scholarly journals Analyses of Genetic Variations of Glutathione S-Transferase Mu1 and Theta1 Genes in Bangladeshi Tannery Workers and Healthy Controls

2016 ◽  
Vol 2016 ◽  
pp. 1-8 ◽  
Author(s):  
Jobaida Akther ◽  
Akio Ebihara ◽  
Tsutomu Nakagawa ◽  
Laila N. Islam ◽  
Fumiaki Suzuki ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Study Groups ◽  
Detoxification Enzymes ◽  
Healthy Controls ◽  
Glutathione S Transferase ◽  
Double Positive ◽  
Allelic Variants ◽  
Glutathione S Transferases ◽  
Tannery Workers ◽  
Gst Activity

Glutathione S-transferases (GSTs) belong to a group of multigene detoxification enzymes, which defend cells against oxidative stress. Tannery workers are at risk of oxidative damage that is usually detoxified by GSTs. This study investigated the genotypic frequencies of GST Mu1 (GSTM1) and GST Theta1 (GSTT1) in Bangladeshi tannery workers and healthy controls followed by their status of oxidative stress and total GST activity. Of the 188 individuals, 50.0% had both GSTM1 and GSTT1 (+/+), 12.2% had GSTM1 (+/−), 31.4% had GSTT1 (−/+) alleles, and 6.4% had null genotypes (−/−) with respect to both GSTM1 and GSTT1 alleles. Among 109 healthy controls, 54.1% were double positive, 9.2% had GSTM1 allele, 32.1% had GSTT1 allele, and 4.6% had null genotypes. Out of 79 tannery workers, 44.3% were +/+, 16.8% were +/−, 30.5% were −/+, and 8.4% were −/−. Though the polymorphic genotypes or allelic variants of GSTM1 and GSTT1 were distributed among the study subjects with different frequencies, the differences between the study groups were not statistically significant. GST activity did not vary significantly between the two groups and also among different genotypes while level of lipid peroxidation was significantly higher in tannery workers compared to controls irrespective of their GST genotypes.

Chemoprotective Effects of Propolis on Aflatoxin B1-Induced Hepatotoxicity in Rats: Oxidative Damage and Hepatotoxicity by Modulating TP53, Oxidative Stress

2020 ◽  
Vol 17 (3) ◽  
pp. 191-199
Author(s):  
Seval Yilmaz ◽  
Fatih Mehmet Kandemir ◽  
Emre Kaya ◽  
Mustafa Ozkaraca
Keyword(s):  
Oxidative Stress ◽  
Gene Expression ◽  
Oxidative Damage ◽  
Aflatoxin B1 ◽  
Tp53 Gene ◽  
Control Group ◽  
Glutathione S Transferase ◽  
Gene Expressions ◽  
Cat Gene ◽  
Gst Activity

Objective: This study aimed to detect hepatic oxidative damage caused by aflatoxin B1 (AFB1), as well as to examine how propolis protects against hepatotoxic effects of AFB1. Method: Rats were split into four groups as control group, AFB1 group, propolis group, AFB1+ propolis group. Results: There was significant increase in malondialdehyde (MDA) level and tumor suppressor protein (TP53) gene expression, Glutathione (GSH) level, Catalase (CAT) activity, CAT gene expression decreased in AFB1 group in blood. MDA level and Glutathione-S-Transferase (GST) activity, GST and TP53 gene expressions increased in AFB1 group, whereas GSH level and CAT activity alongside CAT gene expression decreased in liver. AFB1+propolis group showed significant decrease in MDA level, GST activity, TP53 and GST gene expressions, GSH level and CAT activity and CAT gene expression increased in liver compared to AFB1 group. Conclusion: These results suggest that propolis may potentially be natural agent that prevents AFB1- induced oxidative stress and hepatotoxicity.

scholarly journals Variability of Glutathione S-Transferase α in Human Liver and Plasma

1999 ◽  
Vol 45 (3) ◽  
pp. 355-359 ◽  
Author(s):  
Theo PJ Mulder ◽  
Daniel A Court ◽  
Wilbert HM Peters
Keyword(s):  
Aspartate Aminotransferase ◽  
Alanine Aminotransferase ◽  
Human Liver ◽  
Organ Donors ◽  
Healthy Controls ◽  
Plasma Samples ◽  
Glutathione S Transferase ◽  
Glutathione S Transferases ◽  
The Mean ◽  
Exogenous Compounds

