• Title/Summary/Keyword: S-transferase

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Induction of NAD(P)H:quinone reductase and glutathione S-transferase by Xanthii Fructus and Prunellae Spica Extracts (창이자 및 꿀풀하고초에 의한 NAD(P)H:quinone reductase와 glutathione S-transferase의 유도)

  • Shon, Yun-Hee;Lee, Ki-Taek;Park, Sin-Hwa;Cho, Kyoung-Hee;Lim, Jong-Kook;Nam, Kyung-Soo
    • Korean Journal of Pharmacognosy
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    • v.32 no.4 s.127
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    • pp.269-273
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    • 2001
  • Ethanol extracts from Xanthii Fructus (XFE) and Prunellae Spica (PSE) were investigated for the effects on the induction of cancer chemoprevention-associated enzymes. The following effects were measured: (a) induction of quinone reductase (QR) (b) induction of glutathione S-transferase (GST) (c) reduced glutathione (GSH) level. XFE and PSE were potent inducers of quinone reductase activity in Hepa1c1c7 murine hepatoma cells. Glutathione levels were increased with XFE and PSE. In addition, glutathione S-transferase activity was increased with XFE. However, GST activity was not increased with PSE. These results suggest that XFE and PSE have chemopreventive potentials by inducing quinone reductase and increasing GSH levels.

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The GSTP1 Ile105Val Polymorphism is not Associated with Susceptibility to Colorectal Cancer

  • Khabaz, Mohamad Nidal
    • Asian Pacific Journal of Cancer Prevention
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    • v.13 no.6
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    • pp.2949-2953
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    • 2012
  • The glutathione S transferase (GST) family is a major part of cellular defense mechanisms against endogenous and exogenous substances, many of which have carcinogenic potential. Alteration in the expression level or structure of the glutathione-S-transferase (GST) enzymes may lead to inadequate detoxification of potential carcinogens and consequently contribute to cancer development. A member of the glutathione-S-transferase (GST) family, GSTP1, is an attractive candidate for involvement in susceptibility to carcinogen-associated colorectal cancer. An $Ag{\rightarrow}G$ transition in exon 5 resulting in an Ile105Val amino acid substitution has been identified which alters catalytic efficiency. The present study investigated the possible impact of Ile105Val GSTP1 polymorphism on susceptibility to colorectal cancer. in Jordan We examined 90 tissue samples previously diagnosed with colorectal carcinoma, and 56 non-cancerous colon tissues. DNA was extracted from paraffin embedded tissues and the status of the GSTP1 polymorphism was determined using a polymerase chain reaction restriction fragment length polymorphism (RFLP) method. No statistically significant differences were found between colorectal cancer cases and controls for the GSTP1 Ile/Ile, Ile/Val and Val/Val genotypes. The glutathione S-transferase polymorphism was not associated with risk in colorectal cancer cases in Jordan stratified by age, sex, site, grade or tumor stage. In conclusion, the GSTP1 Ile105Val polymorphism is unlikely to affect the risk of colorectal cancer.

A Study of Glutathione S-transferase Inhibitors obtained from Allium cepa var. cepa Extract (양파 추출물에서의 글루타티온 전달효소 활성 저해제에 관한 연구)

  • Lee, Kwang-Soo;Park, Kyung-Sook
    • The Korean Journal of Food And Nutrition
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    • v.26 no.4
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    • pp.725-730
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    • 2013
  • In this study, an ethanol extract being obtained from Allium cepa var. cepa examins the inhibitory effects on the glutathione S-transferase and the separation had been done by silica-gel column chromatography using various eluents, such as ethyl acetate, methanol, and 50% methanol. A volume of column fraction was 50ml and evaporation has been performde by the rotary evaporator under reduced pressure. Each fraction is being examined by thin layer chromatography and the UV spectrum at 365 nm was used to investigate separation patterns of spots on thin layer chromatography. When the eluent was changed, the spot patterns showed another different pattern on thin layer chromatography, so on. Fractions showing similar pattern are combined and eventually, three fractions are obtained. Each fraction is testified to examine the inhibition effects on glutathione S-transferase. All of these showed inhibition effects on glutathione S-transferase. The GC-MS shows that each fraction contains more than 2 compounds.

