Bibliografie tematiche / Glutathione

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Letteratura scientifica selezionata sul tema "Glutathione"

Autore: Grafiati

Pubblicato: 4 giugno 2021

Ultima modifica: 29 luglio 2024

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Articoli di riviste sul tema "Glutathione"

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, n. 9 (26 aprile 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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Jones, C. M., A. Lawrence, P. Wardman e M. J. Burkitt. "Kinetics of superoxide scavenging by glutathione: an evaluation of its role in the removal of mitochondrial superoxide". Biochemical Society Transactions 31, n. 6 (1 dicembre 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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Smith, K., A. Borges, M. R. Ariyanayagam e A. H. Fairlamb. "Glutathionylspermidine metabolism in Escherichia coli". Biochemical Journal 312, n. 2 (1 dicembre 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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van Hylckama Vlieg, Johan E. T., Hans Leemhuis, Jeffrey H. Lutje Spelberg e Dick B. Janssen. "Characterization of the Gene Cluster Involved in Isoprene Metabolism in Rhodococcus sp. Strain AD45". Journal of Bacteriology 182, n. 7 (1 aprile 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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Iskusnykh, Igor Y., Anastasia A. Zakharova e Dhruba Pathak. "Glutathione in Brain Disorders and Aging". Molecules 27, n. 1 (5 gennaio 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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Miteva, L. P.-E., S. V. Ivanov, V. S. Alexieva e 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 (7 marzo 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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Gutyj, B. V., D. F. Gufriy, V. Y. Binkevych, R. O. Vasiv, N. V. Demus, K. Y. Leskiv, O. M. Binkevych e 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, n. 92 (10 dicembre 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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Kulinsky, V. I., e L. S. Kolesnichenko. "The glutathione system. I. Synthesis, transport, glutathione transferases, glutathione peroxidases". Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry 3, n. 2 (16 maggio 2009): 129–44. http://dx.doi.org/10.1134/s1990750809020036.

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Gaullier, J. M., P. Lafontant, A. Valla, M. Bazin, M. Giraud e R. Santus. "Glutathione Peroxidase and Glutathione Reductase Activities toward Glutathione-Derived Antioxidants". Biochemical and Biophysical Research Communications 203, n. 3 (settembre 1994): 1668–74. http://dx.doi.org/10.1006/bbrc.1994.2378.

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Ullah, Hashmat, e Muhammad Farid Khan. "GLUTATHIONE;". Professional Medical Journal 21, n. 06 (10 dicembre 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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Tesi sul tema "Glutathione"

Petit, Elise. "Etude des Glutathion Transférases : caractérisation de la classe Kappa et rôle de ces enzymes dans l'hépatotoxicité des Thiopurines". Rennes 1, 2007. http://www.theses.fr/2007REN1B072.

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Les Glutathion Tranférases (GST) constituent un système multienzymatique de détoxication. Elles sont impliquées dans la prévention , le développement des tumeurs et dans la réponse aux anticancéreux. Pendant ma thèse , je me suis intéressée à la GST de classe Kappa. Sa caractérisation nous a permis de mettre en évidence sa présence dans les mitochondries et les peroxysomes. Cette localisation particulière suggère que le GST Kappa pourrait avoir un rôle lié aux fonctions cellulaires de ces deux organites. Les GST étant en outre impliquées dans des phénomènes de résistance à des anticancéreux, je me suis également intéressée à l’hépatotoxicité des thiopurines. Nos résultats montrent que les cellules d’origine humaine sont moins sensibles à un traitement par les thiopurines que les hépatocytes de rat, bien que les composés provoquent une hépatoxicité. En conclusion le GST Kappa est présente dans les mitochondries et les peroxysomes et il pourrait y avoir une relation entre son activité et le métabolisme lipidique. Ce travail a également été l’occasion d’initier pour la première fois une étude sur les htiopurines dans les cellules hépatiques humaines

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Van, Eldik Annamaria Johanna. "Synthesis of glutathione conjugates as selective inhibitors for parasitic glutathione S transferases". Thesis, De Montfort University, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.246521.

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Halfwassen, Kathrin. "Untersuchungen zu Glutathion-sensitiven Farbstoffen in der Meerschweinchen-Retina". Doctoral thesis, Universitätsbibliothek Leipzig, 2012. http://nbn-resolving.de/urn:nbn:de:bsz:15-qucosa-89656.

