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 The pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants

2020 ◽  
Vol 71 (12) ◽  
pp. 3405-3416 ◽  
Author(s):  
Haiyan Ding ◽  
Bipeng Wang ◽  
Yi Han ◽  
Shengchun Li
Keyword(s):  
Reduced Form ◽  
Glutathione S Transferase ◽  
Sulfenic Acid ◽  
Abiotic And Biotic Stresses ◽  
Biotic Stresses ◽  
Ping Pong ◽  
Rapid Changes ◽  
Catalytic Cysteine ◽  
Oxidation Analysis

Abstract Under natural conditions, plants are exposed to various abiotic and biotic stresses that trigger rapid changes in the production and removal of reactive oxygen species (ROS) such as hydrogen peroxide (H2O2). The ascorbate-glutathione pathway has been recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR), an enzyme belonging to the glutathione S-transferase (GST) superfamily. Thus, DHAR has been considered to be important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The reaction of DHAR has been proposed to proceed by a ping-pong mechanism, in which binding of DHA to the free reduced form of the enzyme is followed by binding of GSH. Information from crystal structures has shed light on the formation of sulfenic acid at the catalytic cysteine of DHAR that occurs with the reduction of DHA. In this review, we discuss the molecular properties of DHAR and its importance in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development.

scholarly journals Glutathione S-transferases of mouse lung. Selective binding of benzo[a]pyrene metabolites by the subunits which are preferentially induced by t-butylated hydroxyanisole

1987 ◽  
Vol 243 (2) ◽  
pp. 351-358 ◽  
Author(s):  
S V Singh ◽  
G Creadon ◽  
M Das ◽  
H Mukhtar ◽  
Y C Awasthi
Keyword(s):  
Physiological Role ◽  
Mouse Lung ◽  
Butylated Hydroxyanisole ◽  
Natl Cancer Inst ◽  
Glutathione S Transferase ◽  
Catalytic Activities ◽  
Dietary Antioxidant ◽  
Wide Range ◽  
Glutathione S Transferases ◽  
Pyrene Metabolites

Six isoenzymes of glutathione S-transferase (GST) present in mouse lung have been purified and characterized. GST I (pI 9.8) is a dimer of Mr-26,500 subunits and GST II is a heterodimer of Mr-26,500 and -22,000 subunits, and GST III (pI 7.9) and IV (pI 6.4) are dimers of Mr-24,500 subunits. GST V (pI 5.7) is a heterodimer of Mr-24,500 and -23,000 subunits, whereas GST VI (pI 4.9) is a dimer of Mr-23,000 subunits. Immunological studies indicate that the Mr-24,500 subunits present in GST III (pI 7.9) are distinct from those present in GST IV (pI 6.4) and V (pI 5.7). Structural and immunological studies provide evidence that at least five distinct types of subunits in their different binary combinations give rise to various GST isoenzymes of mouse lung. These isoenzymes express varying degrees of catalytic activities towards a wide range of electrophilic substrates including benzo[a]pyrene 7,8-oxide and benzo[a]pyrene 4,5-oxide. The dietary antioxidant t-butylated hydroxyanisole (BHA) preferentially induces GST II and III. Also, these two isoenzymes selectively bind benzo[a]pyrene (B[a]P) metabolites, indicating that they play an important physiological role in the detoxification of B[a]P metabolites. The preferential induction of the GST isoenzymes involved in the detoxification of activated B[a]P metabolites indicates that the anti-neoplastic activity of BHA against B[a]P-induced neoplasia in mouse lung [Wattenberg (1973) J. Natl. Cancer Inst. 50, 1541-1544] may be due to the enhanced detoxification of B[a]P metabolites.

scholarly journals Z-Ligustilide Exerted Hormetic Effect on Growth and Detoxification Enzymes of Spodoptera litura Larvae

2018 ◽  
Vol 2018 ◽  
pp. 1-10 ◽  
Author(s):  
Yang Yi ◽  
Guojun Dou ◽  
Zanyang Yu ◽  
Hui He ◽  
Chengqiang Wang ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Larvicidal Activity ◽  
Spodoptera Litura ◽  
Low Dose ◽  
Critical Role ◽  
Detoxification Enzymes ◽  
Glutathione S Transferase ◽  
Hormetic Effect ◽  
Senkyunolide I