Abstract Background: Glutathione S-transferases are a family of enzymes involved in the binding, transport, and detoxification of a wide variety of endogenous and exogenous compounds. Little information is available about the variability of class α glutathione S-transferases in human liver, where they are highly expressed, or in serum. Methods: Both total class α glutathione S-transferase (GST-α, composed of GSTA1-1, GSTA1-2, and GSTA2-2) as well as GSTA1-1 concentrations were measured by specific and sensitive ELISA in liver cytosols of 35 organ donors and in plasma samples of 350 healthy controls. Results: The mean total GST-α and GSTA1-1 in liver cytosols were 25.1 ± 9.4 and 10.7 ± 5.3 μg/mg protein, respectively, and did not correlate with activities of aspartate aminotransferase or alanine aminotransferase. The mean total GST-α in liver was significantly higher in females compared with males (28.8 ± 10.0 vs 22.0 ± 7.8 μg/mg protein; P <0.05). In contrast, the median total GST-α in plasma was lower in females compared with males (2.0 and 2.8 μg/L, respectively; P <0.0001). The median ratios for GSTA1-1/total GST-α in liver and plasma were 0.42 and 0.58, respectively. Conclusions: GSTA1-1 constitutes approximately one-half of the total amount of α class GSTs in human plasma and liver. Total GST-α values are higher in female liver but lower in plasma compared with the respective values in males.

Microsomal Detoxification Enzymes in Yam Bean [Pachyrhizus erosus (L.) Urban]

2004 ◽  
Vol 59 (9-10) ◽  
pp. 693-700 ◽  
Author(s):  
Ebenezer J. D. Belford ◽  
Ulrike Dörfler ◽  
Andreas Stampf ◽  
Peter Schröder
Keyword(s):  
Cytochrome P450s ◽  
Detoxification Enzymes ◽  
Image Description ◽  
Fluorescence Image ◽  
Catalysed Reaction ◽  
Pachyrhizus Erosus ◽  
Glutathione S Transferases ◽  
Enzyme Families ◽  
First Time ◽  
Gst Activity

Abstract Cytochrome P450s and glutathione-S-transferases (GSTs) constitute two of the largest groups of enzyme families that are responsible for detoxification of exogenous molecules in plants. Their activities differ from plant to plant with respect to metabolism and substrate specificity which is one of the reasons for herbicide selectivity. In the tuber forming yam bean, the legume Pachyrhizus erosus, their activities at the microsomal level were investigated to determine the detoxification status of the plant. The breakdown of the herbicide isoproturon (IPU) to two distinct metabolites, 1-OH-IPU and monodesmethyl-IPU, was demonstrated. GST activity was determined with model substrates, but also by the catalysed formation of the fluorescent glutathione bimane conjugate. This study demonstrates for the first time microsomal detoxification activity in Pachyrhizus and the fluorescence image description of microsomal GST catalysed reaction in a legume.

Influence of Chemical Treatments on Glutathione S-Transferases of Maize with Activity Towards Metolachlor and Cinnamic Acid

1998 ◽  
Vol 53 (11-12) ◽  
pp. 973-979 ◽  
Author(s):  
Charles K. Cottingham ◽  
Kriton K. Hatzios ◽  
Sue Meredith
Keyword(s):  
Cinnamic Acid ◽  
Zea Mays L ◽  
Glutathione S Transferase ◽  
Chemical Treatments ◽  
Etiolated Seedlings ◽  
Glutathione S Transferases ◽  
Membrane Bound ◽  
Herbicide Metolachlor ◽  
Triton X ◽  
Gst Activity

Abstract The subcellular distribution of glutathione S-transferase (GST) activity extracted from shoots of 3-day-old etiolated seedlings of maize (Zea mays L., Northrup-K ing 9283 hybrid) and the induction of soluble and m em brane-bound G ST activity by the safener benoxacor, the herbicide metolachlor and their com bination (CGA -180937) were investigated. GST activity extracted from maize shoots was detected in both cytosolic and microsomal fractions and utilized l-chloro-2,4-dinitrobenzene (CDNB ), metolachlor, and trans-cinnamic acid (CA) as substrates. Soluble GST activity extracted from maize shoots was greater than m icrosom al with CDNB or metolachlor as substrate. Membrane-bound GT activity was greater than soluble with cinnamic acid as substrate. W ashing the microsomal preparations from maize shoots with Triton X-100 increased GST (C A ) activity. Pretreatment with the safener benoxacor or a form ulated combination of the herbicide metolachlor with benoxacor induced soluble GST(CDNB ), GST(metolachlor) and GST (C A ) activities in m aize shoots. Benoxacor and CGA-180937 induced also membrane-bound GST (CDNB ) and GST(CA ) activities in maize shoots, but did not affect membrane-bound GST (metolachlor) activity. These results confirm that maize contains multiple GST isozymes that differ in their subsrate specificity and inducibility by safeners or other chemicals.