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Die Glutathionverhältnisse und -verschiebungen zwischen Gliazellen und Ganglienzellen vor und nach oxidativem Stress wurden erstmals im lebenden Zellverband, ex vivo, untersucht. Die Untersuchungen erfolgten an akut isoliertem Retinagewebe vom Meerschweinchen, von welchem Bilder am Laser scanning microscope (LSM) erstellt wurden. Über die Anwendung des in vivo-Fluoreszenzfarbstoffes CellTracker Green wurde dabei dessen Spezifität für Glutathion überprüft und bestätigt.

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Yang, Bo. "Biliary glutathione transport pathways". Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0019/MQ52967.pdf.

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Lyon, Robert Patrick. "Enzymology at the dimer interface of cytosolic glutathione S-transferases /". Thesis, Connect to this title online; UW restricted, 2002. http://hdl.handle.net/1773/8165.

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Kearns, Pamela Renate. "The role of glutathione and mu class glutathione s-transferases in childhood acute leukaemia". Thesis, University of Newcastle Upon Tyne, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.311134.

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Fläring, Urban. "Glutathione during stress in man /". Stockholm, 2006. http://diss.kib.ki.se/2006/91-7140-799-5/.

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Patzewitz, Eva-Maria. "Glutathione metabolism of Plasmodium falciparum". Thesis, University of Glasgow, 2009. http://theses.gla.ac.uk/913/.

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Apicomplexan parasites of the genus Plasmodium are the causative agent of malaria, one of the most prevalent infectious diseases worldwide. Five different Plasmodium species can cause malaria in humans, leading to a total of approximately 500 million cases each year and of these, P. falciparum causes the most deadly form of the disease and is responsible for more than 1 million deaths annually. A major problem in the global fight against malaria is the widespread resistance of the parasites against the currently available drugs. It is of great importance to identify new drug target as well as to understand the mechanisms that lead to drug resistance in the first instance in order to potentially reverse the resistant phenotypes and to avoid the development of resistance in the future. The tripeptide glutathione (GSH) or γ-glutamylcysteinyl-glycine is the most abundant low molecular weight thiol in most eukaryotic organisms and serves a number of important functions as sulfhydryl-buffer, cofactor for enzymes and for the detoxification of xenobiotics and drugs. GSH is an important component of the antioxidant machinery and because malaria parasites live in an environment rich in iron and oxygen and thus increased oxidative stress, they depend on functional antioxidant systems. The biosynthesis pathway for GSH, consisting of γ-glutamylcysteine synthetase (γGCS) and glutathione synthetase (GS) is present in malaria parasites as well as in their host cells. Previous studies have shown that depletion of GSH has an antimalarial effect, but it remained unclear whether parasites were killed directly or died because their host cell could not survive the depletion of GSH. To address this question, the knockout of both genes encoding the enzymes of the GSH biosynthesis pathway in P. falciparum was attempted. While both gene loci were targeted by control constructs, the knockout of either pfγgcs or pfgs was impossible, indicating both genes are essential for parasite survival in the erythrocytic stages. To analyse the localization of γGCS and GS, GFP-tagged recombinant fusion proteins were expressed in the parasites and showed that GSH biosynthesis is cytosolic. Apart form its other functions GSH has previously been suggested to be involved in resistance to the antimalarial drug chloroquine (CQ). CQ was for a long time the first line antimalarial drug due to its high efficiency, low cost and low toxicity, but is now widely inefficient in the treatment of the disease. CQ resistance is associated with mutations in the CQ resistance transporter (PfCRT), a membrane protein of the digestive vacuole that allows the efflux of the drug form its site of action. However, PfCRT mutations alone cannot explain the full array of phenotypes found in resistant parasites. GSH is able to degrade heme, the target of CQ, in vitro and it has been suggested that elevated GSH levels contribute to CQ resistance. However, analyses of isogenic parasite lines bearing different forms of PfCRT in this study revealed lower GSH levels and higher susceptibility to inhibition of GSH biosynthesis in the CQ resistant lines. These changes did not correlate with changes in the expression of enzymes involved in the de novo biosynthesis or consumption of GSH. However, the cellular accumulation ratio for CQ indicated a decrease of free heme in the resistant parasites. Mutant forms of PfCRT expressed in oocytes of Xenopus laevis were able to transport GSH, while the sensitive wild-type form did not transport the tripeptide. The findings of this study suggest that in parasites bearing mutant PfCRT, GSH is transported into the digestive vacuole where it is able to contribute to resistance by degrading heme, before the tripeptide itself is degraded by peptidases inside the vacuole, consistent with the overall reduction of GSH levels in CQ resistant parasites.

