Journal articles: 'Glutathion transferase'

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Silivanova, E. A., P. A. Shumilova, and M. A. Levchenko. "Activities of detoxifying enzymes in adults of houseflies Musca domestica L. selected with chlorfenapyr." Biomics 12, no. 4 (2020): 492–503. http://dx.doi.org/10.31301/2221-6197.bmcs.2020-43.

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In insects, biochemical mechanisms of insecticide resistance base on increasing of activities of main detoxyfying enzymes – monooxygenases, nonspesific esterases, and glutathion-S-transferases. Currently, the progress of resistance development and the degree of contributing enzymes to resistance in insects have been studied for certain insecticides. The goal of this study was to assess activities of monooxygenase, carboxylesterase, glutathione-S-transferase, and alkaline phosphatase in females and males housefly Musca domestica in the second, fourth, sixth, eighth and tenth generations of the chlorfenapyr-selected strain. Evaluation of chlorfenapyr susceptibility showed that adults M. domestica in tenth generations was tolerating to chlorfenapyr as the resistance ration value was 3.6. In certain generations of chlorfenapyr-selected strain M. domestica, monooxygenase activities in males and females were 1.4-2.1 times more, and alkaline phosphatase activities in females were 2.3-2.7 times more than that in control insects. Glutathione-S-transferase activities had no significant differences in adults M. domestica of control and chlorfenapyr-selected strains. For chlorfenapyr-selected strain M. domestica, activities of monooxygenase, carboxylesterase, and alkaline phosphatase differed in males and females of same generations that suggests that mode and pattern of resistance development might be sex-specific in this specie.

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Ito, Mika, Satoshi Shuto, Yoshihiro Ito, and Hiroshi Abe. "Development of Molecular Probe Targeting on Glutathion Transferase." Journal of Synthetic Organic Chemistry, Japan 72, no. 7 (2014): 822–31. http://dx.doi.org/10.5059/yukigoseikyokaishi.72.822.

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Tison, F., C. Coutelle, P. Henry, and A. Cassaigne. "Glutathion s-transferase (class ?) phenotype in Parkinson's disease." Movement Disorders 9, no. 1 (1994): 117–18. http://dx.doi.org/10.1002/mds.870090128.

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Borkar, Dipali B., and Vishal L. Bagde. "Role of Glutathion-S-Transferase in Imparting Resistance in Plutella Xylostella (L.) Against Flubendiamide." Indian Journal of Applied Research 3, no. 9 (October 1, 2011): 7–8. http://dx.doi.org/10.15373/2249555x/sept2013/3.

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Su, Fengxi, Xiaoqu Hu, Weijuan Jia, Chang Gong, Erwei Song, and Peter Hamar. "Glutathion s transferase π indicates chemotherapy resistance in breast cancer." Journal of Surgical Research 113, no. 1 (July 2003): 102–8. http://dx.doi.org/10.1016/s0022-4804(03)00200-2.

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Kopylchuk, Halyna, and Ivanna Nykolaichuk. "Basic components of glutathion system in rat erythrocytes under conditions of toxic damage on the background of an alimental protein lack." Biolohichni systemy 12, no. 1 (June 25, 2020): 31–38. http://dx.doi.org/10.31861/biosystems2020.01.031.

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The article is devoted to the study of the main components of the glutathione system under conditions of toxic damage against the background of nutritional protein deficiency: the content of reduced and oxidized glutathione with the determination of the GSH/GSSG ratio, the activity of glutathione-dependent enzymes – glutathione peroxidase, glutathione transferase, glutathione reductase, and glucose-6-phosphate dehydrogenase. The concentration of reduced glutathione in the erythrocyte hemolysate was studied using Elman's reagent after deproteinization of the samples. Glutathione transferase activity was determined by the rate of formation of glutathione S conjugates by reacting reduced glutathione with a substrate of 1-chloro-2.4-dinitrobenzene. Glutathione peroxidase activity was evaluated by the formation of oxidized glutathione. The activity of glutathione reductase in erythrocytes was determined by the method, is based on measuring the oxidation rate of NADPH+H+, which is recorded by decreasing absorption at a wavelength of 340 nm. A decrease in the ratio of GSH/GSSG in rat erythrocytes under conditions of toxic damage against a nutritional deficiency of protein is indicated by a functional shift in the thiol-disulfide balance towards increased use of the reduced form of glutathione for antioxidant protection. It was established that toxic damage is a key factor in reducing the level of glutathione transferase against the background of an increase in glutathione peroxidase activity in rat erythrocytes, the activation of which probably prevents the progression of LPO processes. At the same time, under conditions of toxic damage, against the background of alimentary protein deficiency, a decrease in glutathione reductase and glucose-6-phosphate dehydrogenase activity is observed, which leads to blocking of the first stage of glucose-6-phosphate metabolism in the pentose phosphate cycle, resulting in a decrease in the amount of NADPH and, accordingly reduced glutathione.

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Park, Hyeyoung, and Youn-Kyoo Choung. "Degradation of Antibiotics (Tetracycline, Sulfathiazole, Ampicillin) Using Enzymes of Glutathion S-Transferase." Human and Ecological Risk Assessment: An International Journal 13, no. 5 (September 18, 2007): 1147–55. http://dx.doi.org/10.1080/10807030701506223.

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Verbeeck, MAE, P. Marx, EFM Wouters, SjSc Wagenaar, and FBJM Thunnissen. "Increased gene expression of glutathion-S-transferase-pi in human lung carcinomas." Cancer Genetics and Cytogenetics 77, no. 2 (October 1994): 173. http://dx.doi.org/10.1016/0165-4608(94)90328-x.

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Zamora, Zullyt B., Aluet Borrego, Orlay Y. López, René Delgado, Ricardo González, Silvia Menéndez, Frank Hernández, and Siegfried Schulz. "Effects of Ozone Oxidative Preconditioning on TNF-αRelease and Antioxidant-Prooxidant Intracellular Balance in Mice During Endotoxic Shock." Mediators of Inflammation 2005, no. 1 (2005): 16–22. http://dx.doi.org/10.1155/mi.2005.16.