Plants have evolved a variety of phytochemicals to defense insect feeding, whereas insects have also evolved diverse detoxification enzymes, which are adaptively induced as a prosurvival mechanism. Herein, Z-ligustilide in Ligusticum chuanxiong Hort. was found to exhibit a similar trend in the accumulation from December to May as the occurrence of Spodoptera litura (Fabricius) larvae. Importantly, S. litura larvae feeding enhanced Z-ligustilide level in the stem and leaf (p < 0.01). Moreover, Z-ligustilide ranging from 1 to 5 mg·g−1 exhibited remarkable larvicidal activity, antifeedant activity, and growth inhibition against S. litura larvae. The LC50 values of larvicidal activity for phthalides in L. chuanxiong were compared as follows: Z-ligustilide > levistilide A > senkyunolide A > 3-butylidenephthalide > senkyunolide I, implicating the critical role of conjugated structure. Notably, there was a biphasic dose response for glutathione S-transferase (GST), cytochrome P450 (CYP) 450, Acetylcholinesterase (AChE), and Carboxylesterase (CarE) activities and GSTs1, cytochrome P450 (CYP) 4S9, and CYP4M14 mRNA expression. Particularly, low dose (0.1 mg·g−1) of Z-ligustilide conferred the resistance of S. litura larvae against chlorpyrifos (p < 0.05). Together, our data suggest that Z-ligustilide may function in a hormetic way in the chemical defense of L. chuanxiong against S. litura larvae.

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 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.

Relationship between glutathione S-transferase M1, T1, and P1 polymorphisms and chronic lymphocytic leukemia

Blood ◽  
2002 ◽  
Vol 99 (11) ◽  
pp. 4216-4218 ◽  
Author(s):  
Martin Yuille ◽  
Alison Condie ◽  
Chantelle Hudson ◽  
Zsofia Kote-Jarai ◽  
Elaine Stone ◽  
...  
Keyword(s):  
High Risk ◽  
Chronic Lymphocytic Leukemia ◽  
Hematologic Malignancies ◽  
Lymphocytic Leukemia ◽  
Polymorphic Variation ◽  
Glutathione S Transferase ◽  
Risk Alleles ◽  
Glutathione S Transferases ◽  
Increasing Risk ◽  
Gst Family

Interindividual differences in susceptibility to hematologic malignancies may be mediated in part through polymorphic variability in the bioactivation and detoxification of carcinogens. The glutathione S–transferases (GSTs) have been implicated as susceptibility genes in this context for a number of cancers. The aim of this study was to examine whether polymorphic variation in GSTs confers susceptibility to chronic lymphocytic leukemia (CLL). GSTM1, GSTT1, andGSTP1 genotypes were determined in 138 patients and 280 healthy individuals. The frequency of both GSTM1 andGSTT1 null genotypes and the GSTP1-Ile allele was higher in cases than in controls. There was evidence of a trend in increasing risk with the number of putative “high-risk” alleles of the GST family carried (P = .04). The risk of CLL associated with possession of all 3 “high-risk” genotypes was increased 2.8-fold (OR = 2.8, 95% confidence interval: 1.1-6.9). Our findings suggest that heritable GST status may influence the risk of developing CLL.

scholarly journals Resistance in the Genus Spodoptera: Key Insect Detoxification Genes

Insects ◽  
2021 ◽  
Vol 12 (6) ◽  
pp. 544
Author(s):  
Frédérique Hilliou ◽  
Thomas Chertemps ◽  
Martine Maïbèche ◽  
Gaëlle Le Goff
Keyword(s):  
Abc Transporters ◽  
Molecular Mechanisms ◽  
Spodoptera Exigua ◽  
Cytochromes P450 ◽  
Point Mutations ◽  
Detoxification Enzymes ◽  
Over Expression ◽  
Glutathione S Transferases ◽  
Lepidoptera Noctuidae

