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.

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

2001 ◽  
Vol 360 (3) ◽  
pp. 675 ◽  
Author(s):  
Antonio TAMBURRO ◽  
Nerino ALLOCATI ◽  
Michele MASULLI ◽  
Domenico ROTILIO ◽  
Carmine DI ILIO ◽  
...  
Keyword(s):  
Stress Conditions ◽  
Chemical Stress ◽  
Glutathione S Transferase

scholarly journals Modulation of the glutathione S-transferase in Ochrobactrum anthropi: function of xenobiotic substrates and other forms of stress

2000 ◽  
Vol 346 (2) ◽  
pp. 553-559 ◽  
Author(s):  
Bartolo FAVALORO ◽  
Antonio TAMBURRO ◽  
Massimo A. TROFINO ◽  
Luciano BOLOGNA ◽  
Domenico ROTILIO ◽  
...  
Keyword(s):  
Mrna Level ◽  
Membrane Damage ◽  
Amino Acid Residues ◽  
Ochrobactrum Anthropi ◽  
Adaptive Responses ◽  
Glutathione S Transferase ◽  
Aromatic Substrates ◽  
Hydrophobic Compounds ◽  
Degrading Bacterium ◽  
Single Subunit

The gluthathione S-transferase gene of the atrazine-degrading bacterium Ochrobactrum anthropi (OaGST) encodes a single-subunit polypeptide of 201 amino acid residues (Favaloro et al. 1998, Biochem. J. 335, 573-579). RNA blot analysis showed that the gene is transcribed into an mRNA of about 800 nucleotides, indicating a monocistronic transcription of the OaGST gene. The modulation of OaGST in this bacterium, in the presence of different stimulants, was investigated. The level of expression of OaGST was detected both by measuring the mRNA level and by immunoblotting experiments. OaGST is a constitutive enzyme which is also inducible by several stimulants. In fact, atrazine caused an increase in the expression of OaGST even at concentrations which had no effect on growth rates of the bacteria. Moreover, the presence of other aromatic substrates of this bacterium, such as phenol and chlorophenols, leads to a marked enhancement in OaGST expression. In this case, the expression of OaGST was related to growth inhibition and membrane damage caused by these hydrophobic compounds, and to the adaptive responses of the cell membranes. On the other hand, toluene and xylene, two aromatic compounds not degradable by this bacterium, did not induce the OaGST expression. The same was observed for other stress conditions such as low pH, heat shock, hydrogen peroxide, osmotic stress, starvation, the presence of aliphatic alcohols or heavy metals. These results suggest a co-regulation of the OaGST gene by the catabolic pathways of phenols and chlorophenols in this bacterium. Therefore, OaGST could function as a detoxifying agent within the catabolism of these xenobiotics.

scholarly journals Cytoprotective Mechanisms Mediated by Polyphenols from Chilean Native Berries against Free Radical-Induced Damage on AGS Cells

2017 ◽  
Vol 2017 ◽  
pp. 1-13 ◽  
Author(s):  
Felipe Ávila ◽  
Cristina Theoduloz ◽  
Camilo López-Alarcón ◽  
Eva Dorta ◽  
Guillermo Schmeda-Hirschmann
Keyword(s):  
Free Radical ◽  
Radical Scavenging ◽  
Free Radical Scavenging ◽  
Radical Scavenger ◽  
Glyoxalase I ◽  
Protective Effects ◽  
Glutathione S Transferase ◽  
Ags Cells ◽  
Cellular Protection ◽  
Glutathione S Transferases