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Ozone oxidative preconditioning is a prophylactic approach, which favors the antioxidant-prooxidant balance for preservation of cell redox state by the increase of antioxidant endogenous systems in both in vivo and in vitro experimental models. Our aim is to analyze the effect of ozone oxidative preconditioning on serum TNF-αlevels and as a modulator of oxidative stress on hepatic tissue in entodoxic shock model (mice treated with lipopolysaccharide (LPS)). Ozone/oxygen gaseous mixture which was administered intraperitoneally (0.2,0.4, and1.2mg/kg) once daily for five days before LPS (0.1mg/kg, intraperitoneal). TNF-αwas measured by cytotoxicity on L-929 cells. Biochemical parameters such as thiobarbituric acid reactive substances (TBARS), enzymatic activity of catalase, glutathione peroxidase, and glutathione-S transferase were measured in hepatic tissue. One hour after LPS injection there was a significant increase in TNF-αlevels in mouse serum. Ozone/oxygen gaseous mixture reduced serum TNF-αlevels in a dose-dependent manner. Statistically significant decreases in TNF-αlevels after LPS injection were observed in mice pretreated with ozone intraperitoneal applications at0.2(78%),0.4(98%), and1.2(99%). Also a significant increase in TBARS content was observed in the hepatic tissue of LPS-treated mice, whereas enzymatic activity of glutathion-S transferase and glutathione peroxidase was decreased. However in ozone-treated animals a significant decrease in TBARS content was appreciated as well as an increase in the activity of antioxidant enzymes. These results indicate that ozone oxidative preconditioning exerts inhibitory effects on TNF-αproduction and on the other hand it exerts influence on the antioxidant-prooxidant balance for preservation of cell redox state by the increase of endogenous antioxidant systems.

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LAWAL-ARE, Aderonke Omolara, Rasheed Olatunji MORUF, Sarah Oyeyinka OLUSEYE-ARE, and Tajudeen Opeyemi ISOLA. "Antioxidant Defense System Alternations in Four Crab Species as a Bio-Indicator of Environmental Contamination." Bulletin of University of Agricultural Sciences and Veterinary Medicine Cluj-Napoca. Veterinary Medicine 76, no. 1 (June 12, 2019): 73. http://dx.doi.org/10.15835/buasvmcn-vm:2019.0001.

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The ecological health status of aquatic environment is a determinant for the survival and growth of organisms within such niche. An investigative study was carried out on four crab species – Cardiosoma armatum, Goniopsis pelli, Callinectes amnicola, Portunus validusinhabiting contaminated sites in Lagos Lagoon- exploring their anti-oxidant defense mechanism in the light of heavy metal concentration in the crab tissues. Amongst the measured heavy metals, cadmium level proved to be significantly highest (P<0.05) with range concentration of 0.42±0.12mg/kg (G. pelli)- 0.79±0.06 mg/kg (C. armatum). Contrastingly, lead was marginally low with concentration below 0.01 mg/kg in all the crab species. Organismal responses to environmental pollution showed a high level of biomarkers. C. armatum was observed to have elevated level of superoxide dismutase (123.04±0.01min/mg/pro), catalase (7.74±0.05min/mg/pro), glutathion transferase (18.21±0.02 Hmol/mg pro), reduced glutathione (2.92±0.04Hmol/mg pro) and glutathione peroxidase (61.85±0.06 Hmol/mg pro) above other species with C. amnicola recording the lowest concentration of the biomarkers. With the low level of heavy metals and corresponding high concentration of these biomarkers, the pollution indices within the study habitat are quite modest.

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Afifi, Mohamed, Omar A. Almaghrabi, and Naif Mohammed Kadasa. "Ameliorative Effect of Zinc Oxide Nanoparticles on Antioxidants and Sperm Characteristics in Streptozotocin-Induced Diabetic Rat Testes." BioMed Research International 2015 (2015): 1–6. http://dx.doi.org/10.1155/2015/153573.

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The present study investigated the impact of zinc oxide nanoparticles (ZnONPs) on the oxidative status and sperm characteristics in diabetic rat testicular tissue. Forty male albino rats were used in this study; 10 of them served as a control and 30 rats were injected with a single dose (100 mg/kg) of streptozotocin intraperitoneally. They were subdivided into diabetic, diabetic + ZnONPs (10 mg/kg B.W.), and diabetic and cotreated with ZnONPs + insulin groups. The sperm count and motility were assessed. The activity and mRNA expression of superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), glutathione reductase (GRD), and Glutathion-S-Transferase (GST) were determined in the testicular tissue. Malondialdehyde (MDA) and reduced glutathione (GSH) levels were estimated in the testicular tissue. Sperm count and motility increased in ZnONPs treated diabetic rats. A significant increase in the activity and mRNA expression of SOD, CAT, GPx, GRD, and GST was shown in ZnONPs treated diabetic rats. MDA significantly decreased, while GSH increased in testicular tissue of ZnONPs treated diabetic rats. It was concluded that ZnONPs either alone or in combination with insulin have the ability to increase the sperm count and motility and protect the testicular tissue against the oxidative stress induced by diabetes in rats.

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Yang, Mon-Yuan, Tung-Wei Hung, Chau-Jong Wang, and Tsui-Hwa Tseng. "Inhibitory Effect of Nelumbo nucifera Leaf Extract on 2-Acetylaminofluorene-induced Hepatocarcinogenesis Through Enhancing Antioxidative Potential and Alleviating Inflammation in Rats." Antioxidants 8, no. 9 (August 22, 2019): 329. http://dx.doi.org/10.3390/antiox8090329.

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Leaf extract of Nelumbo nucifera (NLE) has been demonstrated to possess anti-atherosclerosis, improve alcohol-induced steatohepatitis, prevent high-fat diet-induced obesity, and inhibit the proliferation and metastasis of human breast cancer cells. This study determines the chemopreventive role of NLE against 2-acetylaminofluorene (AAF)-induced hepatocellular carcinoma (HCC) in rats. AAF was used to induce hepatocarcinogenesis in rats through genetic and nongenetic effects. After administration for 12 weeks, NLE (0.5–2%) supplementation orally inhibited AAF (0.03%)-induced hepatic fibrosis which appears during the development of premalignant lesions in rats. After the 6-month experiment, NLE supplementation resulted in decreasing AAF-induced serum parameters of hepatic injury, including the level of triglycerides, total cholesterol, alpha-fetoprotein (AFP), and inflammatory mediator interleukin (IL)-6 and tumor necrosis factor (TNF)-α as well as the activities of alanine aminotransferase (ALT), aspartate aminotransferase (AST), and gamma-glutamyl transferase (γGT). NLE supplementation also reduced AAF-induced lipid peroxidation and 8-hydroxy-2′-deoxyguanosine (8-OHdG) formation in the rat liver. Hepatic histopathological investigation revealed that NLE supplementation attenuated the AAF-induced HCC and glutathione S-transferase-Pi (GST-Pi) expression. Furthermore, NLE supplementation increased the expression of transcription factor, nuclear factor erythroid 2-related factor 2 (Nrf2) and its downstream targets, including catalase, glutathion peroxidase (GPx), and superoxide dismutase 1 (SOD-1) in the rat liver. Our findings indicate that NLE supplementation inhibited AAF-induced hepatocarcinogenesis by enhancing antioxidative potential and alleviating inflammation in rats.

