• Title, Summary, Keyword: glutathione S-transferase M3

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Inhibition of glutathion-S-transferase and amidase by impurities in technical grade benfuracarb (Benfuracarb 원제에 함유된 불순물들의 glutathione-S-transferase와 amidase 저해 특성)

  • Yum, Chang-Sub;Kim, Song-Mun;Yu, Ji-Sook;Hur, Jang-Hyun
    • The Korean Journal of Pesticide Science
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    • v.6 no.1
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    • pp.31-35
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    • 2002
  • Objectives of this study were to determine if impurities in technical grade benfuracarb inhibit glutathione-S-transferase and amidase and to identify structures of impurities in technical grade benfuracarb. Technical grade benfuracarb, active ingredient, and impurity inhibited glutathione-S-transferase, and their $I_{50}$ were $9.7{\times}10^{-4}M,\;>1.0{\times}10^{-3}M,\;1.8{\times}10^{-4}M$, respectively. Such inhibition, however, was not higher than that by ethacrynic acid, a selective inhibitor to GST. Technical grade benfuracarb, active ingredient, and impurity also inhibited amidase, and their $I_{50}$ were $6.0{\times}10^{-5}M,\;4.3{\times}10^{-4}M,\;7.6{\times}10^{-5}M$, respectively. Our results show that the inhibition of both detoxifying enzymes by impurities in benfuracarb was 10-fold lower than that by active ingredient, suggesting that both active ingredient and impurities are involved in the inhibition of both detoxifying enzymes. Of four impurities (IM $1{\sim}4$) that were separated from technical grade benfuracarb, IM 2 and IM 3 inhibited GST and amidase. Based on data from IR, $^1H$-NMR, $^{13}C$-NMR and MS, it was determined that IM 2 is ethyl-N-isopropylamino propionate and IM 3 is ethyl-N-isopropyl-N(chlorosulfenyl)aminopropionate.

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.

Glutathione S-Transferase Activities of S-Type and L-Type Thioltransferases from Arabidopsis thaliana

  • Cho, Young-Wook;Park, Eun-Hee;Lim, Chang-Jin
    • BMB Reports
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    • v.33 no.2
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    • pp.179-183
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    • 2000
  • The glutathione S-transferase (GST) activities of S-type and L-type thioltransferases (TTases), which are purified from the seeds and leaves of Arabidopsis thaliana, respectively, were identified and compared. The S-type and L-type TTases showed $K_m$ values of 9.72 mM and 3.18mM on 1-chloro-2,4-dinitrobenzene (CDNB), respectively, indicating the L-type TTase has higher affinity for CDNB. The GST activity of the L-type TTase was rapidly inactivated after being heated at $70^{\circ}C$ or higher. The GST activity of the S-type TTase remains active in a range of $30-90^{\circ}C$. $Hg^{2+}$ inhibited the GST activity of the S-type TTase, whereas $Ca^{2+}$ and $Cd^{2+}$ inhibited the GST activity of the L-type TTase. Our results suggest that the GST activities of two TTases of Arabidopsis thaliana may have different catalytic mechanisms. The importance of the co-existence of TTAse and GST activities in one protein remains to be elucidated.

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Characterization of a Novel Glutathione S-Transferase from Pseudomonas sp. DJ77

  • Jung, U-Hee;Cho, Young-Sik;Seong, Hark-Mo;Kim, Seong-Jae;Kim, Young-Chang;Chung, An-Sik
    • BMB Reports
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    • v.29 no.2
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    • pp.111-115
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    • 1996
  • A novel glutathione S-transferase from Pseudomonas sp. DJ77 was expressed in E. coli and purified by glutathione-affinity chromatography. The enzyme was composed of two identical subunits. The molecular size of the enzyme was 42 kDa by sephadex G-150 gel permeation chromatography and Mr of each subunit was 23 kDa by sodium dodecylsulfate-polyacrylamide gel electrophoresis. pI value of the enzyme was approximately 5.8 by isoelectric focusing. This enzyme showed the highest activity toward 1-chloro-2,4-dinitrobenzene as the electrophilic substrate. The relative activities toward p-nitrobenzyl chloride and 1,2-dichloro-4-nitrobenzene were 3.8% and 1.3% of the activity toward 1-chloro-2,4-dinitrobenzene, respectively. $K_m$ and $V_{max}$ values for 1-chloro-2,4-dinitrobenzene calculated by Lineweaver-Burk plot were 0.76 mM and $14.81\;{\mu}mol/min/mg$, respectively, and those for glutathione were 6.23 mM and $64.93\;{\mu}mol/min/mg$, respectively. The enzyme showed highest glutathione S-transferase activity at pH 8.0 and was stable between pH 6.0 and 9.0. The enzyme retained its activity up to $35^{\circ}C$ for 90 min but was unstable above $45^{\circ}C$.

