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Journal articles on the topic 'Glutathione'

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Author: Grafiati

Published: 4 June 2021

Last updated: 29 July 2024

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1

Rubino, Federico Maria. "The Redox Potential of the β-93-Cysteine Thiol Group in Human Hemoglobin Estimated from In Vitro Oxidant Challenge Experiments." Molecules 26, no. 9 (April 26, 2021): 2528. http://dx.doi.org/10.3390/molecules26092528.

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Glutathionyl hemoglobin is a minor form of hemoglobin with intriguing properties. The measurement of the redox potential of its reactive β-93-Cysteine is useful to improve understanding of the response of erythrocytes to transient and chronic conditions of oxidative stress, where the level of glutathionyl hemoglobin is increased. An independent literature experiment describes the recovery of human erythrocytes exposed to an oxidant burst by measuring glutathione, glutathione disulfide and glutathionyl hemoglobin in a two-hour period. This article calculates a value for the redox potential E0 of the β-93-Cysteine, considering the erythrocyte as a closed system at equilibrium described by the Nernst equation and using the measurements of the literature experiment. The obtained value of E0 of −121 mV at pH 7.4 places hemoglobin as the most oxidizing thiol of the erythrocyte. By using as synthetic indicators of the concentrations the electrochemical potentials of the two main redox pairs in the erythrocytes, those of glutathione–glutathione disulfide and of glutathionyl–hemoglobin, the mechanism of the recovery phase can be hypothesized. Hemoglobin acts as the redox buffer that scavenges oxidized glutathione in the oxidative phase and releases it in the recovery phase, by acting as the substrate of the NAD(P)H-cofactored enzymes.

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2

Jones, C. M., A. Lawrence, P. Wardman, and M. J. Burkitt. "Kinetics of superoxide scavenging by glutathione: an evaluation of its role in the removal of mitochondrial superoxide." Biochemical Society Transactions 31, no. 6 (December 1, 2003): 1337–39. http://dx.doi.org/10.1042/bst0311337.

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Superoxide radicals are produced in trace amounts by the mitochondrial respiratory chain. Most are removed rapidly by superoxide dismutase in the matrix. Superoxide is also known to react with glutathione. Reported values of the rate constant for this reaction range from 102 to in excess of 105 M−1·s−1. The magnitude of this rate constant has important physiological implications because, if it is at the upper end of the reported range, a significant proportion of mitochondrial superoxide will evade removal by superoxide dismutase, and will oxidize glutathione to the potentially harmful glutathionyl radical. Using EPR spectroscopy to monitor competition between glutathione and the spin trap 5,5-dimethyl-1-pyrroline N-oxide for reaction with superoxide, we have estimated that the rate constant for the reaction between superoxide and glutathione is only ~200 M−1·s−1. Hence superoxide dismutase will always out-compete glutathione for reaction with the superoxide radical, thereby preventing formation of the glutathionyl radical.

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3

Smith, K., A. Borges, M. R. Ariyanayagam, and A. H. Fairlamb. "Glutathionylspermidine metabolism in Escherichia coli." Biochemical Journal 312, no. 2 (December 1, 1995): 465–69. http://dx.doi.org/10.1042/bj3120465.

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Intracellular levels of glutathione and glutathionylspermidine conjugates have been measured throughout the growth phases of Escherichia coli. Glutathionylspermidine was present in mid-log-phase cells, and under stationary and anaerobic growth conditions accounted for 80% of the total glutathione content. N1,N8-bis(glutathionyl)spermidine (trypanothione) was undetectable under all growth conditions. The catalytic constant kcat/Km of recombinant E. coli glutathione reductase for glutathionylspermidine disulphide was approx. 11,000-fold lower than that for glutathione disulphide. The much higher catalytic constant for the mixed disulphide of glutathione and glutathionylspermidine (11% that of GSSG), suggests a possible explanation for the low turnover of trypanothione disulphide by E. coli glutathione reductase, given the apparent lack of a specific glutathionylspermidine disulphide reductase in E. coli.