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Evans, D. C. "Renal processing of glutathione conjugates". Thesis, University of Nottingham, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.383757.

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Di, Ilio C. "Studies on bacterial glutathione transferase". Thesis, Cranfield University, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.333472.

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Libri sul tema "Glutathione"

1940-, Dolphin David, Avramović Olga e Poulson Rozanne, a cura di. Glutathione. New York: Wiley, 1989.

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1940-, Dolphin David, Avramović Olga e Poulson Rozanne, a cura di. Glutathione. New York: Wiley, 1989.

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1942-, Sies H., e Ketterer Brian, a cura di. Glutathione conjugation: Mechanisms and biological significance. London: Academic Press, 1988.

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C, Awasthi Yogesh, a cura di. Toxicology of glutathione transferases. Boca Raton, FL: CRC\Taylor & Francis, 2007.

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Eldik, Annamaria Johanna van. Synthesis of glutathione conjugates as selective inhibitors for parasitic glutathione s-transferases. Leicester: De Montfort University, 2002.

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1953-, Viña José, a cura di. Glutathione: Metabolism and physiological functions. Boca Raton, Fla: CRC Press, 1990.

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1953-, Viña José, a cura di. Glutathione: Metabolism and physiological functions. Boca Raton, Fla: CRC Press, 1990.

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A, Shaw Christopher, a cura di. Glutathione in the nervous system. Washington, DC: Taylor & Francis, 1998.

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J, Mantle T., Pickett C. B, Hayes J. D e Cancer Research Campaign (Great Britain), a cura di. Glutathione S-transferases and carcinogenesis. London: Taylor & Francis, 1987.

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D, Tew Kenneth, a cura di. Structure and function of glutathione transferases. Boca Raton: CRC Press, 1993.

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Capitoli di libri sul tema "Glutathione"

Forman, Henry J., Hongqiao Zhang e Terrance J. Kavanagh. "Biosynthesis of Glutathione and Its Regulation". In Glutathione, 3–34. Boca Raton: Taylor & Francis, 2018. | Series: Oxidative stress and: CRC Press, 2018. http://dx.doi.org/10.1201/9781351261760-1.

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Schomburg, Lutz. "Glutathione Peroxidases and the Thyroid Gland". In Glutathione, 161–71. Boca Raton: Taylor & Francis, 2018. | Series: Oxidative stress and: CRC Press, 2018. http://dx.doi.org/10.1201/9781351261760-10.

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Mannervik, Bengt, e Birgitta Sjödin. "Glutathione Transferases". In Glutathione, 175–99. Boca Raton: Taylor & Francis, 2018. | Series: Oxidative stress and: CRC Press, 2018. http://dx.doi.org/10.1201/9781351261760-11.

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Tew, Kenneth D. "Protein S-Glutathionylation and Glutathione S-Transferase P". In Glutathione, 201–13. Boca Raton: Taylor & Francis, 2018. | Series: Oxidative stress and: CRC Press, 2018. http://dx.doi.org/10.1201/9781351261760-12.

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Morgenstern, Ralf, Jesper Z. Haeggström, Per-Johan Jakobsson e Leopold Flohé. "The Role of Glutathione in Biosynthetic Pathways and Regulation of the Eicosanoid Metabolism". In Glutathione, 215–26. Boca Raton: Taylor & Francis, 2018. | Series: Oxidative stress and: CRC Press, 2018. http://dx.doi.org/10.1201/9781351261760-13.

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Buxton, Iain L. O., e Scott D. Barnett. "Nitric Oxide and S-Nitrosoglutathione". In Glutathione, 227–32. Boca Raton: Taylor & Francis, 2018. | Series: Oxidative stress and: CRC Press, 2018. http://dx.doi.org/10.1201/9781351261760-14.

