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

Author: Grafiati

Published: 4 June 2021

Last updated: 7 September 2023

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Loscalzo, J., and J. Freedman. "Purification and characterization of human platelet glutathione-S- transferase." Blood 67, no. 6 (1986): 1595–99. http://dx.doi.org/10.1182/blood.v67.6.1595.1595.

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Abstract A glutathione-S-transferase was isolated and purified to homogeneity from human platelets. With a combination of ammonium sulfate fractionation and chromatographic methods, 0.2 mg of pure enzyme was obtained from 9 X 10(11) platelets with a 12% recovery. The purified enzyme had a specific activity of 7.5 U per milligram, representing an approximately 1,100-fold purification. The enzyme was found to be anionic, with an isoelectric point of 4.6. With reduced glutathione as a co-substrate, platelet glutathione-S-transferase was most active with the synthetic substrate, 1-chloro-2,4-dinit

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12

Loscalzo, J., and J. Freedman. "Purification and characterization of human platelet glutathione-S- transferase." Blood 67, no. 6 (1986): 1595–99. http://dx.doi.org/10.1182/blood.v67.6.1595.bloodjournal6761595.

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A glutathione-S-transferase was isolated and purified to homogeneity from human platelets. With a combination of ammonium sulfate fractionation and chromatographic methods, 0.2 mg of pure enzyme was obtained from 9 X 10(11) platelets with a 12% recovery. The purified enzyme had a specific activity of 7.5 U per milligram, representing an approximately 1,100-fold purification. The enzyme was found to be anionic, with an isoelectric point of 4.6. With reduced glutathione as a co-substrate, platelet glutathione-S-transferase was most active with the synthetic substrate, 1-chloro-2,4-dinitrobenzene

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13

Awasthi, Sanjay, Utpal Pandya, Sharad S. Singhal, et al. "Curcumin–glutathione interactions and the role of human glutathione S-transferase P1-1." Chemico-Biological Interactions 128, no. 1 (2000): 19–38. http://dx.doi.org/10.1016/s0009-2797(00)00185-x.

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14

Schulte-Uebbing, C., L. Dibbelt, and E. Kuss. "Steroids as inhibitors of human placental glutathione-S-transferase." Placenta 7, no. 5 (1986): 476. http://dx.doi.org/10.1016/s0143-4004(86)80101-1.

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15

Mulder, Theo PJ, Daniel A. Court та Wilbert HM Peters. "Variability of Glutathione S-Transferase α in Human Liver and Plasma". Clinical Chemistry 45, № 3 (1999): 355–59. http://dx.doi.org/10.1093/clinchem/45.3.355.

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Abstract Background: Glutathione S-transferases are a family of enzymes involved in the binding, transport, and detoxification of a wide variety of endogenous and exogenous compounds. Little information is available about the variability of class α glutathione S-transferases in human liver, where they are highly expressed, or in serum. Methods: Both total class α glutathione S-transferase (GST-α, composed of GSTA1-1, GSTA1-2, and GSTA2-2) as well as GSTA1-1 concentrations were measured by specific and sensitive ELISA in liver cytosols of 35 organ donors and in plasma samples of 350 healthy con

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16

Oakley, Aaron J. "Proposed mechanism for monomethylarsonate reductase activity of human omega-class glutathione transferase GSTO1-1." Biochemical and Biophysical Research Communications 590 (January 2022): 7–13. http://dx.doi.org/10.1016/j.bbrc.2021.12.072.

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17

Zhou, Huina, Joseph Brock, Marco G. Casarotto, Aaron J. Oakley, and Philip G. Board. "Novel Folding and Stability Defects Cause a Deficiency of Human Glutathione Transferase Omega 1." Journal of Biological Chemistry 286, no. 6 (2010): 4271–79. http://dx.doi.org/10.1074/jbc.m110.197822.

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18

Duvoix, A., M. Schmitz, M. Schnekenburger, et al. "Transcriptional regulation of glutathione S-transferase P1-1 in human leukemia." BioFactors 17, no. 1-4 (2003): 131–38. http://dx.doi.org/10.1002/biof.5520170113.

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19

Board, P. G., and K. Pierce. "Expression of human glutathione S-transferase 2 in Escherichia coli. Immunological comparison with the basic glutathione S-transferases isoenzymes from human liver." Biochemical Journal 248, no. 3 (1987): 937–41. http://dx.doi.org/10.1042/bj2480937.

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A plasmid, termed pTacGST2, which contains the complete coding sequence of a GST2 (glutathione S-transferase 2) subunit and permits the expression of the protein in Escherichia coli was constructed. The expressed protein had the same subunit Mr as the enzyme from normal human liver and retained its catalytic function with both GST and glutathione peroxidase activity. Antiserum raised against the bacterially synthesized protein cross-reacted with all the basic GST isoenzymes in human liver. The electrophoretic mobility in agarose of the bacterially expressed isoenzyme suggested that its pI is i

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20

Cooke, R. J., R. Björnestedt, K. T. Douglas, et al. "Photoaffinity labelling of the active site of the rat glutathione transferases 3-3 and 1-1 and human glutathione transferase A1-1." Biochemical Journal 302, no. 2 (1994): 383–90. http://dx.doi.org/10.1042/bj3020383.