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4

van Hylckama Vlieg, Johan E. T., Hans Leemhuis, Jeffrey H. Lutje Spelberg, and Dick B. Janssen. "Characterization of the Gene Cluster Involved in Isoprene Metabolism in Rhodococcus sp. Strain AD45." Journal of Bacteriology 182, no. 7 (April 1, 2000): 1956–63. http://dx.doi.org/10.1128/jb.182.7.1956-1963.2000.

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ABSTRACT The genes involved in isoprene (2-methyl-1,3-butadiene) utilization in Rhodococcus sp. strain AD45 were cloned and characterized. Sequence analysis of an 8.5-kb DNA fragment showed the presence of 10 genes of which 2 encoded enzymes which were previously found to be involved in isoprene degradation: a glutathioneS-transferase with activity towards 1,2-epoxy-2-methyl-3-butene (isoI) and a 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase (isoH). Furthermore, a gene encoding a second glutathioneS-transferase was identified (isoJ). TheisoJ gene was overexpressed in Escherichia coliand was found to have activity with 1-chloro-2,4-dinitrobenzene and 3,4-dichloro-1-nitrobenzene but not with 1,2-epoxy-2-methyl-3-butene. Downstream of isoJ, six genes (isoABCDEF) were found; these genes encoded a putative alkene monooxygenase that showed high similarity to components of the alkene monooxygenase fromXanthobacter sp. strain Py2 and other multicomponent monooxygenases. The deduced amino acid sequence encoded by an additional gene (isoG) showed significant similarity with that of α-methylacyl-coenzyme A racemase. The results are in agreement with a catabolic route for isoprene involving epoxidation by a monooxygenase, conjugation to glutathione, and oxidation of the hydroxyl group to a carboxylate. Metabolism may proceed by fatty acid oxidation after removal of glutathione by a still-unknown mechanism.

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5

Iskusnykh, Igor Y., Anastasia A. Zakharova, and Dhruba Pathak. "Glutathione in Brain Disorders and Aging." Molecules 27, no. 1 (January 5, 2022): 324. http://dx.doi.org/10.3390/molecules27010324.

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Glutathione is a remarkably functional molecule with diverse features, which include being an antioxidant, a regulator of DNA synthesis and repair, a protector of thiol groups in proteins, a stabilizer of cell membranes, and a detoxifier of xenobiotics. Glutathione exists in two states—oxidized and reduced. Under normal physiological conditions of cellular homeostasis, glutathione remains primarily in its reduced form. However, many metabolic pathways involve oxidization of glutathione, resulting in an imbalance in cellular homeostasis. Impairment of glutathione function in the brain is linked to loss of neurons during the aging process or as the result of neurological diseases such as Huntington’s disease, Parkinson’s disease, stroke, and Alzheimer’s disease. The exact mechanisms through which glutathione regulates brain metabolism are not well understood. In this review, we will highlight the common signaling cascades that regulate glutathione in neurons and glia, its functions as a neuronal regulator in homeostasis and metabolism, and finally a mechanistic recapitulation of glutathione signaling. Together, these will put glutathione’s role in normal aging and neurological disorders development into perspective.

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6

Miteva, L. P.-E., S. V. Ivanov, V. S. Alexieva, and E. N. Karanov. "Effect of atrazine on glutathione levels, glutathione s-transferase and glutathione reductase activities in pea and wheat plants." Plant Protection Science 40, No. 1 (March 7, 2010): 160–20. http://dx.doi.org/10.17221/1352-pps.

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Changes were studied in the endogenous level of glutathione (total and oxidised), and in the amount of free thiol groups as caused by the herbicide atrazine on two species of plants with different sensitivity to it. The activities of two enzymes related to glutathione metabolism (glutathione reductase and glutathione S-transferase) were also determined. The application of the herbicide on leaf increased the levels of total and oxidised glutathione in pea and wheat plants. Increased activity glutathione S-transferase in wheat plants was found.

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7

Gutyj, B. V., D. F. Gufriy, V. Y. Binkevych, R. O. Vasiv, N. V. Demus, K. Y. Leskiv, O. M. Binkevych, and O. V. Pavliv. "Influence of cadmium loading on glutathione system of antioxidant protection of the bullocks’bodies." Scientific Messenger of LNU of Veterinary Medicine and Biotechnologies 20, no. 92 (December 10, 2018): 34–40. http://dx.doi.org/10.32718/nvlvet9207.