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Liedgens, Linda, e Marcel Deponte. "The Catalytic Mechanism of Glutaredoxins". In Glutathione, 251–61. Boca Raton: Taylor & Francis, 2018. | Series: Oxidative stress and: CRC Press, 2018. http://dx.doi.org/10.1201/9781351261760-15.

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Berndt, Carsten, Anna Dorothee Engelke, Klaudia Lepka e Lars Bräutigam. "The Role of Glutaredoxins in the Brain". In Glutathione, 263–75. Boca Raton: Taylor & Francis, 2018. | Series: Oxidative stress and: CRC Press, 2018. http://dx.doi.org/10.1201/9781351261760-16.

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Comini, Marcelo A. "Biosynthesis of Polyamine–Glutathione Derivatives in Enterobacteria and Kinetoplastida". In Glutathione, 285–98. Boca Raton: Taylor & Francis, 2018. | Series: Oxidative stress and: CRC Press, 2018. http://dx.doi.org/10.1201/9781351261760-17.

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Hugo, Martin, Madia Trujillo, Lucía Piacenza e Rafael Radi. "Trypanothione Functions in Kinetoplastida". In Glutathione, 307–14. Boca Raton: Taylor & Francis, 2018. | Series: Oxidative stress and: CRC Press, 2018. http://dx.doi.org/10.1201/9781351261760-18.

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Atti di convegni sul tema "Glutathione"

Demopoulos, Harry B., Myron L. Seligman, Brent L. Summers, Jeremy Ollerenshaw e John P. Richie,Jr. "Rapid, Safe, Substantial Repletion Of Intracellular Glutathione In Patients With Aquired Glutathione Insufficiency, Employing Orally Bioavailable, Pharmaceutical Glutathione". In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a1382.

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Kulikova, D. B., V. O. Nosova e A. A. Tishchenko. "FEATURES OF THE GLUTATHIONE REDOX SYSTEM IN PATIENTS AFTER CORONAVIRUS INFECTION". In X Международная конференция молодых ученых: биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023. Novosibirsk State University, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-342.

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COVID-19 includes a wide range of clinical signs and symptoms ranging from asymptomatic infections to acute respiratory distress. The glutathione redox system, represented in the human body by the enzymes glutathione-S-transferase (GST), glutathione peroxidase (GPO), and glutathione reductase (GR), provides antioxidant protection for cells. Oxidative stress plays a significant role in the course of coronavirus infection, therefore, an assessment of the state of the glutathione redox system allows us to draw conclusions about the presence and severity of oxidative stress in sick patients. In addition, studies of the antioxidant role of the glutathione redox system in protecting cells from oxidative stress have a perspective in the development and implementation of various pharmaceutical products.

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Bastiaens, Philippe I., Arie van Hoek, Jean-Claude Brochon e Antonie J. W. G. Visser. "Conformational dynamics in glutathione reductase". In OE/LASE '92, a cura di Joseph R. Lakowicz. SPIE, 1992. http://dx.doi.org/10.1117/12.58216.

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Pokidova, Olesya Viktorovna, Nina Sergeevna Emel’yanova, Alexander Vasilievich Kulikov, Alexander Ivanovich Kotelnikov e Natalia Alekseevna Sanina. "STUDY OF THE TRANSFORMATION OF NITROSYL IRON COMPLEX WITH N-ETHYLTHIOUREA LIGANDS IN MODEL BIOLOGICAL SYSTEMS". In NEW TECHNOLOGIES IN MEDICINE, BIOLOGY, PHARMACOLOGY AND ECOLOGY. Institute of information technology, 2021. http://dx.doi.org/10.47501/978-5-6044060-1-4.52.

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The process of transformation of a mononuclear cationic complex with N-ethylthiourea ligands in Tris-HCl buffer, as well as in a reaction mixture with reduced glutathione and bovine serum albumin, has been studied. It was found that in the presence of glutathione, the complex dimer-izes, while its initial ligands are replaced by glutathione. In the presence of albumin, the decay product of the complex is coordinated with amino acid residues (Cys34 and His39) to form a protein-bound complex.

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Chomoucka, Jana, Jana Drbohlavova, Vojtech Adam, Rene Kizek e Jaromir Hubalek. "Synthesis of glutathione-coated quantum dots". In 2009 32nd International Spring Seminar on Electronics Technology (ISSE). IEEE, 2009. http://dx.doi.org/10.1109/isse.2009.5206958.

