• Title, Summary, Keyword: glutathione S-transferase

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Protective Effect of Diallyl Disulfide on the Bromobenzene-Induced Hepatotoxicity in Mice (Bromobenzene 간손상에 대한 Diallyl Disulfide의 예방효과)

  • Lee, Sang-Il;Yoon, Chong-Guk;Huh, Keun
    • The Korean Journal of Pharmacology
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    • v.26 no.2
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    • pp.185-192
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    • 1990
  • The present work was undertaken to investigate the protective effect of diallyl disulfide on the bromobenzene toxicity in mice. It was observed that the aniline hydroxylase and epoxide hydrolase activities were not changed by the treatment of diallyl disulfide for 5 days. But glutathione S-transferase activity was significantly increased. A striking enhancement of serum alanine aminotransferase activity and hepatic lipid peroxide content after bromobenzene administration was markedly decreased by diallyl disulfide pretreatment. These results indicate that the inducing effects of diallyl disulfide on the bromobenzene intermediate detoxifying enzyme such as glutathione S-transferase are believed to be a possible protective mechanism for the bromobenzene toxicity in mice.

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Naphthazarin Derivative (V) : Formation of Glutathione Conjugate and Cytotoxic Activity of 2-or 6-Substituted 5,8-Dimethoxy-1,4-napthoquinones in the Presence of Glutathione-S-transferase, in Rat Liver S-9 Fraction and Mouse Liver Perfusate

  • Zheng, Xiang-Guo;Kang, Jong-Seong;Kim, Hwan-Mook;Jin, Guang-Zhu;Ahn, Byung-Zun
    • Archives of Pharmacal Research
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    • v.23 no.1
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    • pp.22-25
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    • 2000
  • Formation of glutathione (GSH) conjugates with 2- or 6-(1-hydroxymethyl)- and 2-(1-hydroxyethyl)-DMNQ derivatives (DMNQ, 5,8-dimethoxy-1,4-naphthoquone was carried out in phosphate buffer (pH 7.4), in the presence of glutathione-S-transferase (GST), in rat liver S-9 fraction and by perfusion, and the rates of conjugates formation were compared and correlated to cytotoxicity. The GSH conjugates of 6-(1-hydroxyalkyl)-DMNQ derivatives were formed faster than 2-(1-hydroxyalkyl)-DMNQ derivatives under all of the media, implying that steric hindrance was the cause of lowering the rate of conjugate formation of 2-substituted derivatives. For both isomers, addition of GST did not improve the reaction rate, compared with that in buffer, while the reaction in the S-9 fraction and the perfusate was accelerated to a great extent. The catalytic effect of the S-9 fraction and the perfusate contain an effective system relaxing the steric hindrance of 2-(1-hydroxyalkyl)-DMNQ derivatives. Furthermore, a good correlation between the formation of the GSH conjugates and the cytotoxic activity of both naphthazarin isomers suggests that the steric hindrance is a cause of lowering the cytotoxicity of 2-isomers.

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AMPLIFICATION OF MERCURY TOXICITY BY GLUTATHIONE DEPLETION IN V79 CELLS

  • Yisook Nam;Chung, An-Sik
    • Toxicological Research
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    • v.9 no.2
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    • pp.159-166
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    • 1993
  • The treatmene of V79 cells with diethyl maleate (DEM) led to decrease in glutathione (GSH) level as increasing DEM concentration. Mercuric chloride, treated for 6 hrs with 2ng/ml, affected the GSH metabolizing enzymes glutathione S-transferase (GST) and glutathione peroxidase (GSP), dropping their activities to 60% and 75%, respectively, though not so much in GSH level(80%). However, the toxic effects of mercuric chloride on those enzymes and GSH level were both amplified when the Hg2+ treatment was combined with the preceding DEM treatment.