The prevalence of cytoprotective mechanisms induced by polyphenols such as activation of intracellular antioxidant responses (ICM) and direct free radical scavenging was investigated in native Chilean species of strawberries, raspberries, and currants. Human gastric epithelial cells were co- and preincubated with polyphenolic-enriched extracts (PEEs) from Chilean raspberries (Rubus geoides), strawberries (Fragaria chiloensis ssp. chiloensis f. chiloensis), and currants (Ribes magellanicum) and challenged with peroxyl and hydroxyl radicals. Cellular protection was determined in terms of cell viability, glyoxalase I and glutathione s-transferases activities, and carboxymethyl lysine (CML) and malondialdehyde levels. Our results indicate that cytoprotection induced by ICM was the prevalent mechanism for Rubus geoides and F. chiloensis. This agreed with increased levels of glyoxalase I and glutathione S-transferase activities in cells preincubated with PEEs. ORAC index indicated that F. chiloensis was the most efficient peroxyl radical scavenger. Moreover, ICM mediated by F. chiloensis was effective in protecting cells from CML accumulation in contrast to the protective effects induced by free radical scavenging. Our results indicate that although both polyphenol-mediated mechanisms can exert protective effects, ICM was the most prevalent in AGS cells. These results suggest a potential use of these native berries as functional food.

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.

scholarly journals Glutathione S-Transferases in Marine Copepods

2021 ◽  
Vol 9 (9) ◽  
pp. 1025
Author(s):  
Chiara Lauritano ◽  
Ylenia Carotenuto ◽  
Vittoria Roncalli
Keyword(s):  
Cellular Localization ◽  
Detoxification Enzymes ◽  
Reduced Form ◽  
Glutathione S Transferase ◽  
Status Monitoring ◽  
Wide Range ◽  
Glutathione S Transferases ◽  
Gst Family ◽  
Marine Copepods

The glutathione S-transferase (GST) is a complex family of phase II detoxification enzymes, known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to a wide variety of endogenous and exogenous electrophilic compounds for detoxification purposes. In marine environments, copepods are constantly exposed to multiple exogenous stressors, thus their capability of detoxification is key for survival. Full identification of the GST family in copepods has been limited only to few species. As for insects, the GST family includes a wide range of genes that, based on their cellular localization, can be divided in three classes: cytosolic, microsomal, and mitochondrial. The role of GSTs might have class-specific features, thus understanding the nature of the GST family has become crucial. This paper covers information of the GST activity in marine copepods based on studies investigating gene expression, protein content, and enzymatic activity. Using published literature and mining new publicly available transcriptomes, we characterized the multiplicity of the GST family in copepods from different orders and families, highlighting the possible role of these genes as biomarker for ocean health status monitoring.

scholarly journals A Review of GENETIC Polymorphism of GSTs (Glutathione –s Transferase) Genes in Breast Cancer

2019 ◽  
pp. 1-12
Author(s):  
Mohammad Shokrzadeh ◽  
Nematollah Ahangar ◽  
Abbas Mohammadpour ◽  
Golpar Golmohammadzadeh
Keyword(s):  
Breast Cancer ◽  
Reactive Oxygen Species ◽  
Water Solubility ◽  
Review Article ◽  
Detoxification Enzymes ◽  
Oxygen Species ◽  
Cancer Death ◽  
Glutathione S Transferase ◽  
The World ◽  
Glutathione S Transferases

In this review article, several researchesabout genetic polymorphisms of Glutation –s transferase (GST) enzymes that may have an etiological role in breast cancer have been reviewed. Breast carcinoma is the most frequent malignancy in women and represents the second leading cause of cancer death among women and accounts for about one-fourth of female cancer cases all over the world. GSTs are a family of Phase II detoxification enzymes that catalyze the conjugation of glutathione (GSH) to a wide variety of xenobiotic The incorporation of glutathione increases the molecule’s water solubility. This detoxification ability to become Glutathione S-transferases play an important role in drug, carcinogen, and reactive oxygen species detoxication and act both as peroxidases and as catalysts of glutathione transfer to hydrophobic electrophiles.It is evaluated in Iran and other countries that the annual incidence of cancer in the world will increase to 25 million in 2030, of which more than 70 percent occurs in developing countries.It is the second cause of death among Iranian women and one million new cases diagnosed worldwide every year.