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It was presented the results of studies of the cadmium effect loading on the activity of the glutathione system of antioxidant protection in young cattle, namely on the activity of glutathione peroxidase, glutathione reductase, glucose-6-phosphate dehydrogenase, the level of reduced glutathion. It was established that feeding of cadmium chloride to bullocks at a dose of 0.03 and 0.05 mg/kg body weight contributed to a decrease in both the enzyme and non-enzyme link of the glutathione antioxidant defense system. The toxic effect of cadmium contributes to a change in stationary concentrations of radical metabolites. О2˙ˉ, ˙ОН, НО2˙, which, in turn, initiate lipid peroxidation processes. The lowest level of glutathione indexes of the antioxidant defense system in the blood of young cattle was established on the sixteenth and twenty fourth day of the experiment, it was associated with enhanced activation of lipoperoxidation and an imbalance between the activity of the antioxidant system and the intensity of lipid peroxidation. The feeding of cadmium chloride to bullocks at a dose of 0.03 and 0.05 mg/kg of animal weight did not affect the activity of the glutathione antioxidant defense system in their blood. It was established that the greater the amount of cadmium chloride in the feed, the lower the activity of the glutathione system of the antioxidant defense of the body of bulls. Thus, cadmium chloride suppresses the antioxidant protection system, in particular, by reducing the activity of the enzyme link: glutathione peroxidase, glutathione reductase, glucose-6-phosphate dehydrogenase, and non-enzyme link: reduced glutathione.

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8

Kulinsky, V. I., and L. S. Kolesnichenko. "The glutathione system. I. Synthesis, transport, glutathione transferases, glutathione peroxidases." Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry 3, no. 2 (May 16, 2009): 129–44. http://dx.doi.org/10.1134/s1990750809020036.

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9

Gaullier, J. M., P. Lafontant, A. Valla, M. Bazin, M. Giraud, and R. Santus. "Glutathione Peroxidase and Glutathione Reductase Activities toward Glutathione-Derived Antioxidants." Biochemical and Biophysical Research Communications 203, no. 3 (September 1994): 1668–74. http://dx.doi.org/10.1006/bbrc.1994.2378.

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10

Ullah, Hashmat, and Muhammad Farid Khan. "GLUTATHIONE;." Professional Medical Journal 21, no. 06 (December 10, 2014): 1237–41. http://dx.doi.org/10.29309/tpmj/2014.21.06.2735.

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Background: Compounds of lithium are used as drug of choice in many psychiatric disorders including bipolar disorder, depression, schizophrenia etc. Objective: The aim of this study was to analyze the effect of lithium on lymphocyte’s GSH levels for which terasaki technique was used to separate T-cells and B-cells of human volunteer’s venous blood. Study Design: Experimental Study. Setting: Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Gomal University, Dera Ismail Khan.Period:1st December 2012 to 26 February 2013.Statistical Analysis: One-way ANOVA followed by Dunnet’s HSD test. Results: Thiol quantification was done by using Ellman’s method and was found statistically significant (p < 0.001) decrease in T-cells/B-cells GSH level which was dose and time dependent. T-cells/B-cells dose dependent drop in GSH level was 2.752μM (9.41%) and 2.554 μM (16.12%) by lowest used concentration (0.003μM) of lithium citrate. Conclusion: We have noted that there is significant drop in T-cells and B-cells GSH due to which immunological alterations happen which are linked with GSH contents of lymphocytes and hence inhibition in lymphocytes activity is co-related with depletion in GSH level of these cells which ultimately with the increase in Li+1 concentration cause further decrease in GSH level leading to cells death.

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11

&NA;. "Glutathione." Reactions Weekly &NA;, no. 1309 (July 2010): 22. http://dx.doi.org/10.2165/00128415-201013090-00069.

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12

Noctor, Graham, Guillaume Queval, Amna Mhamdi, Sejir Chaouch, and Christine H. Foyer. "Glutathione." Arabidopsis Book 9 (January 2011): 1–32. http://dx.doi.org/10.1199/tab.0142.