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The glutathione transferases (GSTs) form a group of enzymes responsible for a wide range of molecular detoxications. The photoaffinity label S-(2-nitro-4-azidophenyl)glutathione was used to study the hydrophobic region of the active site of the rat liver GST 1-1 and 2-2 isoenzymes (class Alpha) as well as the rat class-Mu GST 3-3. Photoaffinity labelling was carried out using a version of S-(2-nitro-4-azidophenyl)glutathione tritiated in the arylazido ring. The labelling occurred with higher levels of radioisotope incorporation for the Mu than the Alpha families. Taking rat GST 3-3, 1.18 (+/-

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21

Oakley, Aaron J. "Hidden Glutathione Transferases in the Human Genome." Biomolecules 13, no. 8 (2023): 1240. http://dx.doi.org/10.3390/biom13081240.

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With the development of accurate protein structure prediction algorithms, artificial intelligence (AI) has emerged as a powerful tool in the field of structural biology. AI-based algorithms have been used to analyze large amounts of protein sequence data including the human proteome, complementing experimental structure data found in resources such as the Protein Data Bank. The EBI AlphaFold Protein Structure Database (for example) contains over 230 million structures. In this study, these data have been analyzed to find all human proteins containing (or predicted to contain) the cytosolic glu

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22

Cacciatore, I., A. M. Caccuri, A. Cocco, et al. "Potent isozyme-selective inhibition of human glutathione S-transferase A1-1 by a novel glutathione S-conjugate." Amino Acids 29, no. 3 (2005): 255–61. http://dx.doi.org/10.1007/s00726-005-0232-7.

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23

TU, CHEN-PEI D., and BIAO QIAN. "Nucleotide sequence of the human liver glutathione S-transferase subunit 1 cDNA." Biochemical Society Transactions 15, no. 4 (1987): 734–36. http://dx.doi.org/10.1042/bst0150734.

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24

van Zanden, Jelmer J., Omar Ben Hamman, Marlou L. P. S. van Iersel, et al. "Inhibition of human glutathione S-transferase P1-1 by the flavonoid quercetin." Chemico-Biological Interactions 145, no. 2 (2003): 139–48. http://dx.doi.org/10.1016/s0009-2797(02)00250-8.

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25

Shishido, Yuko, Fumiaki Tomoike, Keiko Kuwata, et al. "A Covalent Inhibitor for Glutathione S ‐Transferase Pi (GSTP 1‐1 ) in Human Cells." ChemBioChem 20, no. 7 (2019): 900–905. http://dx.doi.org/10.1002/cbic.201800671.

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26

Cha, Sun Joo, Yeo Jeong Han, Hyun-Jun Choi, Hyung-Jun Kim, and Kiyoung Kim. "Glutathione S-Transferase Rescues Motor Neuronal Toxicity in Fly Model of Amyotrophic Lateral Sclerosis." Antioxidants 9, no. 7 (2020): 615. http://dx.doi.org/10.3390/antiox9070615.

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Transactive response DNA-binding protein-43 (TDP-43) is involved in the pathology of familial and sporadic amyotrophic lateral sclerosis (ALS). TDP-43-mediated ALS models in mice, Drosophila melanogaster, and zebrafish exhibit dysfunction of locomotor function, defective neuromuscular junctions, and motor neuron defects. There is currently no effective cure for ALS, and the underlying mechanisms of TDP-43 in ALS remain poorly understood. In this study, a genetic screen was performed to identify modifiers of human TDP-43 (hTDP-43) in a Drosophila model, and glutathione S-transferase omega 2 (Gs

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Saisawang, Chonticha, Jantana Wongsantichon, Robert C. Robinson, and Albert J. Ketterman. "Glutathione transferase Omega 1‐1 (GSTO1‐1) modulates Akt and MEK1/2 signaling in human neuroblastoma cell SH‐SY5Y." Proteins: Structure, Function, and Bioinformatics 87, no. 7 (2019): 588–95. http://dx.doi.org/10.1002/prot.25683.

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28

Tochio, Takumi, Yuki Ueno, Yasuyuki Kitaura, et al. "Feeding of 1-Kestose Induces Glutathione-S-Transferase Expression in Mouse Liver." Foods 8, no. 2 (2019): 69. http://dx.doi.org/10.3390/foods8020069.