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Nurkhasanah, Laela Hayu Nurani, and Zainur Rahman Hakim. "Effect of rosella (Hibiscus sabdariffa L) extract on glutathione-S-transferase activity in rats." Tropical Journal of Pharmaceutical Research 16, no. 10 (November 14, 2017): 2411–16. http://dx.doi.org/10.4314/tjpr.v16i10.14.

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Purpose: To determine the effect of rosella (Hibiscus sabdariffa L) extract on glutathione-S-trasferase (GST) activity and its hepatoprotective effect.Methods: A total of 25 rats were divided randomly into 5 groups (5 rats per group). Group I served as the baseline, group II was the negative control group, while groups III, IV and V were treated with rosella extract at doses of 10, 50 and 100 mg /kg /day, respectively for 35 days. On day 36, the animals were given a single dose of dimethyl benz(a)anthracene (DMBA) orally. After one week, blood was taken from the sinus orbitalis for measurement of serum glutamate pyruvate transaminase (SGPT) and serum glutamate oxaloacetate transaminase (SGOT) activities by a kinetic method with DIasys® kit. The activity of GST was measured in liver homogenate using 1-choloro-2,4-dinitrobenzene (CDNB) method, while the expression of GST gene was determined by reverse transcriptase polymerase chain reaction (RT-PCR).Results: Treatment with rosella extract at 10, 50 and 100 mg /kg for 35 days led to significant increasesin GST activity relative to the control group. In addition, serum SGPT and SGOT activities were significantly decreased. There were significant increases in the expression of GST gene as evidenced by increased GST band intensity.Conclusion: These results indicate that rosella possesses significant hepatoprotective effect against hepatic injury caused by DMBA treatment. Thus, rosella may be useful for the prevention of oxidative stress caused by free radicals produced from pollutants and foods.Keywords: Hibiscus sabdariffa, Rosella, Glutamate pyruvate transaminase (SGPT), Glutamate oxaloacetate transaminase (SGOT), glutathion-S-transferase (GST)

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Neefjes, Veronica M., Chris T. Evelo, Leo Baars, and Carlos E. Blanco. "Glutathion-S-transferase as marker of oxidative stress in sick and healthy premature infants. † 985." Pediatric Research 41 (April 1997): 167. http://dx.doi.org/10.1203/00006450-199704001-01004.

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Komiya, Yasuhiro, Hiromasa Tsukino, Hiroyuki Nakao, Yoshiki Kuroda, Hirohisa Imai, and Takahiko Katoh. "Human glutathion S-transferase A1 polymorphism and susceptibility to urothelial cancer in the Japanese population." Cancer Letters 221, no. 1 (April 2005): 55–59. http://dx.doi.org/10.1016/j.canlet.2004.10.042.

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Movafagh, A., F. Maleki, S. G. Mohammadzadeh, and S. Fadaei. "Association of glutathion S-transferase and chromosomal aberrations as a means to determine occupational exposure." International Congress Series 1276 (February 2005): 197–98. http://dx.doi.org/10.1016/j.ics.2004.12.011.

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Zaets, Iryna, Sergij Kramarev, and Natalia Kozyrovska. "Inoculation with a bacterial consortium alleviates the effect of cadmium overdose in soybean plants." Open Life Sciences 5, no. 4 (August 1, 2010): 481–90. http://dx.doi.org/10.2478/s11535-010-0025-1.

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AbstractInoculating plants that have inefficient antioxidant systems with plant-associated bacteria allows them to overcome heavy metal intoxication. We monitored protein oxidation, the activity of plant defense system enzymes, and the phenolics content in soybean (Glycine max L.) during a prolonged exposure to cadmium (Cd). The assistance of the bacterial consortium reduced the bioavailability of Cd in a soil containing 10 times the metal’s Standard Maximum Value (SMV). This reduced the accumulation of Cd in the soybeans’ roots and seeds. At 100 SMV, bacterial inoculation resulted in increased Cd bioavailability, which enhanced cadmium uptake by the soybean plants. At both Cd concentrations, oxidative stress was more prolonged in the soybean’s roots than its leaves. In cadmium-polluted soil, glutathion peroxidase activity changed more rapidly in the roots of plants when they had been inoculated. Inhibition of the peroxidases’ activities strengthened the activity of glutathione-S-transferase; increased the phenolics content in plant roots; and alleviated stress in inoculated soybean plants compared to untreated plants. The bacterial consortium may be recommended for a plant protection at 10 SMV Cd in the soil, and for phytostabilization at 100 SMV.

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CHINAMI, MASANOBU, and MASAHISA SHINGU. "Construction of an Expression Vector for Human Papillomavirus Type 16 E7-Glutathion S Transferase Fusion Protein." Kurume Medical Journal 39, no. 1 (1992): 9–12. http://dx.doi.org/10.2739/kurumemedj.39.9.

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Jahnke, V., R. Strange, Chr Matthias, and A. A. Fryer. "Erste Ergebnisse über Glutathion-S-Transferase GSTM1 und GSTT1 Genotypen und die genetische Prädisposition beim Larynxkarzinom*." Laryngo-Rhino-Otologie 74, no. 11 (November 1995): 691–94. http://dx.doi.org/10.1055/s-2007-997826.

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Matthias, C., V. Jahnke, A. Fryer, and R. C. Strange. "Einfluss von Glutathion S-Transferase und Cytochrom P450 Genpolymorphismen auf das Verhalten von Kopf-Hals-Karzinomen." Laryngo-Rhino-Otologie 81, no. 06 (June 13, 2002): 406–12. http://dx.doi.org/10.1055/s-2002-32208.

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Vyushina, A. V., A. V. Pritvorova, O. G. Semenova, and N. E. Ordyan. "The effect of prenatal stress on antioxidant glutathion-assosiated enzymes activity in subcellular fractions of rat's liver." Biomeditsinskaya Khimiya 67, no. 4 (2021): 347–51. http://dx.doi.org/10.18097/pbmc20216704347.