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13

Day, Brian J. "Glutathione." Chest 127, no. 1 (January 2005): 12–14. http://dx.doi.org/10.1378/chest.83.5.39s.

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14

Day, Brian J. "Glutathione." CHEST Journal 127, no. 1 (January 1, 2005): 12. http://dx.doi.org/10.1378/chest.127.1.12.

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15

Jefferies, Heather, Jane Coster, Alizan Khalil, Joan Bot, Rosalie D. McCauley, and John C. Hall. "Glutathione." ANZ Journal of Surgery 73, no. 7 (July 2003): 517–22. http://dx.doi.org/10.1046/j.1445-1433.2003.02682.x.

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16

Fraternale, Alessandra, Serena Brundu, and Mauro Magnani. "Glutathione and glutathione derivatives in immunotherapy." Biological Chemistry 398, no. 2 (February 1, 2017): 261–75. http://dx.doi.org/10.1515/hsz-2016-0202.

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Abstract Reduced glutathione (GSH) is the most prevalent non-protein thiol in animal cells. Its de novo and salvage synthesis serves to maintain a reduced cellular environment, which is important for several cellular functions. Altered intracellular GSH levels are observed in a wide range of pathologies, including several viral infections, as well as in aging, all of which are also characterized by an unbalanced Th1/Th2 immune response. A central role in influencing the immune response has been ascribed to GSH. Specifically, GSH depletion in antigen-presenting cells (APCs) correlates with altered antigen processing and reduced secretion of Th1 cytokines. Conversely, an increase in intracellular GSH content stimulates IL-12 and/or IL-27, which in turn induces differentiation of naive CD4+ T cells to Th1 cells. In addition, GSH has been shown to inhibit the replication/survival of several pathogens, i.e. viruses and bacteria. Hence, molecules able to increase GSH levels have been proposed as new tools to more effectively hinder different pathogens by acting as both immunomodulators and antimicrobials. Herein, the new role of GSH and its derivatives as immunotherapeutics will be discussed.

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17

Wu, Jian Hui, and Gerald Batist. "Glutathione and glutathione analogues; Therapeutic potentials." Biochimica et Biophysica Acta (BBA) - General Subjects 1830, no. 5 (May 2013): 3350–53. http://dx.doi.org/10.1016/j.bbagen.2012.11.016.

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18

Mustacich, Debbie. "Measurement of Glutathione and Glutathione Disulfide." Current Protocols in Toxicology 00, no. 1 (May 1999): 6.2.1–6.2.14. http://dx.doi.org/10.1002/0471140856.tx0602s00.

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19

Saydam, N., A. Kirb, Ö. Demir, E. Hazan, Ö. Oto, O. Saydam, and G. Güner. "Determination of glutathione, glutathione reductase, glutathione peroxidase and glutathione S-transferase levels in human lung cancer tissues." Cancer Letters 119, no. 1 (October 1997): 13–19. http://dx.doi.org/10.1016/s0304-3835(97)00245-0.

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20

Prasad, C. V. Balasubrahmanya, Mallikarjun V. Kodliwadmath, and Girija Basavaraj Kodliwadmath. "Erythrocyte glutathione peroxidase, glutathione reductase activities and blood glutathione content in leprosy." Journal of Infection 56, no. 6 (June 2008): 469–73. http://dx.doi.org/10.1016/j.jinf.2008.03.009.

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21

Sato, Ikuo, Motoyuki Shimizu, Takayuki Hoshino, and Naoki Takaya. "The Glutathione System ofAspergillus nidulansInvolves a Fungus-specific GlutathioneS-Transferase." Journal of Biological Chemistry 284, no. 12 (January 26, 2009): 8042–53. http://dx.doi.org/10.1074/jbc.m807771200.

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22

Ketterer, B. "Detoxication reactions of glutathione and glutathione transferases." Xenobiotica 16, no. 10-11 (January 1986): 957–73. http://dx.doi.org/10.3109/00498258609038976.