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Paulíková, Helena, Dušan Podhradský, Marian Sabol e Andrea Tóthová. "Glutathione levels in K562 leukemia line". In VIth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 1999. http://dx.doi.org/10.1135/css199903044.

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Chang-Cheng Gao, Xian-Feng Zou, Qiong Wu, Xing Chen, Li-Hong Zhang e Li-Na Chen. "A novel micromolecule glutathione peroxidase mimic". In 2011 International Symposium on Information Technology in Medicine and Education (ITME 2011). IEEE, 2011. http://dx.doi.org/10.1109/itime.2011.6132096.

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Voskresenska, Natalja, Julija Voicehovska, Sergejs Babikovs, Vladimirs Voicehovskis, Aivars Lejnieks, Andrejs Skesters e Alise Silova. "Glutathione level in community-acquired pneumonia patients". In ERS International Congress 2017 abstracts. European Respiratory Society, 2017. http://dx.doi.org/10.1183/1393003.congress-2017.pa988.

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ARDUINI, F., F. RICCI, G. PALLESCHI, D. MOSCONE e A. AMINE. "MODIFIED SCREEN PRINTED ELECTRODES FOR GLUTATHIONE DETECTION". In Proceedings of the 9th Italian Conference. WORLD SCIENTIFIC, 2005. http://dx.doi.org/10.1142/9789812701770_0011.

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Yan, Haitao, e Weining Wang. "Terhertz time-domain spectroscopy of L-Glutathione". In Fourth International Conference on Photonics and Imaging in Biology and Medicine, a cura di Kexin Xu, Qingming Luo, Da Xing, Alexander V. Priezzhev e Valery V. Tuchin. SPIE, 2006. http://dx.doi.org/10.1117/12.710679.

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Rapporti di organizzazioni sul tema "Glutathione"

Woldegiorgis, S., R. C. Ahmed, Y. Zhen, C. A. Erdmann, M. L. Russell e R. Goth-Goldstein. Genetic polymorphism in three glutathione s-transferase genes and breast cancer risk. Office of Scientific and Technical Information (OSTI), aprile 2002. http://dx.doi.org/10.2172/799602.

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Shaw, Collin. Increased Glutathione Metabolic Defense Capabilities in Cultured Alzheimer's Diseased Lymphoblast Cell Lines. Portland State University Library, gennaio 2000. http://dx.doi.org/10.15760/etd.1702.

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Zilinskas, Barbara A., Doron Holland, Yuval Eshdat e Gozal Ben-Hayyim. Production of Stress Tolerant Plants by Overproduction of Enzymatic Oxyradical Scavengers. United States Department of Agriculture, maggio 1993. http://dx.doi.org/10.32747/1993.7568751.bard.

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Most of the objectives that were outlined in the original proposal have been met with two exceptions. Briefly, our goals were to: (1) constract transgenic tobacco plants which overproduce one or more of the enzymatic oxyradical scavengers and associated ancillary enzymes, including superoxide dismutase, ascorbate peroxidase, glutathione peroxidase, glutathione reductase, and monodehydrascorbate reductase; (2) evaluate the tolerance of these transgenic plants to oxidative stress; and (3) extend these studies to an agronomically important crop such as citrus. As can be seen i the following pages, our objectives (1) and (2) have been achieved, although transgenic lines overexpressing phospholipid hydroperoxidase glutathione peroxidase (PHGPX) were not obtained and our evidence to date suggests that constitutive overexpressing of the enzyme is probably lethal. Howeever, transgenic tobacco expressing the antisense construct for PHGPX were obtained. Tobacco plants overexpressing ascorbate peroxidase and those sensesuppressing monodehydroascorbate reductase are more tolerant to oxidative stress, as mediated by the redox-cycling agent paraquant; in contrast, plants expressing the PHGPX-antisense construct are more sensitive to paraquat. Additional research is warranted on each of the six types of transgenic lines which we generated with regard to their tolerance to saline stress. Until recently, attempts to transform citrus were not very successful, and thus additional attention is currently being directed at objective (3). We are optimistic that use of the plant transformation vector, pBIN, will lead to stable transgenic citrus, as preliminary experiments demonstrate stable expression of the GUS reporter gene. Other important contributions resulting from this BARD project include the biochemical characterization of the first plant phospholipid glutathione peroxidase and the biochemical and molecular analysis of another key antioxidant enzyme, monodehydroascorbate reductase. Overall this BARD-supported project was quite successful, and the biological resource of numerous transgenic lines which have altered levels of antioxidant enzymes should be valuable for years to come.