scholarly journals Tryptophan Metabolism, Inflammation, and Oxidative Stress in Patients with Neurovascular Disease

Metabolites ◽  
2020 ◽  
Vol 10 (5) ◽  
pp. 208 ◽  
Author(s):  
Martin Hajsl ◽  
Alzbeta Hlavackova ◽  
Karolina Broulikova ◽  
Martin Sramek ◽  
Martin Maly ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Ischemic Stroke ◽  
Study Groups ◽  
Healthy Controls ◽  
Vascular Events ◽  
Liquid Chromatography Tandem Mass ◽  
Important Player ◽  
Hydroxyanthranilic Acid ◽  
Relationship Of ◽  
The Relationship

Atherosclerosis is a leading cause of major vascular events, myocardial infarction, and ischemic stroke. Tryptophan (TRP) catabolism was recognized as an important player in inflammation and immune response having together with oxidative stress (OS) significant effects on each phase of atherosclerosis. The aim of the study is to analyze the relationship of plasma levels of TRP metabolites, inflammation, and OS in patients with neurovascular diseases (acute ischemic stroke (AIS), significant carotid artery stenosis (SCAS)) and in healthy controls. Blood samples were collected from 43 patients (25 with SCAS, 18 with AIS) and from 25 healthy controls. The concentrations of twelve TRP metabolites, riboflavin, neopterin (NEO, marker of inflammation), and malondialdehyde (MDA, marker of OS) were measured by liquid chromatography–tandem mass spectrometry (LC-MS/MS). Concentrations of seven TRP metabolites (TRP, kynurenine (KYN), 3-hydroxykynurenine (3-HK), 3-hydroxyanthranilic acid (3-HAA), anthranilic acid (AA), melatonin (MEL), tryptamine (TA)), NEO, and MDA were significantly different in the studied groups. Significantly lower concentrations of TRP, KYN, 3-HAA, MEL, TA, and higher MDA concentrations were found in AIS compared to SCAS patients. MDA concentration was higher in both AIS and SCAS group (p < 0.001, p = 0.004, respectively) compared to controls, NEO concentration was enhanced (p < 0.003) in AIS. MDA did not directly correlate with TRP metabolites in the study groups, except for 1) a negative correlation with kynurenine acid and 2) the activity of kynurenine aminotransferase in AIS patients (r = −0.552, p = 0.018; r = −0.504, p = 0.033, respectively). In summary, TRP metabolism is clearly more deregulated in AIS compared to SCAS patients; the effect of TRP metabolites on OS should be further elucidated.

Bacterial peptide methionine sulphoxide reductase: co-induction with glutathione S-transferase during chemical stress conditions

2001 ◽  
Vol 360 (3) ◽  
pp. 675-681 ◽  
Author(s):  
Antonio TAMBURRO ◽  
Nerino ALLOCATI ◽  
Michele MASULLI ◽  
Domenico ROTILIO ◽  
Carmine DI ILIO ◽  
...  
Keyword(s):  
Polyclonal Antibodies ◽  
Mrna Level ◽  
Chemical Compounds ◽  
Stress Conditions ◽  
Detoxification Enzymes ◽  
Chemical Stress ◽  
Ochrobactrum Anthropi ◽  
Glutathione S Transferase ◽  
Cellular Protection ◽  
Glutathione S Transferases