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23

Knapen, Maarten F. C. M., Petra L. M. Zusterzeel, Wilbert H. M. Peters, and Eric A. P. Steegers. "Glutathione and glutathione-related enzymes in reproduction." European Journal of Obstetrics & Gynecology and Reproductive Biology 82, no. 2 (February 1999): 171–84. http://dx.doi.org/10.1016/s0301-2115(98)00242-5.

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24

Huster, Dominik, Ole P. Hjelle, Finn-Mogens Haug, Erlend A. Nagelhus, Winfried Reichelt, and O. P. Ottersen. "Subcellular compartmentation of glutathione and glutathione precursors." Anatomy and Embryology 198, no. 4 (September 1, 1998): 277–87. http://dx.doi.org/10.1007/s004290050184.

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25

Moscow, Jeffrey A., and Katharine H. Dixon. "Glutathione-related enzymes, glutathione and multidrug resistance." Cytotechnology 12, no. 1-3 (1993): 155–70. http://dx.doi.org/10.1007/bf00744663.

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26

Casalone, Enrico, Carmine Di Ilio, Giorgio Federici, and Mario Polsinelli. "Glutathione and glutathione metabolizing enzymes in yeasts." Antonie van Leeuwenhoek 54, no. 4 (July 1988): 367–75. http://dx.doi.org/10.1007/bf00393527.

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27

Chung, Phyllis M., Roseann E. Cappel, and Hiram F. Gilbert. "Inhibition of glutathione disulfide reductase by glutathione." Archives of Biochemistry and Biophysics 288, no. 1 (July 1991): 48–53. http://dx.doi.org/10.1016/0003-9861(91)90163-d.

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28

Aw, Tak Yee, Grazyna Wierzbicka, and Dean P. Jones. "Oral glutathione increases tissue glutathione in vivo." Chemico-Biological Interactions 80, no. 1 (1991): 89–97. http://dx.doi.org/10.1016/0009-2797(91)90033-4.

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29

Dourado, Daniel F A. R., Pedro Alexandrino Fernandes, Bengt Mannervik, and Maria João Ramos. "Glutathione Transferase: New Model for Glutathione Activation." Chemistry - A European Journal 14, no. 31 (October 29, 2008): 9591–98. http://dx.doi.org/10.1002/chem.200800946.

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30

MONTE, Massimo DAL, Ilaria CECCONI, Francesca BUONO, Pier Giuseppe VILARDO, Antonella DEL CORSO, and Umberto MURA. "Thioltransferase activity of bovine lens glutathione S-transferase." Biochemical Journal 334, no. 1 (August 15, 1998): 57–62. http://dx.doi.org/10.1042/bj3340057.

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A Mu-class glutathione S-transferase purified to electrophoretic homogeneity from bovine lens displayed thioltransferase activity, catalysing the transthiolation reaction between GSH and hydroxyethyldisulphide. The thiol-transfer reaction is composed of two steps, the formation of GSSG occurring through the generation of an intermediate mixed disulphide between GSH and the target disulphide. Unlike glutaredoxin, which is only able to catalyse the second step of the transthiolation process, glutathioneS-transferase catalyses both steps of the reaction. Data are presented showing that bovine lens glutathione S-transferase and rat liver glutaredoxin, which was used as a thioltransferase enzyme model, can operate in synergy to catalyse the GSH-dependent reduction of hydroxyethyldisulphide.

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31

De Vega, L., R. Pérez Fernández, M. C. Martin Mateo, J. Bustamante Bustamante, A. Mendiluce Herrero, and E. Bustamante Munguira. "GLUTATHIONE DETERMINATION AND A STUDY OF THE ACTIVITY OF GLUTATHIONE-PEROXIDASE, GLUTATHIONE-TRANSFERASE, AND GLUTATHIONE-REDUCTASE IN RENAL TRANSPLANTS." Renal Failure 24, no. 4 (January 2002): 421–32. http://dx.doi.org/10.1081/jdi-120006769.

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32

Fitri, Loeki Enggar, Agustin Iskandar, Teguh Wahju Sardjono, Ummu Ditya Erliana, Widya Rahmawati, Didi Candradikusuma, Utama Budi Saputra, Eko Suhartono, Bambang Setiawan, and Erma Sulistyaningsih. "Plasma glutathione and oxidized glutathione level, glutathione/oxidized glutathione ratio, and albumin concentration in complicated and uncomplicated falciparum malaria." Asian Pacific Journal of Tropical Biomedicine 6, no. 8 (August 2016): 646–50. http://dx.doi.org/10.1016/j.apjtb.2016.06.003.