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The activity of glutathione-associated antioxidant enzymes in subcellular fractions (cytosolic, mitochondrial, and cell nucleus fractions) was investigated in the liver of adult male Wistar rats born after prenatal stress was. Two groups of animals were studied in the experiment: (1) control group included — animals was born by intact mothers, and (2) prenatal stress group included animals whose mothers were subjected to immobilization stress in high-light conditions from the 15th to the 19th day of pregnancy. The activity of glutathione peroxidase (EC 1.11.1.9) in prenatally stressed animals decreased in the fractions of nuclei and mitochondria compared to the control group, while the activity of glutathione reductase (EC 1.8.1.7.) increased in the same subcellular fractions. The activity of glutathione transferase (EC 2.5.1.18) in prenatally stressed rats reduced in the cytosol and mitochondrial fractions as compared to control group. Redistribution of the antioxidant enzyme activity in the cytosol, the fraction of nuclei and the mitochondrial fraction of liver tissue may contribute to the formation of the pathological phenotype of prenatally stressed offspring.

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Weimin, Yang, Zeng Xiaoyong, Chen Chunlian, Chen Zhong, and Du Guanghui. "Correlative expression of glutathion S-Transferase-π and multidrug resistance associated protein in bladder transitional cell carcinoma." Journal of Tongji Medical University 20, no. 4 (December 2000): 311–14. http://dx.doi.org/10.1007/bf02888188.

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Беляева, Elena Belyaeva, Ершова, and Oksana Ershova. "Polymorphism of gene glutathion-s-transferase Pi in teenagers from Buryat ethnic group living in the irkutsk region." Бюллетень Восточно-Сибирского научного центра Сибирского отделения Российской академии медицинских наук 1, no. 5 (December 6, 2016): 165–69. http://dx.doi.org/10.12737/23418.

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Human glutathione-S-transferases play an important role in phase II detoxification process. But poly-morphism in the GSTP1 gene has not been studied in certain populations.Aim: to determine the distribution of allele and genotype frequencies of GSTP1 gene in teenagers from Buryat ethnic group.Materials and methods. Blood samples were obtained from 55 teenagers from Buryat ethnic group. There were 28 males and 27 females with an age of 14.05±0.99 years over the range of 13 to 16. DNA was isolated from blood samples. The polymerase chain reaction was used to amplify A313G and C341T markers of the GSTP1 gene. Chi-square testing was used to evaluate the significant difference of the GSTP1 genotype frequencies between observed and expected values.Results. Allele and genotype frequencies of A313G and C341T markers GSTP1 were determined in teenagers from Buryat ethnic group. The study showed that the frequencies of A and G alleles at the A313G marker were 0.809 and 0.191 while those of C and T alleles at the C341T marker were 0.973 and 0.027, respectively. The distribution of the genotype frequencies at the A313G marker were consistent with expected in a Hardy–Weinberg equilibrium (χ2=0 .77; d.f.=1; p>0.05). However, the distribution of the genotype frequencies at the C341T marker were not consistent with expected in a Hardy – Weinberg equilibrium (χ2= 0.043; d.f.= 1; p<0.05). It was because the homozygous of T allele was not found in the ethnic group of Buryat.

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Tsikas, Dimitrios, Kay Kohlhaw, and Gorig Brunner. "Funktionen und Anwendung von Glutathion S-Transferase und Epoxid-Hydratase in einem enzymatischen Hohlfaser-Reaktor zur extrakorporalen Entgiftung." Chemie Ingenieur Technik 63, no. 11 (November 1991): 1150–51. http://dx.doi.org/10.1002/cite.330631126.

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Cakir, Tayfun, and Seyho Yucetas. "Comparison of glutathion-s-transferase A-4 expression values between lumbar spinal canal stenosis and lumbar discal hernia patients." Annals of Medical Research 26, no. 12 (2019): 2887. http://dx.doi.org/10.5455/annalsmedres.2019.09.534.

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Németh, Zs K., M. Abonyi, T. Tóth, Z. Bori, and P. Nagy. "The efficacy of alpha-glutathion-S-transferase determination asamarker of hepatic injury in asymptomatic HCV carriers,alcoholicsand drug abusers." Journal of Hepatology 32 (2000): 189. http://dx.doi.org/10.1016/s0168-8278(00)81050-8.

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Akgul, S. U., F. S. Oguz, Y. Çalişkan, C. Kekik, H. Gürkan, A. Türkmen, I. Nane, and F. Aydin. "The Effect of Glutathion S-Transferase Polymoprhisms and Anti-GSST1 Antibodies on Allograft Functions in Recipients of Renal Transplant." Transplantation Proceedings 44, no. 6 (July 2012): 1679–84. http://dx.doi.org/10.1016/j.transproceed.2012.04.004.

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Danielson, U. H., and B. Mannervik. "Paradoxical inhibition of rat glutathione transferase 4-4 by indomethacin explained by substrate-inhibitor-enzyme complexes in a random-order sequential mechanism." Biochemical Journal 250, no. 3 (March 15, 1988): 705–11. http://dx.doi.org/10.1042/bj2500705.

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Under standard assay conditions, with 1-chloro-2,4-dinitrobenzene (CDNB) as electrophilic substrate, rat glutathione transferase 4-4 is strongly inhibited (I50 = 1 microM) by indomethacin. No other glutathione transferase investigated is significantly inhibited by micromolar concentrations of indomethacin. Paradoxically, the strong inhibition of glutathione transferase 4-4 was dependent on high (millimolar) concentrations of CDNB; at low concentrations of this substrate or with other substrates the effect of indomethacin on the enzyme was similar to the moderate inhibition noted for other glutathione transferases. In general, the inhibition of glutathione transferases can be explained by a random-order sequential mechanism, in which indomethacin acts as a competitive inhibitor with respect to the electrophilic substrate. In the specific case of glutathione transferase 4-4 with CDNB as substrate, indomethacin binds to enzyme-CDNB and enzyme-CDNB-GSH complexes with an even greater affinity than to the corresponding complexes lacking CDNB. Under presumed physiological conditions with low concentrations of electrophilic substrates, indomethacin is not specific for glutathione transferase 4-4 and may inhibit all forms of glutathione transferase.

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Stockman, P. K., G. J. Beckett, and J. D. Hayes. "Identification of a basic hybrid glutathione S-transferase from human liver. Glutathione S-transferase δ is composed of two distinct subunits (B1 and B2)." Biochemical Journal 227, no. 2 (April 15, 1985): 457–65. http://dx.doi.org/10.1042/bj2270457.