Peptide methionine sulphoxide reductase (MsrA; EC 1.8.4.6) is a ubiquitous enzyme catalysing the reduction of methionine sulphoxide to methionine in proteins, while the glutathione S-transferases (GSTs) are a major family of detoxification enzymes. A gene homologous to MsrA was identified in a chromosomal fragment from the bacterium Ochrobactrum anthropi, and this gene is located just downstream of a GST gene identified previously (OaGST) [Favaloro, Tamburro, Angelucci, De Luca, Melino, Di Ilio and Rotilio (1998) Biochem. J. 335, 573–579]. This raises the question of whether the products of these two genes may be involved in a common cellular protection function. To test this hypothesis, the hypothetical MsrA protein has been overexpressed in Escherichia coli as a functional 51kDa GST fusion protein. Following cleavage with thrombin and purification, the soluble 24kDa protein showed MsrA activity with N-acetylmethionine sulphoxide as substrate, as well as with other sulphoxide compounds. Therefore polyclonal antibodies were raised against the recombinant protein, and the modulation of MsrA in this bacterium, grown in the presence of different stimulants simulating several stress conditions, was investigated. The level of expression of MsrA was detected both by measuring the mRNA level and by immunoblotting experiments, in addition to measuring its catalytic activity. MsrA is a constitutive enzyme which is also inducible by chemical stress involving phenolic compounds such as phenol and 4-chlorophenol. Recently we reported that the GST of this bacterium, like MsrA, is only modulated by toxic chemical compounds [Favaloro, Tamburro, Trofino, Bologna, Rotilio and Heipieper (2000) Biochem. J. 346, 553–559]; therefore this is the first indication of a co-induction of the MsrA and GST enzymes during chemical stress.

Tissue Distribution and Properties of Glutathione S-transferases in Micromelalopha troglodyta (Lepidoptera: Notodontidae)

2008 ◽  
Vol 43 (3) ◽  
pp. 268-278 ◽  
Author(s):  
Fang Tang ◽  
Xiu-Bo Zhang ◽  
Yu-Sheng Liu ◽  
Xi-Wu Gao
Keyword(s):  
Tissue Distribution ◽  
Tannic Acid ◽  
Fat Body ◽  
Inhibitory Effect ◽  
Transferase Activity ◽  
Glutathione S Transferase ◽  
Important Pest ◽  
Glutathione S Transferases ◽  
Gst Activity ◽  
Different Tissues

The small prominent, Micromelalopha troglodyta (Graeser) (Lepidoptera: Notodontidae), is an important pest of poplar in China. Glutathione S-transferases are known to be responsible for adaptation mechanisms of M. troglodyta. Thus, the tissue distribution and kinetic constants of glutathione S-transferase activity in the small prominent were studied. Significant differences in glutathione S-transferase (GST) activity and distribution percentages of GST activity and kinetic characteristics were observed among 4 tissues (head, midgut, fat body and integument). Furthermore, the inhibition of glutathione S-transferase activity in 4 tissues by 21 inhibitors was conducted. The results showed the inhibition of GST activity of different tissues by 21 inhibitors is different. For GST activity in heads, chlorpyrifos, profenofos, lambda-cyhalothrin, fipronil and quercetin were the best inhibitors tested. Tannic acid was the most potent inhibitor of midgut GST activity. In the fat body, GST activity was inhibited most by tannic acid, chlorpyrifos and profenofos. The inhibitory effect of profenofos and phoxim was highest for GST activity in the integument. Our results showed that glutathione S-transferases in different tissues are qualitatively different in isozyme composition and thus different in sensitivity to inhibitors.

scholarly journals Reciprocal regulation of glutathione S-transferase spliceforms and the Drosophila c-Jun N-terminal kinase pathway components

2004 ◽  
Vol 383 (3) ◽  
pp. 483-490 ◽  
Author(s):  
Rungrutai UDOMSINPRASERT ◽  
Marie A. BOGOYEVITCH ◽  
Albert J. KETTERMAN
Keyword(s):  
Binding Constants ◽  
Detoxification Enzymes ◽  
Mitogen Activated Protein Kinase ◽  
Glutathione S Transferase ◽  
Anopheles Dirus ◽  
Reciprocal Effect ◽  
Jnk Pathway ◽  
Reciprocal Regulation ◽  
Catalytic Function ◽  
Gst Activity

In mammalian systems, detoxification enzymes of the GST (glutathione S-transferase) family regulate JNK (c-Jun N-terminal kinase) signal transduction by interaction with JNK itself or other proteins upstream in the JNK pathway. In the present study, we have studied GSTs and their interaction with components of the JNK pathway from Diptera. We have evaluated the effects of four Delta class Anopheles dirus GSTs, GSTD1-1, GSTD2-2, GSTD3-3 and GSTD4-4, on the activity of full-length recombinant Drosophila HEP (mitogen-activated protein kinase kinase 7; where HEP stands for hemipterous) and the Drosophila JNK, as well as the reciprocal effect of these kinases on GST activity. Interestingly, even though these four GSTs are alternatively spliced products of the same gene and share >60% identity, they exerted different effects on JNK activity. GSTD1-1 inhibited JNK activity, whereas the other three GST isoforms activated JNK. GSTD2-2, GSTD3-3 and GSTD4-4 were inhibited 50–80% by HEP or JNK but GSTD1-1 was not inhibited by JNK. However, there were some similarities in the actions of HEP and JNK on these GSTs. For example, binding constants for HEP or JNK inhibiting a GST were similar (20–70 nM). Furthermore, after incubation of the GSTs with JNK, both JNK and the GSTs changed catalytic properties. The substrate specificities of both GSTs and JNK were also altered after their co-incubation. In addition, glutathione modulated the effects of JNK on GST activity. These results emphasize that different GST spliceforms possess different properties, both in their catalytic function and in their regulation of signalling through the JNK pathway.