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Antioxidant Activities of Citrus unshiu Extracts obtained from Different Solvents (추출용매에 따른 진피 추출물의 항산화 활성)

  • Lee, Sung-Gu;Oh, Sung-Cheon;Jang, Jae-Seon
    • The Korean Journal of Food And Nutrition
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    • v.28 no.3
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    • pp.458-464
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    • 2015
  • In this study, the total polyphenol content, electron donating ability (EDA) and inhibitory activity of glutathione S-transferase (GST) of freeze-dried Citrus unshiu extracts were examined. The Citrus unshiu extracts was obtained from four solvents such as ethyl acetate, acetone, methyl chloride and methanol, to evaluate its functional properties. Total polyphenol contents were measured in the two different extracts, and the extracts were screened for their potential antioxidant activities using tests such as electron donating ability (EDA), glutathione S-transferase (GST). The total polyphenol contents of Citrus unshiu extracts were $928.48{\pm}1.19{\mu}g\;GAE/mL$ in ethyl acetate (EA), $886.03{\pm}0.44{\mu}g\;RE/mL$ in acetone (AC), $413.08{\pm}1.39{\mu}g\;GAE/mL$ in methylene chloride (MC), $12,648.60{\pm}0.56{\mu}g\;GAE/mL$ in methanol (MeOH), respectively. Also, the total polyphenol contents of EtOH Citrus unshiu extracts were $664.64{\pm}0.74{\mu}g\;GAE/mL$ in EA, $702.67{\pm}0.85{\mu}g\;RE/mL$ in AC, $429.64{\pm}0.61{\mu}g\;GAE/mL$ in MC, $16,108{\pm}0.73{\mu}g\;GAE/mL$ in MeOH, respectively. The total polyphenol contents were significantly difference (p<0.05) between the solvents. The electron donating ability of Citrus unshiu extracts were $62.80{\pm}0.36%$ in EA, $97.43{\pm}0.51%$ in AC, $52.20{\pm}0.30%$ in MC, $97.63{\pm}0.46%$ in MeOH, respectively. Also, the electron donating ability of EtOH Citrus unshiu extracts were $51.49{\pm}0.26%$ in EA, $63.17{\pm}0.31%$ in AC, $67.68{\pm}0.55%$ in MC, $96.18{\pm}0.41%$ in MA, respectively. The electron donating ability were significantly difference (p<0.05) between the solvents. The inhibitory activity of glutathione S-transferase in Citrus unshiu extracts were $76.22{\pm}0.65%$ in EA, $31.73{\pm}0.48%$ in MC, $97.48{\pm}0.56%$ in MeOH, respectively. Also, inhibitory activity of glutathione S-transferase in EtOH Citrus unshiu extracts were $75.54{\pm}0.55%$ in EA, $73.53{\pm}0.38%$ in MC, $48.70{\pm}0.46%$ in MeOH, respectively. The inhibitory activity of glutathione S-transferase were significantly difference (p<0.05) between the solvents. These results indicated that the Citrus unshiu extracts is a high-valued food ingredient and the extraction with methanol will be useful as a nutritional source with natural antioxidant activities. Considering high consumer demand beneficial health effects, Citrus unshiu extracts can be utilized to develop functional food health- promoting and natural antioxidant agents.

Crystallization of 28 kDa Clonochis sinesis Glutathione S-transferase

  • Kim, Young-Kwan;Chung, Yong-Je
    • Korean Journal of Crystallography
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    • v.14 no.1
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    • pp.32-34
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    • 2003
  • A helminth glutathione S-transferase. 28 kDa isozyme from Clonorchis sinensis has been crystallized under several conditions. One of the crystals, grown from a 10% polyehtylene glycol MME 550 (PEG MME 5 K) solution in 0.05 M potassium phosphate buffer (pH 7.0), diffracts to $3.0{\AA}$ resolution, and belongs to monoclinic space group C2, with unit cell parameters $a=95.83{\AA}$, $b=63.82{\AA}$, $c=235.09{\AA}$, and ${\beta}=97.2^{\circ}$.

Glutathione-S-transferase Activity and its Changes to Chemical Pollution in Edible Shells and Fishes (식용 어패류 조직중의 glutathione S-transferase 활성과 화학물질 오염에 의한 변화)

  • Song, Mi-Ran;Choe, Sun-Nam;Park, Kwan-Ha
    • 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.