The genus Spodoptera (Lepidoptera: Noctuidae) includes species that are among the most important crop pests in the world. These polyphagous species are able to feed on many plants, including corn, rice and cotton. In addition to their ability to adapt to toxic compounds produced by plants, they have developed resistance to the chemical insecticides used for their control. One of the main mechanisms developed by insects to become resistant involves detoxification enzymes. In this review, we illustrate some examples of the role of major families of detoxification enzymes such as cytochromes P450, carboxyl/cholinesterases, glutathione S-transferases (GST) and transporters such as ATP-binding cassette (ABC) transporters in insecticide resistance. We compare available data for four species, Spodoptera exigua, S. frugiperda, S. littoralis and S. litura. Molecular mechanisms underlying the involvement of these genes in resistance will be described, including the duplication of the CYP9A cluster, over-expression of GST epsilon or point mutations in acetylcholinesterase and ABCC2. This review is not intended to be exhaustive but to highlight the key roles of certain genes.

scholarly journals A glutathione s-transferase confers herbicide tolerance in rice

2014 ◽  
Vol 14 (2) ◽  
pp. 76-81 ◽  
Author(s):  
Tingzhang Hu
Keyword(s):  
Transgenic Rice ◽  
Oryza Sativa L ◽  
Herbicide Tolerance ◽  
Glutathione S Transferase ◽  
Over Expression ◽  
Rice Plants ◽  
Vegetative Tissues ◽  
Transgenic Rice Plants ◽  
Glutathione S Transferases

Plant glutathione S-transferases (GSTs) have been a focus of attention due to their role in herbicide detoxification. OsGSTL2 is a glutathione S-transferase, lambda class gene from rice (Oryza sativa L.). Transgenic rice plants over-expressing OsGSTL2 were generated from rice calli by the use of an Agrobacterium transformation system, and were screened by a combination of hygromycin resistance, PCR and Southern blot analysis. In the vegetative tissues of transgenic rice plants, the over-expression of OsGSTL2 not only increased levels of OsGSTL2 transcripts, but also GST and GPX expression, while reduced superoxide. Transgenic rice plants also showed higher tolerance to glyphosate and chlorsulfuron, which often contaminate agricultural fields. The findings demonstrate the detoxification role of OsGSTL2 in the growth and development of rice plants. It should be possible to apply the present results to crops for developing herbicide tolerance and for limiting herbicide contamination in the food chain.

scholarly journals Nitroglycerin metabolism in vascular tissue: role of glutathione S-transferases and relationship between NO. and NO2– formation

1993 ◽  
Vol 292 (2) ◽  
pp. 545-550 ◽  
Author(s):  
M A Kurz ◽  
T D Boyer ◽  
R Whalen ◽  
T E Peterson ◽  
D G Harrison
Keyword(s):  
Vascular Tissue ◽  
Potent Inhibitor ◽  
Metabolic Process ◽  
No Production ◽  
Transferase Activity ◽  
Glutathione S Transferase ◽  
No Release ◽  
Glutathione S Transferases ◽  
No2 Formation

Nitroglycerin is a commonly employed pharmacological agent which produces vasodilatation by release of nitric oxide (NO.). The mechanism by which nitroglycerin releases NO. remains undefined. Recently, glutathione S-transferases have been implicated as important contributors to this process. They are known to release NO2- from nitroglycerin, but have not been shown to release NO.. The present studies were designed to examine the role of endogenous glutathione S-transferases in this metabolic process. Homogenates of dog carotid artery were incubated anaerobically with nitroglycerin, and NO. and NO2- production was determined by chemiluminescence. The role of glutathione S-transferases was studied by incubating homogenates with nitroglycerin in the presence of 1 mM GSH or 1 mM S-hexyl-glutathione, a potent inhibitor of glutathione S-transferases. Homogenates released 163 pmol of NO./h per mg of protein from nitroglycerin, and 2370 pmol of NO2-/h per mg. Adding GSH decreased NO. production by 82% and increased NO2- production by 98%. S-Hexylglutathione inhibited glutathione S-transferase activity by 96% and decreased NO2- production by 78%, but had no effect on NO. release. A linear relationship between glutathione S-transferase activity and NO2- production was observed, whereas glutathione S-transferase activity and NO. release were unrelated. Western-blot analysis demonstrated that dog carotid vascular smooth muscle contained Pi and Mu forms of glutathione S-transferases, with a predominance of the former. Purified preparations of human Pi and rat Mu isoforms metabolized nitroglycerin only to NO2- and not to NO.. On the basis of these findings, we conclude that (1) glutathione S-transferases do not contribute to the bioconversion of nitroglycerin to NO., but instead act as a degradative pathway for nitroglycerin, and (2) the release of NO. from nitroglycerin is not dependent on the formation of NO2-.

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.

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