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Diamond, A. M., J. L. Murray, P. Dale, R. Tritz e D. J. Grdina. The effects of selenium on glutathione peroxidase activity and radioprotection in mammalian cells. Office of Scientific and Technical Information (OSTI), settembre 1995. http://dx.doi.org/10.2172/510356.

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Mauzy, Camilla A., Nathan H. Johnson, Jason J. Jacobsen, Adam G. Quade, Jeremiah N. Betz, Jeanette S. Frey, Amanda Hanes e David Kaziska. Correlation Between Iron and alpha and pi Glutathione-S-Transferase Levels in Humans. Fort Belvoir, VA: Defense Technical Information Center, settembre 2012. http://dx.doi.org/10.21236/ada580919.

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Anders, M. W. Biosynthesis, Physiological Disposition, and Biochemical Effects of Nephrotoxic Glutathione and Cysteine S-Conjugates. Fort Belvoir, VA: Defense Technical Information Center, aprile 1990. http://dx.doi.org/10.21236/ada221522.

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Amir, Rachel, David J. Oliver, Gad Galili e Jacline V. Shanks. The Role of Cysteine Partitioning into Glutathione and Methionine Synthesis During Normal and Stress Conditions. United States Department of Agriculture, gennaio 2013. http://dx.doi.org/10.32747/2013.7699850.bard.

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The objective of this research is to study the nature of the competition for cysteine (Cys), the first organic sulfur-containing compound, between its two main metabolites, glutathione (GSH) and methionine (Met). GSH plays a central role in protecting plants during various stresses, while Met, an essential amino acid, regulates essential processes and metabolites in plant cells through its metabolite S-adenosyl-Met. Our results, which are based on flux analysis and measurements of Met- metabolites, show that the flux towards Met synthesis is high during non-stress conditions, however the flux is significantly reduced under stress conditions, when there is high synthesis of GSH. Under oxidative stress the expression level of the regulatory enzyme of Met synthesis, cystathionine g-synthase (CGS) was reduced. By using three different systems, we have found that that GSH down regulates the expression level of CGS, thus reducing Met synthesis. We have found that this regulation occurs at the post-transcriptional level, and further studies have shown that it occurs at post-translationaly. To reveal how oxidative stress affects the flux towards Met and GSH, flux analysis was performed. We have found that the level of Met is significantly reduced, while the level of glutathione significantly increases during stress. Under stress conditions most of the glutathione is converted from GSH to GSSG (the oxidised form of glutathione). These results suggest that under normal growth conditions, Cys is channelled towards both pathways to support GSH accumulation and the synthesis of growth-essential Met metabolites. However, during oxidative stress, when a high level of GSH is required to protect the plants, the levels of GSH increase while those of CGS are reduced. This reduction leaves more Cys available for GSH synthesis under stress conditions. In addition we have also studied the effects of high GSH level on the transcriptome profile. The analysis revealed that GSH affects the expression level of many major genes coding to enzymes or proteins associated with photosynthesis, starch degradation, hormone metabolism (especially genes associated with jasmonate), biotic stress (especially genes associated with PR-proteins), cytochrome P450 genes, regulation of transcription and signaling (especially genes associated with receptor kinases and calcium). These results suggest that indeed GSH levels affect different pathways and metabolites in plants.

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Ross, Jeffrey S. Development of an Assay for Prostate Cancer Based on Methylation Status of Glutathione S-Transferase (p). Fort Belvoir, VA: Defense Technical Information Center, marzo 2001. http://dx.doi.org/10.21236/ada395450.

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Ross, Jeffrey S. Development of an Assay for Prostate Cancer Based on Methylation Status of Glutathione S-Transferase-pi. Fort Belvoir, VA: Defense Technical Information Center, marzo 2000. http://dx.doi.org/10.21236/ada392285.

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Haynes, Robin L., e Alan J. Townsend. Glutathione Transferases and the Multidrug Resistance - Associated Protein in Prevention of Potentially Carcinogenic Oxidant Stress in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, giugno 2001. http://dx.doi.org/10.21236/ada398035.

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