러한 변화는 알코올 발효과정 중 발효부산물 및 유기산 때문으로 사료된다. 한방약술의 산도는 0.55%로 발효 전의 대조구 0.09%보다 약 6배 증가하였다. 이런 결과는 유기산이 알코올 등과 결합하여 ester와 같은 향미 형성 등에 이용되는 것을 알 수 있다. 한방약술 15%의 glutathione S-transferase의 활성 저해능 $5.1{\pm}0.3$, 한방약술 20%는 저해능 $6.5{\pm}0.5$, 한방약술 25%는 $7.6{\pm}0.6$, 한방약술 30%는 $8.4{\pm}0.2$, 최대 농도인 35%에서의 저해능은 $9.7{\pm}0.7$로 나타내었다. 추출 농도별로 glutathione S-transferase의 활성 저해능은 통계학적으로 유의한 차이가 있음을 보였다 (p<0.05).

• BMB Reports
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• 제38권2호
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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.

• 한국응용곤충학회지
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• 제43권4호
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• pp.317-322
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• 2004

배추좀나방의 발육단계별 indoxacarb의 살충활성, 침투이행성 및 잔효성을 조사하였고, esterase, acetylcholinesterase, glutathione S-transferase 등의 효소활성에 미치는 영향을 검토하였다. 배추좀나방 유충에 대해서 높은 살충효과를 나타내었으나, 알과 번데기에 대해서는 살충율이 $10\%$이하이었다. 엽면침투이행성과 근부침투이행성의 효과는 없었으며, 잔효성은 10일째까지 $80\%$의 살충효과를 유지하였다. Indoxacarb는 esterase와 glutathione S-transferase의 활성은 저해하지 않았지만 acetylcholinesterase의 활성을 저해하였다.

• Journal of Microbiology and Biotechnology
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• 제15권1호
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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.