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33

Asojo, Oluwatoyin A., and Christopher Ceccarelli. "Structure of glutathioneS-transferase 1 from the major human hookworm parasiteNecator americanus(Na-GST-1) in complex with glutathione." Acta Crystallographica Section F Structural Biology Communications 70, no. 9 (August 29, 2014): 1162–66. http://dx.doi.org/10.1107/s2053230x1401646x.

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GlutathioneS-transferase 1 fromNecator americanus(Na-GST-1) is a vaccine candidate for hookworm infection that has a high affinity for heme and metal porphyrins. As part of attempts to clarify the mechanism of heme detoxification by hookworm GSTs, co-crystallization and soaking studies ofNa-GST-1 with the heme-like molecules protoporphyrin IX disodium salt, hematin and zinc protoporphyrin were undertaken. While these studies did not yield the structure of the complex ofNa-GST-1 with any of these molecules, co-crystallization experiments resulted in the first structures of the complex ofNa-GST-1 with the substrate glutathione. The structures of the complex ofNa-GST-1 with glutathione were solved from pathological crystalline aggregates comprising more than one crystal form. These first structures of the complex ofNa-GST-1 with the substrate glutathione were solved by molecular replacement from data collected with a sealed-tube home source using the previously reported apo structure as the search model.

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34

Dixon, David P., and Robert Edwards. "Glutathione Transferases." Arabidopsis Book 8 (January 2010): e0131. http://dx.doi.org/10.1199/tab.0131.

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35

Kulinsky, V. I., and L. S. Kolesnichenko. "Mitochondrial glutathione." Biochemistry (Moscow) 72, no. 7 (July 2007): 698–701. http://dx.doi.org/10.1134/s0006297907070024.

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36

Anderson, M. E. "Glutathione biosynthesis." Pathophysiology 5 (June 1998): 59. http://dx.doi.org/10.1016/s0928-4680(98)80507-5.

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37

Lu, Shelly C. "Glutathione synthesis." Biochimica et Biophysica Acta (BBA) - General Subjects 1830, no. 5 (May 2013): 3143–53. http://dx.doi.org/10.1016/j.bbagen.2012.09.008.

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38

García-Giménez, José Luis, Jelena Markovic, Francisco Dasí, Guillaume Queval, Daniel Schnaubelt, Christine H. Foyer, and Federico V. Pallardó. "Nuclear glutathione." Biochimica et Biophysica Acta (BBA) - General Subjects 1830, no. 5 (May 2013): 3304–16. http://dx.doi.org/10.1016/j.bbagen.2012.10.005.

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39

Bachhawat, Anand K., Anil Thakur, Jaspreet Kaur, and M. Zulkifli. "Glutathione transporters." Biochimica et Biophysica Acta (BBA) - General Subjects 1830, no. 5 (May 2013): 3154–64. http://dx.doi.org/10.1016/j.bbagen.2012.11.018.

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40

Brigelius-Flohé, Regina, and Matilde Maiorino. "Glutathione peroxidases." Biochimica et Biophysica Acta (BBA) - General Subjects 1830, no. 5 (May 2013): 3289–303. http://dx.doi.org/10.1016/j.bbagen.2012.11.020.

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41

Bachhawat, Anand Kumar, and Amandeep Kaur. "Glutathione Degradation." Antioxidants & Redox Signaling 27, no. 15 (November 20, 2017): 1200–1216. http://dx.doi.org/10.1089/ars.2017.7136.

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42

Hayes, John D., Jack U. Flanagan, and Ian R. Jowsey. "GLUTATHIONE TRANSFERASES." Annual Review of Pharmacology and Toxicology 45, no. 1 (September 22, 2005): 51–88. http://dx.doi.org/10.1146/annurev.pharmtox.45.120403.095857.