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Tolerance Mechanism to Simazine in Coix lacryma-jobi (율무(Coix lacryma-jobi)의 제초제 Simazine에 대한 내성기구)

  • Ma, Sang-Yong;Kim, Jong-Seok;Chun, Jae-Chul
    • Korean Journal of Environmental Agriculture
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    • v.16 no.1
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    • pp.37-43
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    • 1997
  • Tolerance mechanism to simazine (6-chloro-N,N'-diethyl-1,3,5-triazine-2,4-diamine) in Coix lacryma-jobi was investigated with respect to herbicide detoxification via glutathione conjugation. Simazine was initially absorbed by seedlings of C. lacryma-jobi and corn, but after 12 hours of treatment, no significant difference in simazine absorption was found in both species. Simazine absorbed was rapidly metabolized to glutathione-simazine conjugate. One to six hours after treatment, metabolism was approximately 2-fold faster in C. lacryma-jobi than in corn. Glutathione content was found 1.5- and 2.3-fold higher in coleoptile and root of C. lacryma-jobi, respectively, compared with corn. In both species, the highest concentration of glutathione was found in coleoptile tissue. Glutathione S-transferase that exhibits activity with 1-chloro-2,4-dinitrobenzene was not significantly different between two species. However, glutathione S-transferase activity with simazine was approximately 2-fold greater in C. lacryma-jobi than in corn. The glutathione S-transferase activity was 20 to 30% greater in shoot of either species than in root. Fast protein liquid chromatography-anion exchange column was used to separate glutathione S-transferase isozymes in coleoptiles of C. lacryma-jobi and corn. A peak of glutathione S-transferase activity with 1-chloro-2,4-dinitrobenzene and two peaks of glutathione S-transferase activity with simazine from C. lacryma-jobi were coeluted with those from corn, but showed greater activity than in the case of corn. Another glutathione S-transferase isozyme that exhibits activity with simazine was detected in the elution of C. lacryma-jobi extract, but not in corn. Electron transport in chloroplast thylakoids isolated from leaves of both species was equally sensitive to simazine applied at 1 to 100 nM. These results indicate that the simazine tolerance in C. lacryma-jobi is due to its capacity to detoxify the herbicide via glutathione conjugation, which is positively correlated with the level of glutathione content and glutathione S-transferase activity.

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Glutathione S-transferase M1 Null Genotype and Hepatocellular Carcinoma Susceptibility in China and India: Evidence from an Updated Meta-analysis

  • Liu, Hong-Zhou;Peng, Jie;Peng, Chun-Yan;Yan, Ming;Zheng, Fang
    • Asian Pacific Journal of Cancer Prevention
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    • v.15 no.12
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    • pp.4851-4856
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    • 2014
  • Background: Glutathione S-transferase M1 (GSTM1) have been reported to be associated with hepatocellular carcinoma. However, the effect of the GSTMl null genotype was divergent in the literature and we therefore performed the present meta-analysis to explore the relationship in detail. Materials and Metbods: Reported studies were searched from 1990 to March 1, 2014 in PubMed and Wanfang Med Online. The total odds oatio (OR) and 95% CI were calculated and analyzed by Review Manager 5.1 and STATE 12. Results: Total OR was calculated from 26 articles with 3,769 cases and 5,517 controls and the association proved significant (OR [95%CI]=1.50 [1.25, 1.80], P<0.05) in the Chinese population. However, there was no significant association between hepatocellular carcinoma risk among subjects carrying the GSTM1 null genotype (OR [95%CI]=1.20 [0.88-1.64], P=0.24) in subgroups of publication in English and in Indian populations (OR [95%CI]=1.80 [0.80-4.20], P=0.15). Conclusions: The GSTM1 deletion polymorphism might not have a significant effect on the susceptibility of hepatocellular carcinoma overall.

Glutathione S-Transferase T1 and M1 Polymorphisms and Risk of Uterine Cervical Lesions in Women from Central Serbia

  • Stosic, Ivana;Grujicic, Darko;Arsenijevic, Slobodan;Brkic, Marija;Milosevic-Djordjevic, Olivera
    • Asian Pacific Journal of Cancer Prevention
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    • v.15 no.7
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    • pp.3201-3205
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    • 2014
  • The aim of this study was to investigate the frequencies of GSTT1 and GSTM1 deletion polymorphisms in newly-diagnosed patients with uterine cervical lesions from central Serbia. Polymorphisms of GST genes were genotyped in 97 patients with cervical lesions and 50 healthy women using a multiplex polymerase chain reaction (PCR). The GSTM1 null genotype was significantly more prominent among the patients than in controls (74.2% vs 56.0%), the risk associated with lesions being almost 2.3-fold increased (OR=2.26, 95%CI=1.10-4.65, p=0.03) and 3.17-fold higher in patients above >45 years old (95%CI=1.02-9.79, p=0.04). The analysis of the two genotypes demonstrated that GSTM1 null genotype significantly increased risk only for low grade squamous intraepithelial lesion-LSIL (OR=2.81, 95%CI=1.03-7.68, p=0.04). GSTT1 null genotype or different genotype combinations were not found to be risk factors, irrespective to lesion stages, age or smoking. We found that the risk of cervical lesions might be significantly related to the GSTM1 null genotype, especially in women aged above 45 years. Furthermore, the GSTM1 polymorphism might have greater role in development of early stage lesions.