scholarly journals RETRACTED ARTICLE: Silencing of Glutathione S-Transferase Pi Inhibits Cancer Cell Growth via Oxidative Stress Induced by Mitochondria Dysfunction

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Naoki Fujitani ◽  
Akihiro Yoneda ◽  
Motoko Takahashi ◽  
Akira Takasawa ◽  
Tomoyuki Aoyama ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Cancer Cells ◽  
Cancer Cell ◽  
Transcriptional Level ◽  
Glutathione S Transferase ◽  
Mitochondria Dysfunction ◽  
Cancer Cell Growth ◽  
Retracted Article ◽  
Significant Impairment ◽  
Glutathione S Transferases

AbstractAntitumor drug development based on the concept of intervening in the antioxidant system of cancer cells has been gaining increased interest. In this study, we propose a promising strategy for cancer treatment using modulation of oxidative stress by suppression of glutathione S-transferases (GSTs), a typical antioxidant enzyme. siRNA which can be applied to the development of nucleic acid drugs, enabling them to eliminate unwanted side effects, increase specificity, and avoid the problem of drug resistance, was employed for GSTP-silencing at the transcriptional level. The silencing of the pi class of GST (GSTP) that displayed the most characteristic expression profile in 13 kinds of cancer cell lines has shown significant impairment in the growth of cancer cells due to oxidative stress caused by excess ROS accumulation. Comparative proteomics between normal cells and GSTP-silenced pancreatic cancer cell PANC-1 suggested that GSTP-silencing facilitated the mitochondrial dysfunction. These findings show promise for the development of strategies toward cancer therapy based on the mechanism that allows genetic silencing of GSTP to promote oxidative stress through mitochondria dysfunction.

scholarly journals Oxidant/Antioxidant Status of Breast Cancer Patients in Pre- and Post-Operative Periods

Medicina ◽  
2020 ◽  
Vol 56 (2) ◽  
pp. 70 ◽  
Author(s):  
Janina Didžiapetrienė ◽  
Birutė Kazbarienė ◽  
Renatas Tikuišis ◽  
Audrius Dulskas ◽  
Daiva Dabkevičienė ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Oxidative Stress ◽  
Cancer Patients ◽  
Thiobarbituric Acid ◽  
Breast Cancer Surgery ◽  
Oxidative Stress Marker ◽  
Breast Cancer Patients ◽  
Glutathione S Transferase ◽  
Before And After ◽  
Gst Activity

Background and Objectives: The purpose of this study is to evaluate the level of oxidative stress before and after breast cancer surgery. Materials and Methods: Malondialdehyde (MDA) level was tested using a thiobarbituric acid (TBA) assay based on the release of a color complex due to TBA reaction with MDA. The glutathione S-transferase (GST) activity was evaluated by enzymatic conjugation of reduced glutathione (GSH) with 1-chloro-2,4-dinitrobenzene. The level of total glutathione (reduced GSH and oxidized GSSG) was detected using a recycling system by 5,5-dithiobis(2-nitrobenzoic acid). The levels of the indices were determined in the serum of 52 patients before surgery, two hours and five days after surgery, and in 42 healthy women. Results: In the patients over 50 years old the level of MDA was higher after surgery in comparison with before surgery, and GST activity was lower in comparison with the control. The GSH + GSSG level in both ages groups after surgery was lower than in the control. Significant differences of MDA level were detected in patients with stage III after surgery compared to the control. The level of GSH + GSSG was significantly lower in the patients with I–III stages compared to the control. Conclusion: The most expressed changes demonstrate the significance of MDA as a marker to evaluate oxidative stress in breast cancer patients. The degree of oxidative stress depends on the patient’s age and stage of disease. (1) Malondialdehyde can be used as an oxidative stress marker; (2) A higher stage of the disease and older age correspond to a higher rise of malondialdehyde, suggesting more intensive oxidative stress.

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