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Relevant bibliographies by topics / Human Glutathione S-Transferase Omega-1

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Academic literature on the topic 'Human Glutathione S-Transferase Omega-1'

Author: Grafiati

Published: 4 June 2021

Last updated: 7 September 2023

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Journal articles on the topic "Human Glutathione S-Transferase Omega-1"

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Sampayo-Reyes, Adriana, and Robert A. Zakharyan. "Tocopherol esters inhibit human glutathione S-transferase omega." Acta Biochimica Polonica 53, no. 3 (2006): 547–52. http://dx.doi.org/10.18388/abp.2006_3326.

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Human glutathione S-transferase omega 1-1 (hGSTO1-1) is a newly identified member of the glutathione S-transferase (GST) family of genes, which also contains alpha, mu, pi, sigma, theta, and zeta members. hGSTO1-1 catalyzes the reduction of arsenate, monomethylarsenate (MMA(V)), and dimethylarsenate (DMA(V)) and exhibits thioltransferase and dehydroascorbate reductase activities. Recent evidence has show that cytokine release inhibitory drugs, which specifically inhibit interleukin-1b (IL-1b), directly target hGSTO1-1. We found that (+)-alpha-tocopherol phosphate and (+)-alpha-tocopherol succi

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Peng, Xingyu, Jinfeng Zhu, Sicheng Liu, et al. "The Upregulation of GSTO2 is Associated with Colon Cancer Progression and a Poor Prognosis." Journal of Oncology 2023 (January 11, 2023): 1–21. http://dx.doi.org/10.1155/2023/4931650.

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Colorectal cancer is the second-leading cause of cancer-related mortality in the United States. Glutathione S-transferase can affect the development of cancer. Glutathione S-transferase omega 2, a member of the GST family, plays an important role in many tumors. However, the role of Glutathione S-transferase omega 2 in the development of colon cancer remains unclear. Herein, our study aimed to investigate the exact role of Glutathione S-transferase omega 2 in colon cancer. We used RNA sequencing data from The Cancer Genome Atlas and the Genotype-Tissue Expression database to analyze Glutathion

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Yin, Zhan-Li, Jane E. Dahlstrom, David G. Le Couteur, and Philip G. Board. "Immunohistochemistry of Omega Class Glutathione S-Transferase in Human Tissues." Journal of Histochemistry & Cytochemistry 49, no. 8 (2001): 983–87. http://dx.doi.org/10.1177/002215540104900806.

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Omega class glutathione transferase (GSTO) has been recently described in a number of mammalian species. We used immunohistochemistry to determine the cellular and tissue distribution of GSTO1–1 in humans. Expression of GSTO1–1 was abundant in a wide range of normal tissues, particularly liver, macrophages, glial cells, and endocrine cells. We also found nuclear staining in several types of cells, including glial cells, myoepithelial cells of the breast, neuroendocrine cells of colon, fetal myocytes, hepatocytes, biliary epithelium, ductal epithelium of the pancreas, Hoffbauer cells of the pla

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Garcerá, Ana, Lina Barreto, Lidia Piedrafita, Jordi Tamarit, and Enrique Herrero. "Saccharomyces cerevisiae cells have three Omega class glutathione S-transferases acting as 1-Cys thiol transferases." Biochemical Journal 398, no. 2 (2006): 187–96. http://dx.doi.org/10.1042/bj20060034.

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The Saccharomyces cerevisiae genome encodes three proteins that display similarities with human GSTOs (Omega class glutathione S-transferases) hGSTO1-1 and hGSTO2-2. The three yeast proteins have been named Gto1, Gto2 and Gto3, and their purified recombinant forms are active as thiol transferases (glutaredoxins) against HED (β-hydroxyethyl disulphide), as dehydroascorbate reductases and as dimethylarsinic acid reductases, while they are not active against the standard GST substrate CDNB (1-chloro-2,4-dinitrobenzene). Their glutaredoxin activity is also detectable in yeast cell extracts. The en

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Sampayo-Reyes, A., and R. A. Zakharyan. "Inhibition of human glutathione S-transferase omega by tocopherol succinate." Biomedicine & Pharmacotherapy 60, no. 5 (2006): 238–44. http://dx.doi.org/10.1016/j.biopha.2006.04.005.

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Gupta, Jeetendra Kumar. "Implications of Glutathione-S-transferases in Mitogen-activated protein kinase pathway: Risk associated with anticancer drug resistance." Research Journal of Chemistry and Environment 26, no. 12 (2022): 185–90. http://dx.doi.org/10.25303/2612rjce1850190.