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The purification of a hybrid glutathione S-transferase (B1 B2) from human liver is described. This enzyme has an isoelectric point of 8.75 and the B1 and B2 subunits are distinguishable immunologically and are ionically distinct. Hybridization experiments demonstrated that B1 B1 and B2 B2 could be resolved by CM-cellulose chromatography and have pI values of 8.9 and 8.4 respectively. Transferase B1 B2, and the two homodimers from which it is formed, are electrophoretically and immunochemically distinct from the neutral enzyme (transferase mu) and two acidic enzymes (transferases rho and lambda). Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis demonstrated that B1 and B2 both have an Mr of 26 000, whereas, in contrast, transferase mu comprises subunits of Mr 27 000 and transferases rho and lambda both comprise subunits of Mr 24 500. Antisera raised against B1 or B2 monomers did not cross-react with the neutral or acidic glutathione S-transferases. The identity of transferase B1 B2 with glutathione S-transferase delta prepared by the method of Kamisaka, Habig, Ketley, Arias & Jakoby [(1975) Eur. J. Biochem. 60, 153-161] has been demonstrated, as well as its relationship to other previously described transferases.

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Alin, P., H. Jensson, E. Cederlund, H. Jörnvall, and B. Mannervik. "Cytosolic glutathione transferases from rat liver. Primary structure of class alpha glutathione transferase 8-8 and characterization of low-abundance class Mu glutathione transferases." Biochemical Journal 261, no. 2 (July 15, 1989): 531–39. http://dx.doi.org/10.1042/bj2610531.

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Six GSH transferases with neutral/acidic isoelectric points were purified from the cytosol fraction of rat liver. Four transferases are class Mu enzymes related to the previously characterized GSH transferases 3-3, 4-4 and 6-6, as judged by structural and enzymic properties. Two additional GSH transferases are distinguished by high specific activities with 4-hydroxyalk-2-enals, toxic products of lipid peroxidation. The most abundant of these two enzymes, GSH transferase 8-8, a class Alpha enzyme, has earlier been identified in rat lung and kidney. The amino acid sequence of subunit 8 was determined and showed a typical class Alpha GSH transferase structure including an N-acetylated N-terminal methionine residue.

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Özkan-Yılmaz, Ferbal, Arzu Özlüer-Hunt, Mehmet Berköz, and Metin Yıldırım. "Investigation of Glutathion S-Transferase, Adenosine deaminase, Paraoxonase Activities in Liver of Oncorhynchus mykiss Fed with Nucleotide-Yeast Supplemented Diet." Natural and Engineering Sciences 3, no. 3 (October 10, 2018): 300–310. http://dx.doi.org/10.28978/nesciences.468960.

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Grubisa, Ivana, Petar Otasevic, Nebojsa Despotovic, Velimir Dedic, Jelena Milasin, and Nada Vucinic. "Genetic polymorphism of glutathion S-transferase P1 (GSTP1) Ile105Val and susceptibility to atherogenesis in patients with type 2 diabetes mellitus." Genetika 45, no. 1 (2013): 227–36. http://dx.doi.org/10.2298/gensr1301227g.

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One of the characteristics of type 2 diabetes mellitus (T2DM) is the state of persistent oxidative stress (OS) that has been implicated in the pathogenesis of diseases such is atherosclerosis mainly through chronic hyperglycemia that stimulates production of reactive oxygen species (ROS) and increases OS. Glutathione S-transferase P1 (GSTP1) is a member of the cytosolic GST superfamily. It plays an important role in neutralizing OS as an enzyme. Also, it participates in regulation of stress signaling and protects cells against apoptosis via its noncatalytic ligand-binding activity. GSTP1 Ile105Val functional polymorphism influences protein catalytic activity and stability and the aim of this study was to determine whether this gene variation influences susceptibility to atherogenesis in T2DM patients. A total of 240 individuals (140 patients with T2DM, accompanied with clinical manifestations of atherosclerosis, and 100 healthy controls) were included in this study. Genomic DNA was isolated from peripheral blood cells and genotyping was performed using polymerase chain reaction followed by restriction fragment length polymorphism (PCR-RFLP) analysis. We obtained no statistically significant differences in the distribution of alleles and genotypes between cases and controls (P>0.05) but association between Ile/Val (OR=0.6, 95%CI=0.35-1.05, P=0.08) and Val/Val (OR=0.45, 95%CI=0.18-1.11, P=0.08) genotypes and disease approached significance (P=0.08). Our results indicated that a larger study group is needed to establish the true relationship between potentialiy protective allele Val and the disease, and to determine the influence of other GSTP1 polymorphisms on atherogenesis in T2DM patients.

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Danielson, U. H., H. Esterbauer, and B. Mannervik. "Structure-activity relationships of 4-hydroxyalkenals in the conjugation catalysed by mammalian glutathione transferases." Biochemical Journal 247, no. 3 (November 1, 1987): 707–13. http://dx.doi.org/10.1042/bj2470707.

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The substrate specificities of 15 cytosolic glutathione transferases from rat, mouse and man have been explored by use of a homologous series of 4-hydroxyalkenals, extending from 4-hydroxypentenal to 4-hydroxypentadecenal. Rat glutathione transferase 8-8 is exceptionally active with the whole range of 4-hydroxyalkenals, from C5 to C15. Rat transferase 1-1, although more than 10-fold less efficient than transferase 8-8, is the second most active transferase with the longest chain length substrates. Other enzyme forms showing high activities with these substrates are rat transferase 4-4 and human transferase mu. The specificity constants, kcat./Km, for the various enzymes have been determined with the 4-hydroxyalkenals. From these constants the incremental Gibbs free energy of binding to the enzyme has been calculated for the homologous substrates. The enzymes responded differently to changes in the length of the hydrocarbon side chain and could be divided into three groups. All glutathione transferases displayed increased binding energy in response to increased hydrophobicity of the substrate. For some of the enzymes, steric limitations of the active site appear to counteract the increase in binding strength afforded by increased chain length of the substrate. Comparison of the activities with 4-hydroxyalkenals and other activated alkenes provides information about the active-site properties of certain glutathione transferases. The results show that the ensemble of glutathione transferases in a given species may serve an important physiological role in the conjugation of the whole range of 4-hydroxyalkenals. In view of its high catalytic efficiency with all the homologues, rat glutathione transferase 8-8 appears to have evolved specifically to serve in the detoxication of these reactive compounds of oxidative metabolism.

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Peters, W. H. M., H. M. J. Roelofs, F. M. Nagengast, and J. H. M. van Tongeren. "Human intestinal glutathione S-transferases." Biochemical Journal 257, no. 2 (January 15, 1989): 471–76. http://dx.doi.org/10.1042/bj2570471.