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Taraxacum mongolieum Hand-Mass Aqua-acupuncture Solution as the Blocking Agent of Carcinogenesis (포공영약침액의 발암과정 blocking agent로서의 활성)

  • 손윤희;김소연;임종국;남경수
    • Journal of Life Science
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    • v.12 no.5
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    • pp.549-554
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    • 2002
  • Taraxacunf mongofieum Hand-Mass aqua-acupuncture solution (TMAS) was prepared and investigated og, the effect on initiation of carcinogenesis. The following effe.Is as a blocking agent were measured. .(a) Indu.ction of quinone reductase, (b) Induction of glutathione S-transferase activity (c) Increase of reduced glutathione. TMAS was potent inducer of quinone reductase in Hepa Iclc7 murine hepatoma cells. Clutathione S-transferase activity was increased with TMAS. In addition glutathione levels were increased about 1.6-fold with TMAS in cultured murine hepatoma Hepa Iclc7 cells.

A Second Thioltransferase of Schizosaccharomyces pombe Contains Glutathione S-transferase Activity

  • Kim, Hong-Gyum;Park, Eun-Hee;Lim, Chang-Jin
    • BMB Reports
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    • v.32 no.6
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    • pp.535-540
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    • 1999
  • Two types of the thioltransferase (also called glutaredoxin) have been previously detected in the cytosolic extract of Schizosaccharomyces pombe, a fission yeast. Previously, the one with a smaller molecular mass (14kDa) was purified and characterized. In the present study, the second thioltransferase was purified. The purification procedure included ammonium sulfate fractionation (40-80%), Sephadex G-200 gel filtration, DEAE-cellulose ion-exchange chromatography, Sephadex G-50 gel filtration, and glutathione-agarose affinity chromatography. The purified enzyme showed a single band on SDS-PAGE, and its molecular mass was determined to be 23 kDa. It utilizes various compounds as substrates, including 2-hydroxyethyl disulfide. Interestingly, we found that the purified thioltransferase also contains significant glutathione S-transferase activity.

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Nucleotide Sequence and Homology Analysis of phnC Gene Encoding Glutathione S-transferase from Pseudomonas sp.DJ77 (Pseudomonas sp. DJ77에서 Glutathione S-transferase를 암호하는 phnC 유전자의 염기서열과 상동성 분석)

  • 우희종;신명수;김성재;정용제;정안식;박광균;김영창
    • Korean Journal of Microbiology
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    • v.33 no.2
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    • pp.86-91
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    • 1997
  • Pseudomonas sp. DJ77로부터 클로닝된 glutathione S-transferase 유전자(phnC)의 염기서열을 결정하였다. 603bp의 open reading frame(ORF)이 존재하였고 개시코돈 앞에서 Shine-Dalgarno sequence를, 종결코돈 뒤에서는 terminator sequence를 발견하였다. phnC 유전자에서 만들어지는 phnC 단백질은 21,416 Da으로 SDS-polyacrylamide gel 전기영동 결과와 일치하였다. PhnC는 Bulkholderia cepacia LB400, Cycloclasticus oligotrophus RB1의 GST와 각각 53.7%, 49%의 높은 상동성을 나타냈다. 아미노산 서열의 상동성과 필수잔기들의 존재유무로 판단할 때 PhnC GST는 theta class GSTs와 진화적으로 유연관계가 높았지만 alpha, mu, pi, sigma class GSTs에서 구조적, 기능적으로 중요하다고 알려진 아미노산 잔기들이 PhnC GST에도 보존되어 있었다. 또한, phnC 유전자의 위치가 C. oligotrophus RB1, B. cepacia LB400 등의 GST 유전자 위치와 유사하다는 점에서 PhnC 효소는 난분해성 방향족 탄화수소의 분해에 관여하는 것으로 생각된다.

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Functional analysis of Tyr7 residue in human glutathione S-transferase P1-1 (Human glutathione S-transferase 중 tyrosine 7 잔기의 기능 분석)

  • Kong, Kwang-Hoon;Park, Hee-Joong;Yoon, Suck-Young;Cho, Sung-Hee
    • 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.

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Protective Effect of Diallyl Disulfide on the Carbon Tetrachloride-Induced Hepatotoxicity in Mice (Diallyl Disulfide 가 사염화탄소에 의한 마우스 간손상에 미치는 영향)

  • 이상일;김승희;조수열
    • 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.

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Antioxidant Enzyme Activity in Rat Liver and Kidney Related to Coix Intake

  • Kim, Kyeok;Lee, Mie-Soon
    • 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.

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