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Anticancer drug resistance is a perilous glitch to accomplish alleviation of disease in patients with cancer. The setback of drug resistance in chemotherapy is a weighty snag of present time. Hassle of carcinoma has ability to develop resistance that arises due to certain alterations in drug targets. In the course of anticancer administrations, development of targeted therapies anticipates a new arena to subdue the drug resistance. Exalted levels of certain glutathione transferase isozymes have been identified with malign transformations as well as with anticancer drug resistance. Glutathione-

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Haaften, Rachel I. M. van, Guido R. M. M. Haenen, Chris T. A. Evelo, and Aalt Bast. "Tocotrienols Inhibit Human Glutathione S-Transferase P1-1." IUBMB Life (International Union of Biochemistry and Molecular Biology: Life) 54, no. 2 (2002): 81–84. http://dx.doi.org/10.1080/15216540214315.

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Hu, Su-Wei, Yen-Hao Su, Zhon-Min Huang, et al. "Association between human glutathione S-transferase omega rs4925 polymorphism and bladder cancer." Advances in Bioscience and Biotechnology 04, no. 01 (2013): 62–66. http://dx.doi.org/10.4236/abb.2013.41009.

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Huang, Zhon-Min, Jow-Yu Sheu, Min-Che Tung, Chia-Chang Wu, and Yuan-Hung Wang. "Association between human glutathione S-transferase omega rs4925 polymorphism and bladder cancer." Urological Science 26, no. 4 (2015): 298. http://dx.doi.org/10.1016/j.urols.2015.11.053.

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

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Nitroglycerin is a commonly employed pharmacological agent which produces vasodilatation by release of nitric oxide (NO.). The mechanism by which nitroglycerin releases NO. remains undefined. Recently, glutathione S-transferases have been implicated as important contributors to this process. They are known to release NO2- from nitroglycerin, but have not been shown to release NO.. The present studies were designed to examine the role of endogenous glutathione S-transferases in this metabolic process. Homogenates of dog carotid artery were incubated anaerobically with nitroglycerin, and NO. and

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Dissertations / Theses on the topic "Human Glutathione S-Transferase Omega-1"

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Eklund, Birgitta I. "Role of Multiple Glutathione Transferases in Bioactivation of Thiopurine Prodrugs : Studies of Human Soluble Glutathione Transferases from Alpha, Kappa, Mu, Omega, Pi, Theta, and Zeta Classes." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis : Universitetsbiblioteket [distributör], 2006. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-7102.

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Stewart, Richard K. "Detoxification of aflatoxin B¦1 in rabbit and human lung, role of glutathione s-transferases." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/nq22497.pdf.

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Johansson, Ann-Sofie. "Exploring the Functional Plasticity of Human Glutathione Transferases : Allelic Variants, Novel Isoenzyme and Enzyme Redesign." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis : Univ.-bibl. [distributör], 2002. http://publications.uu.se/theses/91-554-5270-1/.

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Viljanen, Johan. "A Novel Route for Construction of Multipurpose Receptors through Chemical Modification of Glutathione Transferases." Doctoral thesis, Linköpings universitet, Organisk Kemi, 2008. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-11612.

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This thesis describes how the human Alpha class glutathione transferase (GST) A1-1 can be reprogrammed either to function as a multipurpose biosensor for detection of small molecule analytes, or as a handle providing for more efficient protein purification. A novel, user-friendly, and efficient method for site-specific introduction of functional groups into the active site of hGST A1-1 is the platform for these achievements. The designed thioester reagents are glutathione-based and they are able to label one single nucleophile (Y9) and leave the other 50 nucleophiles (in hGST A1-1) intact. The

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Brock, Joseph Sydney. "A structural investigation of mechanism in human glutathione transferase omega 1." Phd thesis, 2011. http://hdl.handle.net/1885/151494.

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This thesis investigates the structural details of catalysis associated with the human enzyme, Glutathione Transferase Omega 1 (hGSTO1-1), a member of the most recently discovered class of Glutathione Transferase. The human genome contains two Omega class genes (hGSTO1 and 2) and their transcribed products have been found at varied levels within almost every tissue of the human body. The crystal structure of hGSTO1-1 displays a distinguishing cysteine residue in the active site, a feature that undoubtedly plays a role in the novel biochemistry it displays. Of most interest is the hGSTO1-1 medi

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Bhaskara, Ramachandra M. "Structure, Stability and Evolution of Multi-Domain Proteins." Thesis, 2013. http://etd.iisc.ac.in/handle/2005/3384.

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Analyses of protein sequences from diverse genomes have revealed the ubiquitous nature of multi-domain proteins. They form up to 70% of proteomes of most eukaryotic organisms. Yet, our understanding of protein structure, folding and evolution has been dominated by extensive studies on single-domain proteins. We provide quantitative treatment and proof for prevailing intuitive ideas on the strategies employed by nature to stabilize otherwise unstable domains. We find that domains incapable of independent stability are stabilized by favourable interactions with tethered domains in the multi-doma

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Bhaskara, Ramachandra M. "Structure, Stability and Evolution of Multi-Domain Proteins." Thesis, 2013. http://etd.iisc.ernet.in/2005/3384.