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Cytosolic glutathione S-transferases were purified from the epithelial cells of human small and large intestine. These preparations were characterized with regard to specific activities, subunit and isoenzyme composition. Isoenzyme composition and specific activity showed little variation from proximal to distal small intestine. Specific activities of hepatic and intestinal enzymes from the same patient were comparable. Hepatic enzymes were mainly composed of 25 kDa subunits. Transferases from small intestine contained 24 and 25 kDa subunits, in variable amounts. Colon enzymes were composed of 24 kDa subunits. In most preparations, however, minor amounts of 27 and 27.5 kDa subunits were detectable. Separation into isoforms by isoelectric focusing revealed striking differences: glutathione S-transferases from liver were mainly basic or neutral, enzymes from small intestine were basic, neutral and acidic, whereas large intestine contained acidic isoforms only. The intestinal acidic transferase most probably was identical with glutathione S-transferase Pi, isolated from human placenta. In the hepatic preparation, this isoform was hardly detectable. The specific activity of glutathione S-transferase showed a sharp fall from small to large intestine. In proximal and distal colon, activity seemed to be about equal. In the ascending colon there might be a relationship between specific activity of glutathione S-transferases and age of the patient, activity decreasing with increasing age.

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Hasni, Dita, Kamal B. Siregar, and Hadyanto Lim. "The influence of glutathion S-transferase P-1 polymorphism A313G rs1695 on the susceptibility to cyclophosphamide hematologic toxicity in Indonesian patients." Medical Journal of Indonesia 25, no. 2 (July 26, 2016): 118–26. http://dx.doi.org/10.13181/mji.v25i2.1308.

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Background: Chemotherapy often causes side effects such as hematologic toxicity. The degree of toxicity is often associated with genetic polymorphism. This study aims to determine the influence of GSTP1 A313G polymorphism, an enzyme responsible for detoxifying cyclophosphamid, on incidence and severity of cyclophosphamid hematologic toxicity.Methods: 91 Indonesian females diagnosed with breast cancer at Haji Adam Malik Central General Hospital, Medan, receiving cyclophosphamide, doxorubicin/epirubicin and 5-FU were included in this retrospective cohort study. DNA was extracted from peripheral leukocytes and GSTP1 A313G genotyping was analyzed using polymerase chain reaction-restriction length fragment polymorphism (PCR-RFLP). Genotype deviation and allele frequencies were also determined by Hardy-Weinberg Equilibrium. The degrees of hematologic toxicity (leucopenia and neutropenia data after chemotherapy cycles 1 and 3) were collected from the patient medical records. The data were analyzed using chi-square test.Results: 60.4% of the patients had the wildtype (A/A), while 29.7% were heterozygous (A/G), and 9.9% were homozygous mutant (G/G). There was no significant deviation of allele and genotype frequency from Hardy-Weinberg Equilibrium. The G allele (A/G & G/G) contributes to more severe degree of leukopenia compared to patients with wild type allele (A/A) (p<0.05) after the 3rd chemotherapy cycles.Conclusion: There was association between GSTP1 polymorphism with the degree of hematologic toxicity in breast cancer patients receiving cyclophosphamide chemotherapy regimen.

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Schön, M. R., N. Akkoc, W. Heil, St Wolf, M. Matthes, H. Schrem, O. Kollmar, and P. Neuhaus. "Die Bestimmung der α-Glutathion-S-Transferase-Konzentration zur Beurteilung hepatozellulärer Ischämieschäden im Vergleich zu GOT, GPT und LDH im Lebertransplantationsmodell." LaboratoriumsMedizin 23, no. 4 (January 1999): 218–27. http://dx.doi.org/10.1515/labm.1999.23.4.218.

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Ilyinskikh, N. N., E. N. Ilyinskikh, A. M. Subbotin, and V. N. Nekrasov. "Teratozoospermia and karyopathological abnormalities of blood cells in human granulocytic anaplasmosis depending on polymorphism of GSTM1 gene of glutathion-S-transferase." Problemy reproduktsii 24, no. 5 (2018): 101. http://dx.doi.org/10.17116/repro201824051101.

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Kurz, M. A., T. D. Boyer, R. Whalen, T. E. Peterson, and D. G. Harrison. "Nitroglycerin metabolism in vascular tissue: role of glutathione S-transferases and relationship between NO. and NO2– formation." Biochemical Journal 292, no. 2 (June 1, 1993): 545–50. http://dx.doi.org/10.1042/bj2920545.

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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-.

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Meyer, D. J., E. Lalor, B. Coles, A. Kispert, P. Ålin, B. Mannervik, and B. Ketterer. "Single-step purification and h.p.l.c. analysis of glutathione transferase 8–8 in rat tissues." Biochemical Journal 260, no. 3 (June 15, 1989): 785–88. http://dx.doi.org/10.1042/bj2600785.

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GSSG selectively elutes two GSH transferases from a mixture of rat GSH transferases bound to a GSH-agarose affinity matrix. One is a form of GSH transferase 1-1 and the other is shown to be GSH transferase 8-8. By using tissues that lack this form of GSH transferase 1-1 (e.g. lung), GSH transferase 8-8 may thus be purified from cytosol in a single step. Quantitative analysis of the tissue distribution of GSH transferase 8-8 was obtained by h.p.l.c.

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Syafitri, Syafitri. "PENGARUH PEMBERIAN Curcuma xanthoriza Roxb TERHADAP PERBAIKAN KERUSAKAN SEL HEPAR." Jurnal Ilmu Kedokteran dan Kesehatan 6, no. 3 (December 31, 2019): 236–41. http://dx.doi.org/10.33024/jikk.v6i3.2192.

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Hepatitis kronis merupakan salah satu masalah besar yang dihadapi dunia termasuk di Indonesia. Hepatitis kronis dapat berkembang menjadi progresif yang menjadi awal terjadinya sirosis hati dan akhirnya kanker hati pada 20-30 % kasus. Hepatitis secara patofisiologi akan menyebabkan kerusakan sel pada hati. Hepatoprotektor adalah suatu senyawa obat yang dapat memberikan perlindungan pada hati dari kerusakan yang ditimbulkan oleh racun, obat, dan lain-lain. Temulawak diteliti dapat berperan sebagai hepatoprotektor. Temulawak adalah salah satu tanaman herbal yang dapat dijadikan alternatif pengobatan karena komponen didalamnya seperti curcumin (diferuloylmethane), demetoxycurcumin, bisdemetoxycurcumin serta banyak zat aktif lainnya. Mekanisme kurkumin dalam menjaga sel-sel hepar dari kerusakan yaitu sejalan dengan efek kurkumin sebagai antioksidan. Kurkumin akan menangkap ion superoksida dan memutus rantai ion antar superoksida (O2-) yang pada akhirnya proses peroksidasi lipid ini akan mencegah kerusakan hepar yang dimediasi oleh enzim antioksidan yaitu Superoxide Dismutase (SOD) dimana enzim SOD akan mengonversi O2- menjadi produk yang kurang toksik. Selain mekanisme tersebut, mekanisme kurkumin dalam mencegah terjadinya kerusakan sel hepar yaitu juga dengan meningkatkan glutathion S-transferase (GST) dan menghambat beberapa faktor proinflamasi seperti nuclear factor-ĸB (NF-kB) dan profibrotik sitokin. Temulawak dapat mencegah kerusakan sel pada hepar.