Analysis of glutathione S-transferase genes polymorphisms and the risk of schizophrenia in a sample of Iranian population

2011 ◽  
Vol 7 (2-4) ◽  
pp. 199-203 ◽  
Author(s):  
Farah Lotfi Kashani ◽  
Dor Mohammad Kordi-Tamandani ◽  
Roya Sahranavard ◽  
Mohammad Hashemi ◽  
Farzaneh Kordi-Tamandani ◽  
...  
Keyword(s):  
Genomic Dna ◽  
Case Control Study ◽  
Gene Interaction ◽  
Case Control ◽  
Glutathione S Transferase ◽  
Chain Reaction ◽  
Healthy Control ◽  
Glutathione S Transferases ◽  
Polymerase Chain ◽  
Control Study

Glutathione S-transferases (GSTs) are major intracellular antioxidants, which, impaired in their function, are involved in the progress of schizophrenia (SCZ). The aim of this case-control study was to investigate the association between the polymorphism of glutathione S-transferases M1 (GSTM1), T1 (GSTT1), the glutathione S-transferase P1 gene (GSTP1) and SCZ. We isolated genomic DNA from peripheral blood of 93 individuals with SCZ and 99 healthy control subjects' genotypes analyzing them for GSTM1, GSTT1 and GSTP1 using polymerase chain reaction. The analysis of the gene–gene interaction between GSTs indicated that the magnitude of the association was greater for the combined AG/GSTT1 & GSTM1 genotypes (OR = 2.51; 95% CI: 1.13–5.63, P = 0.02). The AG and combined AG + GG genotypes of GSTP1 increased the risk of SCZ (OR = 1.83; 95% CI: 0.94–3.75 and OR = 1.71; 95% CI: 0.92–3.19, respectively). The genotypes of GSTT/NULL, NULL/GSTM and NULL/NULL increased the risk of SCZ (OR = 2.05; 95% CI: 0.9–4.74; OR = 2.0; 95% CI: 1.68–2.31; and OR = 1.8; 95% CI: 0.57–2.46, respectively). The present study supports previous data that suggest that impairment in the function of GSTs genes may increase the risk of SCZ.

Current Status of Pyrethroids Resistance in Aedes aegypti (Culicidae: Diptera) in Lahore District, Pakistan: A Novel Mechanistic Insight

2021 ◽  
Author(s):  
Saira Nawaz ◽  
Hafiz Muhammad Tahir ◽  
Muhammad Asif Mahmood ◽  
Muhammad Summer ◽  
Shaukat Ali ◽  
...  
Keyword(s):  
Aedes Aegypti ◽  
Enzyme Level ◽  
Laboratory Strain ◽  
Current Status ◽  
Glutathione S Transferase ◽  
Development Of Resistance ◽  
Biochemical Assays ◽  
Dengue Transmission ◽  
Lambda Cyhalothrin ◽  
Glutathione S Transferases

Abstract Aedes aegypti (Linnaeus, 1762) is a major vector responsible for dengue transmission. Insecticides are being used as the most effective tool to control vector populations in Lahore, Pakistan. Control of Ae. aegypti is threatened by the development of resistance against insecticides. The current status of insecticide resistance was evaluated against pyrethroids (deltamethrin, cypermethrin, and lambda-cyhalothrin) in different populations of Lahore (Model Town, Mishri Shah, Sadar Cantt, Walton, and Valencia). The susceptibility of the larval and adult populations was tested following the standard WHO guidelines. Moderate to high levels of resistance were found against pyrethroids in the larval (RR50: 3.6–27.2 and RR90: 5–90) and adult populations (percentage mortality < 98%). Biochemical assays revealed a statistically significant increase in the enzyme level in all field populations compared to the laboratory strain. The value of esterase was one-fold higher, monooxygenase was 3.9- to 4.7-fold higher, and glutathione S-transferases was 1.9- to 2.6-fold higher in field populations compared to the laboratory strain. These results depict the presence of resistance against deltamethrin, cypermethrin, and lambda-cyhalothrin in field populations of Lahore mediated by metabolic enzymes i.e. esterases, monooxygenases, and glutathione S-transferase.

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