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Articoli di riviste sul tema "Glutathione"

Autore: Grafiati

Pubblicato: 4 giugno 2021

Ultima modifica: 25 luglio 2025

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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, № 9 (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 o

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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 (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 glutath

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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 (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

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4

Sardari, Veronica, Valeriana Pantea, Aurelian Gulea, et al. "Thiol-disulfide metabolism in kidney tissue at the administration of some copper coordination compounds." Moldovan Medical Journal 63 (2) (May 30, 2020): 12–17. https://doi.org/10.5281/zenodo.3865976.

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<strong>Background: </strong>Thiol-disulfide metabolism is essential for normal function of the organism. Thus the interest of the scientists in this area of research continues to grow. <strong>Material and methods: </strong>Copper coordination compounds (CCC), derivatives of thiosemicarbaside (CMD-4, CMJ-33, CMT-67), action on thiol-disulfide metabolism in the healthy <em>Ratta albicans</em> kidneys were studied. The animals were divided in 6 groups of 7 rats each. The control group included healthy rats which were injected i/m physiological solution 3 times a week, for 30 days. The rats from

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5

Iskusnykh, Igor Y., Anastasia A. Zakharova, and Dhruba Pathak. "Glutathione in Brain Disorders and Aging." Molecules 27, no. 1 (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

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6

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 (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 col

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7

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 (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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8

Gutyj, B. V., D. F. Gufriy, V. Y. Binkevych, et al. "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 (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

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9

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 (2009): 129–44. http://dx.doi.org/10.1134/s1990750809020036.

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10

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 (1994): 1668–74. http://dx.doi.org/10.1006/bbrc.1994.2378.

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11

Ullah, Hashmat, and Muhammad Farid Khan. "GLUTATHIONE;." Professional Medical Journal 21, no. 06 (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

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12

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

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13

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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14

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

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15

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

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16

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

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17

Fraternale, Alessandra, Serena Brundu, and Mauro Magnani. "Glutathione and glutathione derivatives in immunotherapy." Biological Chemistry 398, no. 2 (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 alte

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18

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

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19

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

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20

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

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21

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 (2008): 469–73. http://dx.doi.org/10.1016/j.jinf.2008.03.009.

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22

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 (2009): 8042–53. http://dx.doi.org/10.1074/jbc.m807771200.

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23

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

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24

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 (1999): 171–84. http://dx.doi.org/10.1016/s0301-2115(98)00242-5.

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25

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 (1998): 277–87. http://dx.doi.org/10.1007/s004290050184.

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26

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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27

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

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28

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 (1991): 48–53. http://dx.doi.org/10.1016/0003-9861(91)90163-d.

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29

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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30

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 (2008): 9591–98. http://dx.doi.org/10.1002/chem.200800946.

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31

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 (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 len

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32

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 (2002): 421–32. http://dx.doi.org/10.1081/jdi-120006769.

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33

Fitri, Loeki Enggar, Agustin Iskandar, Teguh Wahju Sardjono, et al. "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 (2016): 646–50. http://dx.doi.org/10.1016/j.apjtb.2016.06.003.

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34

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 (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-

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35

Kolesnikova, L. I., O. A. Vanteeva, N. A. Kurashova, and B. Ya Vlasov. "GLUTATHION AS AN IMPORTANT COMPONENT OF THIOSULFID SYSTEM OF INFERTILITY PATHOGENESIS IN OVERWEIGHT MEN." Annals of the Russian academy of medical sciences 68, no. 7 (2013): 9–12. http://dx.doi.org/10.15690/vramn.v68i7.705.

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Aim: to study the glutathionic part of thiosulfid system and oxidative stress in infertile men with different body mass index. Patients and methods: examined 60 infertile men with normal and overweight, and 40 healthy men with proven fertility. Active components of the antioxidant defense system of the body was assessed by the level of reduced and oxidized glutathione by the method of PY Hissin, determination of TBA-active products was carried out by the method VB Gavrilova. In the analysis of inter-group differences for independent samples was used parametric Student criterion. Results: the o

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36

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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37

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

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38

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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39

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

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40

García-Giménez, José Luis, Jelena Markovic, Francisco Dasí, et al. "Nuclear glutathione." Biochimica et Biophysica Acta (BBA) - General Subjects 1830, no. 5 (2013): 3304–16. http://dx.doi.org/10.1016/j.bbagen.2012.10.005.

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41

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

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42

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

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43

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

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44

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

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Abstract (sommario):

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

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45

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

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46

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

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47

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

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48

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 (1993): 1413–17. http://dx.doi.org/10.1038/bjc.1993.262.

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49

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

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50

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 (1999): 1383–87. http://dx.doi.org/10.1016/s0891-5849(98)00335-9.

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