Effect of Bromobenzene Pretreatment on the Hepatic Glutathione Content and Glutathione S-transferase Activity in Bromobenzene Treated Rats (흰쥐에 있어서 Bromobenzene전처치가 간조직 중 Glutathione 및 Glutathione S-transferase활성에 미치는 영향)

  • 신중규
    • Journal of Environmental Health Sciences
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    • v.23 no.2
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    • pp.83-88
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    • 1997
  • To evaluate the effect of bromobenzene pretreatment on the bromobenzene metabolism, the animal group was induced the stage of slight liver damage with 7 times bromobenzene injection every two days (400 mg/kg body wt. i.p.). In the present experimental animal model, the single dose of bromobenzene(400 mg/kg body wt. i.p.) was injected to the bromobenzene-pretreated rats and the hepatic aniline hydroxylase(AH) activity, glutathione(GSH) content and glutathione S-transferase (GST) activity were determined at the intervals of 2, 4, 8, 24 hours throughout 24 hr. The activities of hepatic AH and GST were generally higher in bromobenzene-pretreated rats than those in normal group throughout the whole course of experiment. Furthermore, the decreasing rate of hepatic GSH content was also higher in bromobenzene pretreated rats than in normal rats. Moreover, the value of V$_{max}$ in hepatic GST was higher in bromobenzene pretreated rats than that in the normal rats. In conclusion, these results indicate that the pretreatment of bromobenzene may rather enhance the bromobenzene metabolism.

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Insecticidal activity of thiodicarb on lepidopterous pests (나방류에 대한 thiodicarb의 살충활성)

  • Choi, Yu-Mi;Kim, Gil-Hah
    • The Korean Journal of Pesticide Science
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    • v.8 no.1
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    • pp.16-21
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    • 2004
  • A series of experiments was conducted to determine the toxicities of thiodicarb on the six lepidopterous pests (Pseudaletia separata, Plutella xylostella, Palpita indica, Spodoptera exigua, Helicoverpa assulta, Spodoptera litura) and to elucidate factors insecticidal effects mechanism of thiodicarb. Thiodicarb was very effective against six lepidopterous young larvae, but less effective to the old larvae and it acted slowly. Thiodicarb inhibited acetylcholinesterase and glutathione S-transferase activities, but not inhibit esterase activity.

Molecular Cloning and mRNA Expression a Glutathione S-Transferase cDNA from the Spider, Araneus ventricosus

  • Shin, Geun Ho;Kim, Hyung Suk;Kwon, Dong Wook;Lee, Jin Young;Byeon, Gyeong Min;Sohn, Hung Dae;Jin, Byung Rae
    • International Journal of Industrial Entomology and Biomaterials
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    • v.9 no.1
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    • pp.65-71
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    • 2004
  • A fat body-specific glutathione S-transferase cDMA was cloned from the spider, Araneus ventricosus. The cDNA encoding A. ventricosus glutathione S-transferase (AvGST) is 645 base pairs long with an open reading frame of 215 amino acid residues with a calculated molecular weight of approximately 24 kDa. Northern blot analysis showed the tissue-specifically expression of AvGST in the A. ventricosus fat body.

Glutathione S-transferase Activity and Hyaluronidase Inhibitory Effect of Medicinal Plants (생약의 Glutathione S-transferase 활성과 Hyaluronidase 저해효과)

  • Lee, Eun-Hee;Cho, Jae-Yong;Cha, Bae-Cheon
    • Korean Journal of Pharmacognosy
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    • v.35 no.3 s.138
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    • pp.184-188
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    • 2004
  • This study was carried out to evaluate glutathione S-transferase (GST) activity and hyaluronidase inhibitory effect of medicinal plants. The EtOH extracts of 20 species plants were tested. As the result, Acorus gramineus and Pueraria lobata exhibited GST activity. On the continuous experiment, the n-BuOH fraction of Acorus gramineus and the $H_2O$ fraction of Pueraria lobata showed the elevation of GST activity. On the experiment of hyaluronidase inhibitory effect, Acorus gramineus exhibited a potent inhibitory activity. These results suggest that the extract of Acorus gramineus can be applicable for the development of a new anti-inflammatory agent.