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Schecter, Robyn L., Moulay A. Alaoui-Jamali, and Gerald Batist. "Glutathione S-transferase in chemotherapy resistance and in carcinogenesis." Biochemistry and Cell Biology 70, no. 5 (May 1, 1992): 349–53. http://dx.doi.org/10.1139/o92-054.

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Cytosolic glutathione S-transferases are composed of two monomeric subunits. These monomers are the products of different gene families designated alpha, mu, and pi. Dimerization yields either homodimeric or heterodimeric holoenzymes within the same family. The members of this complex group of proteins have been linked to the detoxification of environmental chemicals and carcinogens, and have been shown to be overexpressed in normal and tumor cells following exposure to cytotoxic drugs. They also are overexpressed in carcinogen-induced rat liver preneoplastic nodules in rat liver. In all of these cases, the changes in exprssion of glutathione S-transferases are paralleled by increased resistance to cytotoxic chemicals. The degree of resistance is related to the substrate specificity of the isozyme. The relationship of the glutathione S-transferase genes to drug resistance has been directly demonstrated by gene transfer studies, where cDNAs encoding the various subunits of glutathione S-transferase have been transfected into a variety of cell types. This review discusses the results of numerous studies that associate resistance to alkylating agents with overexpression of protective detoxifying glutathione S-transferase enzymes.Key words: glutathione S-transferase, chemotherapy, carcinogenesis, alkylating agents, DNA damage.

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Tan, K. H., D. J. Meyer, N. Gillies, and B. Ketterer. "Detoxification of DNA hydroperoxide by glutathione transferases and the purification and characterization of glutathione transferases of the rat liver nucleus." Biochemical Journal 254, no. 3 (September 15, 1988): 841–45. http://dx.doi.org/10.1042/bj2540841.

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DNA peroxidized by exposure to ionizing radiation in the presence of oxygen is a substrate for the Se-independent GSH peroxidase activity of several GSH transferases, GSH transferases 5-5, 3-3 and 4-4 being the most active in the rat liver soluble supernatant fraction (500, 35 and 20 nmol/min per mg of protein respectively) and GSH transferases mu and pi the most active, so far found, in the human liver soluble supernatant fraction (80 and 10 nmol/min per mg respectively). Although the GSH transferase content of the rat nucleus was found to be much lower than that of the soluble supernatant, nuclear GSH transferases are likely to be more important in the detoxification of DNA hydroperoxide produced in vivo. Two nuclear fractions were studied, one extracted with 0.075 M-saline/0.025 M-EDTA, pH 8.0, and the other extracted from the residue with 8.5 M-urea. The saline/EDTA fraction contained subunits 1, 2, 3, 4 and a novel subunit, similar but not identical to 5, provisionally referred to as 5*, in the proportions 40:25:5:5:25 respectively. The 8.5 M-urea-extracted fraction contained principally subunit 5* together with a small amount of subunit 6 in the proportion 95:5 respectively. GSH transferase 5*-5* purified from the 8.5 M-urea extract has the highest activity towards DNA hydroperoxide of any GSH transferase so far studied (1.5 mumol/min per mg). A Se-dependent GSH peroxidase fraction from rat liver was also active towards DNA hydroperoxide; however, since this enzyme accounts for only 14% of the GSH peroxidase activity detectable in the nucleus, GSH transferases may be the more important source of this activity. The possible role of GSH transferases, in particular GSH transferase 5*-5*, in DNA repair is discussed.

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Bier, Henning, and Uwe Gamer. "ln-vitro-Untersuchungen an zehn Kopf-Hals-Karzinomlinien zur Abhängigkeit der Chemosensitivität vom Glutathiongehalt und von der Aktivität der Glutathion-S-Transferase." Oto-Rhino-Laryngologia Nova 4, no. 5-6 (1994): 273–77. http://dx.doi.org/10.1159/000313138.

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Chianale, Jose, Ana M. Wielandt, and Valeska Vollrath. "Co-induction of multispecific organic anion transporter, Г-glutamylcysteine synthetase and glutathion-S-transferase genes by phenolic antioxidants in the mouse liver." Gastroenterology 118, no. 4 (April 2000): A999. http://dx.doi.org/10.1016/s0016-5085(00)86148-x.

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Tahir, M. K., N. Ozer, and B. Mannervik. "Isoenzymes of glutathione transferase in rat small intestine." Biochemical Journal 253, no. 3 (August 1, 1988): 759–64. http://dx.doi.org/10.1042/bj2530759.

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The major glutathione transferases in the rat small-intestine cytosol were isolated and characterized. The enzymes active with 1-chloro-2,4-dinitrobenzene as second substrate were almost quantitatively recovered after affinity chromatography on immobilized S-hexylglutathione. The different basic forms of glutathione transferase, which account for 90% of the activity, were resolved by chromatofocusing. Fractions containing enzymes with lower isoelectric points were not further resolved. The isolated fractions were characterized by their elution position in chromatofocusing, apparent subunit Mr, reactions with specific antibodies, substrate specificities and inhibition characteristics. The major basic forms identified were glutathione transferases 1-1, 4-4 and 7-7. In addition, evidence for the presence of a variant form of subunit 1, as well as trace amounts of subunits 2 and 3, was obtained. A significant amount of transferase 8-8 in the fraction of acidic enzyme forms was demonstrated by immunoblot and Ouchterlony double-diffusion analysis. In the comparison of the occurrence of the different forms of glutathione transferase in liver, lung, kidney and small intestine, it was found that the small intestine is the richest source of glutathione transferase 7-7.

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Paret, Aurelie, Delphine Rolland, Vincent Ribrag, Bertrand Coiffier, and Catherine Thieblemont. "Inhibition of GSTpi Activity Increases the Sensitivity of MCL Cell Lines to Cisplatin, Cytarabin and Bortezomib, but Not Doxorubicin." Blood 106, no. 11 (November 16, 2005): 2806. http://dx.doi.org/10.1182/blood.v106.11.2806.2806.