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Analyses of protein sequences from diverse genomes have revealed the ubiquitous nature of multi-domain proteins. They form up to 70% of proteomes of most eukaryotic organisms. Yet, our understanding of protein structure, folding and evolution has been dominated by extensive studies on single-domain proteins. We provide quantitative treatment and proof for prevailing intuitive ideas on the strategies employed by nature to stabilize otherwise unstable domains. We find that domains incapable of independent stability are stabilized by favourable interactions with tethered domains in the multi-doma

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Wallace, Louise Annette. "The unfolding and refolding of human glutathione transferase A1-1." Thesis, 1998. https://hdl.handle.net/10539/26456.

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A thesis submitted to the Faculty of Science, University of the Witwatersrand, Johannesburg, in fulfillment of the requirements for the degree of Doctor of Philosophy.<br>The thermodynamic stability and the properties of the unfolding/refolding pathways of homodimeric human glutathione transferase A1-1 (hGST A1-1) were investigated. The conformational stability, assessed by urea- and temperature-induced denaturation studies, was consistent with a folded dimer/unfolded monomer transition with no stable intermediates. The high energy of stabilisation and the highly co-operative transition

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Whitbread, Astrid Kristine. "Molecular genetics of the Omega class glutathione transferases in human and mouse." Phd thesis, 2003. http://hdl.handle.net/1885/148653.

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Little, Tessa. "Implications of N-capping motifs for folding and design of human glutathione transferase A1-1." Thesis, 2006. http://hdl.handle.net/10539/1804.

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Student Number : 9306227A - PhD thesis - School of Molecular and Cell Biology - Faculty of Science<br>It is well documented that N-capping motifs are stabilising local motifs for -helices. N-capping motifs have been identified within hGST A1-1 at the N-terminal ends of -helix 9 and helix 6. The conservational role of these two motifs in protein stability, folding and function was investigated. -Helix 9 is a unique structural feature to class Alpha GSTs that is important for its catalytic functioning. This amphipathic helix is highly dynamic, where upon ligand binding at the active-

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Book chapters on the topic "Human Glutathione S-Transferase Omega-1"

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Hsu, Ching-Hsiang, Kaw-Yan Chua, Shau-Ku Huang, I.-Ping Chiang, and Kue-Hsiung Hsieh. "Glutathione S-Transferase Induces Murine Dermatitis that Resembles Human Allergic Dermatitis." In Advances in Experimental Medicine and Biology. Springer US, 1996. http://dx.doi.org/10.1007/978-1-4615-5855-2_5.

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Watanabe, Minro. "Genetic Polymorphisms of Cytochromes P450 1A1 and 2E1 and of Glutathione S-Transferase Ml and Cancer Susceptibility in the Human." In Molecular and Applied Aspects of Oxidative Drug Metabolizing Enzymes. Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-4855-3_9.

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Lantum, Hoffman B. M., Philip G. Board, and M. W. Anders. "Inactivation of Polymorphic Variants of Human Glutathione Transferase Zeta (hGSTZ1-1) by Maleylacetone and Fumarylacetone." In Advances in Experimental Medicine and Biology. Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-0667-6_54.

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Monge, María Eugenia, Manuela R. Martinefski, Mariela Bollini, and Lucas B. Pontel. "UHPLC-HRMS-Based Analysis of S-Hydroxymethyl-Glutathione, GSH, and GSSG in Human Cells." In Methods in Molecular Biology. Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-3247-5_10.

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"Dynamic Docking Study of the Binding of 1-Chloro-2,4-Dinitrobenzene in the Putative Electrophile Binding Site of Naturally Occurring Human Glutathione S-Transferase pi Allelo-Polymorphic Proteins." In Biologically Active Natural Products. CRC Press, 1999. http://dx.doi.org/10.1201/9781420048650-19.

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A. Zubillaga, Rafael, Lucía Jiménez, Ponciano García-Gutiérrez, and Abraham Landa. "Development of New Drugs to Treat Taenia solium Cysticercosis: Targeting 26 kDa Glutathione Transferase." In Current State of the Art in Cysticercosis and Neurocysticercosis [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.97342.

