The role of Glutathione-S-transferases in phoxim and chlorfenapyr tolerance in a major mulberry pest, Glyphodes pyloalis walker (Lepidoptera: Pyralidae)

2021 ◽  
pp. 105004
Author(s):  
Zhi-Xiang Liu ◽  
Xiao-Rong Xing ◽  
Xin-Hao Liang ◽  
Jian-hao Ding ◽  
Yi-Jiangcheng Li ◽  
...  
Keyword(s):  
Glyphodes Pyloalis ◽  
Glutathione S Transferases ◽  
Lepidoptera Pyralidae

scholarly journals Antioxidant role of glutathione S-transferases: 4-Hydroxynonenal, a key molecule in stress-mediated signaling

2015 ◽  
Vol 289 (3) ◽  
pp. 361-370 ◽  
Author(s):  
Sharad S. Singhal ◽  
Sharda P. Singh ◽  
Preeti Singhal ◽  
David Horne ◽  
Jyotsana Singhal ◽  
...  
Keyword(s):  
Glutathione S Transferases

The Role of Human Glutathione S-Transferases hGSTA1-1 and hGSTA2-2 in Protection against Oxidative Stress

1999 ◽  
Vol 367 (2) ◽  
pp. 216-224 ◽  
Author(s):  
Tiejun Zhao ◽  
Sharad S. Singhal ◽  
John T. Piper ◽  
Jizhong Cheng ◽  
Utpal Pandya ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Glutathione S Transferases

scholarly journals Glutathione S - transferases class Pi and Mi and their significance in oncology

2017 ◽  
Vol 71 (1) ◽  
pp. 0-0 ◽  
Author(s):  
Zofia Marchewka ◽  
Agnieszka Piwowar ◽  
Sylwia Ruzik ◽  
Anna Długosz
Keyword(s):  
Redox Homeostasis ◽  
Current Data ◽  
Altered Expression ◽  
Potential Marker ◽  
Inflammatory Processes ◽  
Glutathione S Transferases ◽  
Endogenous Substrates ◽  
Cancer Tissues ◽  
Serum And Urine

In this article the current data, which shows that glutathione S-transferases (GST) class Pi and Mi are interesting and promising biomarkers in acute and chronic inflammatory processes as well as in the oncology, were presented based on the review of the latest experimental and clinical studies. The article shows their characteristics, functions and participation (direct - GST Pi, indirect - GST Mi) in the regulation of signaling pathways of JNK kinases, which are involved in cell differentiation. Overexpression of glutathione S-transferases class Pi and Mi in many cancer cells plays a key role in cancer treatment, making them resistant to chemotherapy. GST isoenzymes are involved in the metabolism of various types of xenobiotics and endogenous substrates, so their altered expression in cancer tissues as well as in serum and urine could be an important potential marker of the cancer and an indicator of oxidative stress. The study shows the role of glutathione S-transferases in redox homeostasis of tumor cells and in the mechanism of resistance to anticancer drugs.

scholarly journals Association of Genetic Polymorphisms in GSTP1, GSTM1, and GSTT1 Genes with Vesicoureteral Reflux Susceptibility in the Children of Southeast Iran

2020 ◽  
Author(s):  
Sima SHAHROKHZADEH ◽  
Azam SOLEIMANI ◽  
Dor-Mohammad KORDI-TAMANDANI ◽  
Mohammad Hossein SANGTARASH ◽  
Omid NEJATI ◽  
...  
Keyword(s):  
Vesicoureteral Reflux ◽  
Genetic Risk ◽  
Protective Role ◽  
Common Type ◽  
Chain Reaction ◽  
Eastern Iran ◽  
Multifunctional Enzymes ◽  
Glutathione S Transferases ◽  
Polymerase Chain

Background: Vesicoureteral reflux (VUR) disease is the most common type of urinary tract anomalies in children. Genetic risk factors may be associated with the etiology of VUR. The role of the Glutathione S-transferases (GSTs) as multifunctional enzymes is cellular oxidative stress handling. This is the first study aimed at evaluating the relative risk of GSTP1, GSTM1, and GSTT1 polymorphisms in VUR susceptibility in children and provides new important insights into the genetics of affected children. Methods: The study was done in 2013 in Sistan and Baluchestan University, eastern Iran. Genotyping of three GSTP1, GSTM1, and GSTT1 genes were determined using the multiplex polymerase chain reaction assay in 216 reactions for 72 VUR children and 312 reactions for 104 healthy controls. Results: The presence of GSTT1 deletion was associated with high risk of VUR in children, whereas GSTP1 and GSTM1 genotypes did not show the same effect. Furthermore, the combination of GSTT1/GSTM1 and GSTT1/ GSTP1 genotypes showed a significant influence on lower risk of VUR in children. Conclusion: Deletion of GSTT1 functional gene is a genetic risk factor causing VUR in children. Interestingly, the combination of GSTM1 and GSTP1 null genotypes with GSTT1 has shown a protective role against risk of GSTT1 deletion.