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Abstract Preliminary data suggest drug resistance plays a major role in mantle cell lymphoma (MCL) and is linked to the aberrant expression of molecules such as Glutathion S-Transferase pi (GST pi) that catalyzes the nuclear conjugation of a broad variety of reactive electrophiles to the glutathion. We investigated in vitro the effect of the inhibition of GSTpi activity on the chemosensitivity of MCL cell lines by inhibiting the nuclear transport of GSTpi with Agaricus bisporus leptine (ABL). Methods. Four MCL cell lines (Granta, NCEB, REC and UPN1) were analyzed for GSTP1 transcript expression by RT-PCR analysis and for GSTP1 genetic Ile105Val polymorphism. The effect of ABL on the 4 MCL cell lines viability was examined using cells pre-treated with ABL (40μg/ml) for 10 h followed by treatment with various concentrations of doxorubicin (DOX), cisplatin (CDDP), cytarabin and bortezomib for 48 h. The cell viability was estimated by MTT assay repeated three times. Results. All the 4 cell lines expressed GSTPI transcript. Two of them (UPN1 and REC) were heterozygous for Ile105Val polymorphism, whereas NCEB and GRANTA were homozygous GSTP1-105Ile which has been correlated with an enzyme of high activity. DOX, CDDP, cytarabin and bortezomib have cytotoxic effects compared to non-treated cells, without any difference between the 4 MCL cell lines when considering their genetic polymorphism status. Co-administration of ABL caused a significant increasis of the cytotoxicity of CDDP and bortezomib in all cell lines (Student test: p between 0.0004 to 0.02 for CDDP; and p between 0.013 and 0.05 for velcade, depending on the cell lines). Co-administration of ABL caused an increasis of the cytotoxicity of cytarabin in 3 cell lines, the 4th being actually tested. No influence of ABL was detected on the cytotoxic effect of DOX. The analysis of the nuclear and the cytoplasmic localizations of GSTpi is currently realized by immunohistochemistry. Conclusion. These results suggest that inhibition of the nuclear transfer of GSTpi increases in vitro the MCL sensitivity to CDDP, cytarabin and velcade but not DOX.

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Del Boccio, G., C. Di Ilio, P. Alin, H. Jörnvall, and B. Mannervik. "Identification of a novel glutathione transferase in human skin homologous with class alpha glutathione transferase 2-2 in the rat." Biochemical Journal 244, no. 1 (May 15, 1987): 21–25. http://dx.doi.org/10.1042/bj2440021.

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Six forms of glutathione transferase with pI values of 4.6, 5.9, 6.8, 7.1, 8.5 and 9.9 have been isolated from the cytosol fraction of normal skin from three human subjects. The three most abundant enzymes were an acidic Class Pi transferase (pI 4.6; apparent subunit Mr 23,000), a basic Class Alpha transferase (pI 8.5; apparent subunit Mr 24,000) and an even more basic glutathione transferase of Class Alpha (pI 9.9; apparent subunit Mr 26,500). The last enzyme, which was previously unknown, accounts for 10-20% of the glutathione transferase in human skin. The novel transferase showed greater similarities with rat glutathione transferase 2-2, another Class Alpha enzyme, than with any other known transferase irrespective of species. The most striking similarities included reactions with antibodies, amino acid compositions and identical N-terminal amino acid sequences (16 residues). The close relationship between the human most basic and the rat glutathione transferase 2-2 supports the classification of the transferases previously proposed and indicates that the similarities between enzymes isolated from different species are more extensive than had been assumed previously.

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Brophy, P. M., C. Southan, and J. Barrett. "Glutathione transferases in the tapeworm Moniezia expansa." Biochemical Journal 262, no. 3 (September 15, 1989): 939–46. http://dx.doi.org/10.1042/bj2620939.

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Four forms of GSH transferase were resolved from Moniezia expansa cytosol by GSH-Sepharose affinity chromatography and chromatofocusing in the range pH 6-4, and the presence of isoenzymes was further suggested by analytical isoelectric focusing. The four GSH transferase forms in the cestode showed no clear biochemical relationship to any one mammalian GSH transferase family. The N-terminal of the major GSH transferase form showed sequence homology with the Mu and Alpha family GSH transferases. The major GSH transferase appeared to bind a number of commercially available anthelmintics but did not appear to conjugate the compounds with GSH. The major GSH transferase efficiently conjugated members of the trans-alk-2-enal and trans, trans-alka-2,4-dienal series, established secondary products of lipid peroxidation.

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Çelık, Veysel Kenan, Zeynep Deniz Şahın, İsmail Sari, and Sevtap Bakir. "Comparison of Oxidant/Antioxidant, Detoxification Systems in Various Tissue Homogenates and Mitochondria of Rats with Diabetes Induced by Streptozocin." Experimental Diabetes Research 2012 (2012): 1–5. http://dx.doi.org/10.1155/2012/386831.

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Objective. Oxidative stress is considered to be the main factor in the development of diabetic complications and tissue injury. our objective was to investigate and compare the oxidant/antioxidant conditions and detoxification mechanisms of the liver, lung, kidney, cardiac tissues, and mitochondria of rats with diabetes induced by streptozocin (STZ).Methods. Rats with diabetes induced by streptozocin were anesthetized by administering 90 mg/kg ketamine hydrochloride and 3 mg/kg xylazine hydrochloride. Thoracic cavities were incised open; liver, lung, kidney, and cardiac tissues were removed and stored at−70°C. All samples were homogenized and mitochondrial fractions were separated. Total Antioxidant Status (TAS), Total Oxidant Status (TOS), Oxidative Stress Index (OSI), Paraoxonase (PON), Arylesterase, Catalase (Cat), Malondialdehyde (MDA), and Glutathion-S-transferase were measured in each fraction.Results. MDA and TOS levels were significantly increased in liver tissues, and T OS and OSI were increased in the mitochondrial fractions of diabetic rats. These increases were not statistically significant compared to the control group. No significant differences were determined in the antioxidant and GST activities.Conclusion. According to our results, oxidative stress has not developed in rats with diabetes induced by streptozocin. The detoxification system was induced; however, this induction did not differ significantly from the controls.

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Gervas, Polina, Natalia Smetannikova, Maria Vasilieva, Nadejda Cherdyntseva, Valentina Belyavskaya, Aleksey Dobrodeev, Sergey Tusikov, Natalia Sevostianova, and Alla Dmitrieva. "P2-008: Influence of common glutathion-S-transferase and DNA repair variant alleles on p53 function: relation to lung cancer risk and progression." Journal of Thoracic Oncology 2, no. 8 (August 2007): S484—S485. http://dx.doi.org/10.1097/01.jto.0000283450.55572.61.

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Journal articles on the topic 'Glutathion transferase'

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