Synergistic action of pesticide mixtures using glutathione-s-transferase- and esterase-inhibiting properties in diamondback moth (Plutella xylostella L.) (Glutathione-S-transferase와 esterase 효소 저해특성을 이용한 농약의 혼합 상승효과)

  • Yu, Yong-Man;Hong, S.S.;Kim, S.;Hur, J.H.
    • The Korean Journal of Pesticide Science
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    • v.7 no.1
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    • pp.38-44
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    • 2003
  • In vitro inhibitory activity of 34 insecticides and 31 fungicides to glutathione-S-transferase and esterases extracted from rats was determined. Of tested pesticides, the pesticides with high activity on both detoxifying enzymes were mixed with pesticides that are known to be detoxified by detoxifying enzymes. Glutathione-S-transferase was inhibited by thiodicarb $(I_{50}:1.87\times10^{-4}M)$, thiocyclam $(7.40\times10^{-4}M)$, dithianon $(7.55\times10^{-5}M)$, and tolylfluanide $(8.66\times10^{-5}M)$, while esterases by dichlorvos $(8.95\times10^{-8}M)$, pirimicarb $(2.74\times10^{-6}M)$, pyrazophos $(3.31\times10^{-5}M)$, and benomyl $(4.96\times10^{-5}M)$. After acephate known to be detoxified by glutathione-S-transferase was mixed with glutathione-S-transferase-inhibiting pesticides and phenthoate known to be detoxified by esterases was mixed with esterases-inhibiting pesticides, insecticidal activities of such mixtures were determined against diamondback moth (PlutelLa xylostella L.). Synergistic action was observed in all pesticide combinations. The highest synergistic action was obtained when phenthoate was combined with dichlorvos, showing that co-toxicity coefficients were 1512 and 1877 after 24 and 48 hours of treatment, respectively. Several other combinations of pesticides, such as phenthoate with benomyl, and acephate with dithianon, also showed synergism, showing that their co-toxicity coefficients were about 1,000 and 500, after 24 hours of treatment, respectively. Our results showed that combinations of pesticides inhibited by detoxifying enzymes and ones detoxified by detoxifying enzymes resulted in increased toxicities of pesticides, suggesting that such combinations could be used to develop pesticide mixtures with more broad spectrum and high effectiveness.

Study on the immobilization of plant glutathione S-transferase for development of herbicide detection kit (제초제 검출 키트 개발을 위한 식물 해독효소 고정화 연구)

  • Cho, Hyun-Young;Lee, Jin-Joo;Kong, Kwang-Hoon
    • Analytical Science and Technology
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    • v.23 no.2
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    • pp.172-178
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    • 2010
  • Glutathione S-transferase is known to play a crucial role in detoxification in many cases. To develop a herbicide detection biosensor, we in this study attempted to immobilize glutathione S-transferase enzyme on solid supports, polystyrene and agarose, and Na-alginate. These matrixes were attractive materials for the construction of biosensors and might also have utility for the production of immobilized enzyme bioreactors. We also compared the activities of glutathione-S-transferase immobilized OsGSTF3 and free OsGSTF3. The specific activity of the free enzyme in solution was 3.3 higher than the immobilized enzyme. These results suggest that 50% of the enzyme was bound with the catalytic site in polystyrene-alkylamine bead and immobilized enzymes showed 80% remaining activity until 3 times reuse.

An Efficient System for the Expression and Purification of Yeast Geranylgeranyl Protein Transferase Type I

  • Kim, Hyun-Kyung;Kim, Young-Ah;Yang, Chul-Hak
    • BMB Reports
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    • v.31 no.1
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    • pp.77-82
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    • 1998
  • To purify the geranylgeranyl protein transferase type I (GGPT-I) efficiently, a gene expression system using the pGEX-4T-1 vector was constructed. The cal1 gene, encoding the ${\beta}$ subunit of GGPT-I, was subcloned into the pGEX-4T-1 vector and co-transformed into E. coli cells harboring the ram2 gene, the ${\alpha}$ subunit gene of GGPT-I. GGPT-I was highly expressed as a fusion protein with glutathione S-transferase (GST) in E. coli, purified to homogeneity by glutathione-agarose affinity chromatography, and the GST moiety was excised by thrombin treatment. The purified yeast GGPT-I showed a dose-dependent increase in the transferase activity, and its apparent $K_m$ value for an undecapeptide fused with GST (GST-PEP) was $0.66\;{\mu}M$ and the apparent value for geranylgeranyl pyrophosphate (GGPP) was $0.071\;{\mu}M$.

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