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This review describes the three mammalian glutathione transferase (GST) families, namely cytosolic, mitochondrial, and microsomal GST, the latter now designated MAPEG. Besides detoxifying electrophilic xenobiotics, such as chemical carcinogens, environmental pollutants, and antitumor agents, these transferases inactivate endogenous α,β-unsaturated aldehydes, quinones, epoxides, and hydroperoxides formed as secondary metabolites during oxidative stress. These enzymes are also intimately involved in the biosynthesis of leukotrienes, prostaglandins, testosterone, and progesterone, as well as the degradation of tyrosine. Among their substrates, GSTs conjugate the signaling molecules 15-deoxy-Δ12,14-prostaglandin J2 (15d-PGJ2) and 4-hydroxynonenal with glutathione, and consequently they antagonize expression of genes trans-activated by the peroxisome proliferator-activated receptor γ (PPARγ) and nuclear factor-erythroid 2 p45-related factor 2 (Nrf2). Through metabolism of 15d-PGJ2, GST may enhance gene expression driven by nuclear factor-κB (NF-κB). Cytosolic human GST exhibit genetic polymorphisms and this variation can increase susceptibility to carcinogenesis and inflammatory disease. Polymorphisms in human MAPEG are associated with alterations in lung function and increased risk of myocardial infarction and stroke. Targeted disruption of murine genes has demonstrated that cytosolic GST isoenzymes are broadly cytoprotective, whereas MAPEG proteins have proinflammatory activities. Furthermore, knockout of mouse GSTA4 and GSTZ1 leads to overexpression of transferases in the Alpha, Mu, and Pi classes, an observation suggesting they are part of an adaptive mechanism that responds to endogenous chemical cues such as 4-hydroxynonenal and tyrosine degradation products. Consistent with this hypothesis, the promoters of cytosolic GST and MAPEG genes contain antioxidant response elements through which they are transcriptionally activated during exposure to Michael reaction acceptors and oxidative stress.

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43

Anderson, Mary E., and Alton Meister. "Glutathione monoesters." Analytical Biochemistry 183, no. 1 (November 1989): 16–20. http://dx.doi.org/10.1016/0003-2697(89)90164-4.

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44

Gilliland, Gary L. "Glutathione proteins." Current Opinion in Structural Biology 3, no. 6 (January 1993): 875–84. http://dx.doi.org/10.1016/0959-440x(93)90151-a.

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45

Compagnone, D., R. Massoud, C. Di Ilio, and G. Federici. "Potentiometric Determination of Glutathione and Glutathione Transferase Activity." Analytical Letters 24, no. 6 (June 1991): 993–1004. http://dx.doi.org/10.1080/00032719108054369.

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46

Peters, WH, HMJ Roelofs, MP Hectors, FM Nagengast, and JBM Jansen. "Glutathione and glutathione S-transferases in Barrett's epithelium." British Journal of Cancer 67, no. 6 (June 1993): 1413–17. http://dx.doi.org/10.1038/bjc.1993.262.

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47

van Lieshout, F. M. M., J. B. M. J. Jansen, and W. H. M. Peters. "Glutathione and glutathione S-transferases in Barrettʼs epithelium." European Journal of Gastroenterology & Hepatology 10, no. 12 (December 1998): A33. http://dx.doi.org/10.1097/00042737-199812000-00119.

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Bosch-Morell, Francisco, Leopold Flohé, Nuria Marín, and Francisco J. Romero. "4-hydroxynonenal inhibits glutathione peroxidase: protection by glutathione." Free Radical Biology and Medicine 26, no. 11-12 (June 1999): 1383–87. http://dx.doi.org/10.1016/s0891-5849(98)00335-9.

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van Lieshout, EMM, JBMJ Jansen, and WHM Peters. "Glutathione and glutathione S-transferases in Barrett's epithelium." Gastroenterology 114 (April 1998): A321. http://dx.doi.org/10.1016/s0016-5085(98)81303-6.

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Gelinsky, M., R. Vogler, and H. Vahrenkamp. "Zinc complexation of glutathione and glutathione-derived peptides." Inorganica Chimica Acta 344 (February 2003): 230–38. http://dx.doi.org/10.1016/s0020-1693(02)01320-8.

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