scholarly journals The Role of Glutathione S-Transferases in Urinary Tract Tumors

2008 ◽  
Vol 27 (3) ◽  
pp. 360-366 ◽  
Author(s):  
Tatjana Simić ◽  
Ana Savić-Radojević ◽  
Marija Plješa-Ercegovac ◽  
Marija Matić ◽  
Tatjana Sašić ◽  
...  
Keyword(s):  
Urinary Tract ◽  
Urinary Bladder ◽  
Cell Carcinoma ◽  
Allelic Variation ◽  
Transitional Cell ◽  
Chemotherapy Resistance ◽  
High Recurrence Rate ◽  
Specific Chemical ◽  
Glutathione S Transferases

The Role of Glutathione S-Transferases in Urinary Tract Tumors Exposure to potential carcinogens is among the etiological factors for renal cell carcinoma (RCC) and transitional cell carcinoma (TCC) of the urinary bladder. RCC is very resistant, while TCC exhibits a high recurrence rate and multifocality. Cytosolic glutathione S-transferases (GST) are a superfamily of enzymes which protect normal cells by catalyzing conjugation reactions between electrophylic compounds, including carcinogens, and glutathione. Some GST enzymes posses hydroperoxidase activity. The most well characterized classes have been named Alpha (GSTA), Mu (GSTM), Pi (GSTP) and Theta (GSTT) and each of these classes contains several different isoenzymes. Several types of allelic variation have been identified within classes, among which GSTM1-null and GSTT1-null confer impaired catalytic activity. Individuals with the GSTM1-null genotype carry a substantially higher risk for bladder carcinogenesis. The effects of glutathione S-transferase T1 polymorphism on the increased susceptibility to RCC and TCC of urinary bladder depend on the presence of specific chemical exposures to compounds metabolized via the GSTT1-1 pathway. In the process of kidney cancerisation expression of GST alpha isoenzymes tends to decrease, consequently favoring a prooxidant environment necessary for the growth of RCC. GST pi enzyme activities are generally retained in RCC and might contribute to the chemotherapy resistance of RCC. In the malignant phenotype of TCC of the urinary bladder up regulation of various GST classes occurs. Up regulation of GSTT1-1 and GSTP1-1 might have important consequences on the tumor growth, by providing a reduced environment and inhibition of apoptotic pathways.

scholarly journals The role of an evolutionarily conserved cis-proline in the thioredoxin-like domain of human class Alpha glutathione transferase A1-1

2003 ◽  
Vol 372 (1) ◽  
pp. 241-246 ◽  
Author(s):  
Chris NATHANIEL ◽  
Louise A. WALLACE ◽  
Jonathan BURKE ◽  
Heini W. DIRR
Keyword(s):  
Glutathione Transferase ◽  
Conformational Stability ◽  
Wild Type ◽  
Catalytic Function ◽  
Evolutionarily Conserved ◽  
Glutathione S Transferases ◽  
Equilibrium Unfolding ◽  
The Stability ◽  
Unfolding Kinetics

The thioredoxin-like fold has a βαβαββα topology, and most proteins/domains with this fold have a topologically conserved cis-proline residue at the N-terminus of β-strand 3. This residue plays an important role in the catalytic function and stability of thioredoxin-like proteins, but is reported not to contribute towards the stability of glutathione S-transferases (GSTs) [Allocati, Casalone, Masulli, Caccarelli, Carletti, Parker and Di Ilio (1999) FEBS Lett. 445, 347–350]. In order to further address the role of the cis-proline in the structure, function and stability of GSTs, cis-Pro-56 in human GST (hGST) A1-1 was replaced with a glycine, and the properties of the P56G mutant were compared with those of the wild-type protein. Not only was the catalytic function of the mutant dramatically reduced, so was its conformational stability, as indicated by equilibrium unfolding and unfolding kinetics experiments with urea as denaturant. These findings are discussed in the context of other thioredoxin-like proteins.

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