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Taenia solium causes neurocysticercosis, a parasitic infection of the central nervous system in humans. The costs of management, treatment, and diagnosis of patients with neurocysticercosis are high, and some patients do not respond to the currently available treatments. Helminth cytosolic glutathione transferases (GSTs) are essential enzymes involved in the regulation of immune responses, transport, and detoxification. In T. solium, three cytosolic GSTs with molecular masses of 26.5 (Ts26GST), 25.5 (Ts25GST), and 24.3 kDa (TsMσGST), classified as mu-alpha, mu and sigma GST-classes, respectively, constitute the main detoxification system, and they may be immune targets for the development of vaccines and new anthelmintics. We performed a successful virtual screen, and identified I7, a novel selective inhibitor of Ts26GST that showed a non-competitive inhibition mechanism towards substrate glutathione with a Ki of 55.7 mM and mixed inhibition towards the electrophilic substrate 1-chloro-2,4-dinitrobenzene with a Ki of 8.64 mM. Docking simulation studies showed that I7 can bind to a site that is adjacent to the electrophilic site and the furthest from the glutathione site. This new inhibitor of Ts26GST will be used as a lead molecule to develop new effective and safe drugs against diseases caused by T. solium.

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Okwudiri Ihegboro, Godwin, and Chimaobi James Ononamadu. "Drug-Induced Hepatotoxicity." In Hepatotoxicity [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.103766.

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This chapter aims at discussing the consequential effects of drug-induced hepatotoxicity on man. The liver carries out drug detoxification among other roles, but sometimes, drug toxicity can occur caused by either medication overdose or imbalance drug metabolic reactions (Phase 1 & 2), resulting in the formation of reactive (toxic) metabolites (electrophilic compounds or free radicals) that binds covalently to hepatocytes, leading to liver injury/diseases like acute and chronic hepatitis, cholestasis, steatosis among others. Mitochondrial dysfunction, oxidative stress and lipid peroxidation are some of the mechanisms of liver injury. Furthermore, drug hepatotoxicity results in hepatocellular, gastroenterological, cholestatic as well as immunological disorders. The clinical manifestations of drug toxicity arise from the abnormalities observed in liver’s biochemical and molecular indicators. Our findings, revealed that in the event of liver injury, liver function indices like aspartate and alanine aminotransferases, ALP (alkaline phosphatase) and gamma glutamyl transferase (GGT) activities, intracellular calcium (Ca2+) and lipid peroxidation increases whereas indices of oxidative stress such as glutathione and its allies, catalase and superoxide dismutase activity deplete. At molecular level, the gene expression levels of Bcl-2 mRNA and microRNA genes (miR-122, 192 and 194) reduces while mitochondrial genes (MMP-2 and MMP-9) overexpresses. Since drug abuse is deleterious to human health, therefore, adherence to doctors’ prescription guidelines should be followed.

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Conference papers on the topic "Human Glutathione S-Transferase Omega-1"

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Sumiya, Ryusuke, Masayoshi Terayama, Teruki Hagiwara, et al. "Abstract 4716: Glutathione S transferase omega 2 (GSTO2) is a novel tumor suppressor gene of human lung squamous cell carcinoma." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-4716.

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Calvaresi, Matteo, Marco Stenta, Piero Altoè, et al. "Computational QM∕MM Study of the Reaction Mechanism of Human Glutathione S-Transferase A3-3." In COMPUTATIONAL METHODS IN SCIENCE AND ENGINEERING: Theory and Computation: Old Problems and New Challenges. Lectures Presented at the International Conference on Computational Methods in Science and Engineering 2007 (ICCMSE 2007): VOLUME 1. AIP, 2007. http://dx.doi.org/10.1063/1.2836181.

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Lecomte, M., and J. M. Boeynaems. "COVALENT BINDING OF CYCLOOXYGENASE AND LIPOXYGENASE PRODUCTS TO HUMAN PLATELET PROTEINS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643397.

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Several studies in acellular systems have shown a covalent binding of eicosanoids to proteins (1). We have therefore investigated whether eicosanoids bind covalently to proteins in intact platelets. After incubation of washed human platelets with 14C-arachidonic acid, ethanol precipitation followed by extractions, a small fraction of the radioactivity (0.3%) was tightly bound to the protein pellet. Four criteria suggest the covalent nature of this binding. The radioactivity remained bound after exhaustive extractions with solvents of various polarities, and was not removed by dialysis against

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Okuma, M., K. Kanaji, F. Ushikubi, and H. Uchino. "SUBCELLULAR LOCALIZATION OF HUMAN PLATELET LIPOXYGENASE ACTIVITY: COMPARISON BETWEEN NORMAL AND LIPOXYGENASE-DEFICIENT PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644871.

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Lipoxygenase activities were estimated in platelet subcellular fractions as well as in intact platelets obtained from normal subjects and patients with deficient platelet lipoxygenase activities (<mean - 2SD of normal activities). From a washed platelet suspension (intact platelets), subcellular fractions including 12,000 x g supernatant of sonicated platelets (F-I), 105,000 x g supernatant (cytosol, F-II) and sediment (microsomal fraction, F-III) of F-I were prepared by differential centrifugation at 4°C. The enzyme activity was studied by the determination of 12-hy-droxyeicosatetraenoic a

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