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Functional food ingredients, including prebiotics, have been increasingly developed for human health. The improvement of the human intestinal environment is one of their main targets. Fructooligosaccarides (FOS) are oligosaccharide fructans that are well studied and commercialized prebiotics. 1-Kestose, one of the components of FOS, is considered to be a key prebiotic component in FOS. However, to our knowledge, no studies have been reported on the physiological efficacy of 1-Kestose regarding its anti-oxidative activity. In the present study, we examined the effects of dietary 1-Kestose on ge

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Ouwerkerk-Mahadevan, S., J. H. van Boom, M. C. Dreef-Tromp, J. H. T. M. Ploemen, D. J. Meyer, and G. J. Mulder. "Glutathione analogues as novel inhibitors of rat and human glutathione S-transferase isoenzymes, as well as of glutathione conjugation in isolated rat hepatocytes and in the rat in vivo." Biochemical Journal 308, no. 1 (1995): 283–90. http://dx.doi.org/10.1042/bj3080283.

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Inhibitors of rat and human Alpha- and Mu-class glutathione S-transferases that effectively inhibit the glutathione (GSH) conjugation of bromosulphophthalein in the rat liver cytosolic fraction, isolated rat hepatocytes and in the rat liver in vivo have been developed. The GSH analogue (R)-5-carboxy-2-gamma-(S)-glutamylamino-N-hexylpentamide [Adang, Brussee, van der Gen and Mulder (1991) J. Biol. Chem. 266, 830-836] was used as the lead compound. To obtain more potent inhibitors, it was modified by replacement of the N-hexyl moiety by N-2-heptyl and by esterification of the 5-carboxy group wit

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Board, P. G., T. Suzuki, and D. C. Shaw. "Human muscle glutathione S-transferase (GST-4) shows close homology to human liver GST-1." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 953 (January 1988): 214–17. http://dx.doi.org/10.1016/0167-4838(88)90027-1.

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31

Dalmizrak, O., G. Kulaksiz-Erkmen та N. Ozer. "Possible prenatal impact of sertraline on human placental glutathione S-transferase-π". Human & Experimental Toxicology 31, № 5 (2011): 457–64. http://dx.doi.org/10.1177/0960327111429585.

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Sertraline (SER), a tricyclic antidepressant, is considered to belong to the group of selective amine reuptake inhibitors. Its ability to cross the blood–brain barrier and transplacental transport has been reported previously. It is widely distributed in the brain and is bound to human glutathione S-transferase-π (GST-π). If SER is taken during pregnancy, it gets accumulated in the embryo and fetus, and some studies have suggested it may cause congenital malformations, thus the study of the interaction of GST-π with antidepressants is crucial. In this study, the interaction of human placental

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32

Younis, Islam R., Meenal Elliott, Cody J. Peer, et al. "Dehydroalanine Analog of Glutathione: An Electrophilic Busulfan Metabolite That Binds to Human Glutathione S-Transferase A1-1." Journal of Pharmacology and Experimental Therapeutics 327, no. 3 (2008): 770–76. http://dx.doi.org/10.1124/jpet.108.142208.

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33

McLellan, L. I., C. R. Wolf, and J. D. Hayes. "Human microsomal glutathione S-transferase. Its involvement in the conjugation of hexachlorobuta-1,3-diene with glutathione." Biochemical Journal 258, no. 1 (1989): 87–93. http://dx.doi.org/10.1042/bj2580087.

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A microsomal glutathione S-transferase (GST) was purified from human liver. This enzyme was shown to have characteristics similar to those of the rat microsomal GST described by Morgenstern & De Pierre [(1983) Eur. J. Biochem. 134, 591-597]. The specific activity of human microsomal GST towards 1-chloro-2,4-dinitrobenzene or cumene hydroperoxide can be stimulated by treating the enzyme with N-ethylmaleimide. This enhancement of activity is accompanied by increased sensitivity to inhibition by haematin and cholic acid. The subunit Mr values of the rat and human enzymes are similar (approx.

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34

Stockman, P. K., L. I. McLellan, and J. D. Hayes. "Characterization of the basic glutathione S-transferase B1 and B2 subunits from human liver." Biochemical Journal 244, no. 1 (1987): 55–61. http://dx.doi.org/10.1042/bj2440055.

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The basic glutathione S-transferases in human liver are composed of at least two immunochemically distinct polypeptides, designated B1 and B2. These subunits exist as homodimers, but can hybridize to form the B1B2 heterodimer [Stockman, Beckett & Hayes (1985) Biochem. J. 227, 457-465]. Although these basic glutathione S-transferases possess similar catalytic properties, the B2 subunit exhibits significantly greater selenium-independent glutathione peroxidase activity than subunit B1. The use of the ligands haematin, tributyltin acetate and Bromosulphophthalein as inhibitors of 1-chloro-2,4

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35

Juronen, Erkki, Gunnar Tasa, Mart Uusküla, Margus Pooga, and Aavo-Valdur Mikelsaar. "Purification, characterization and tissue distribution of human class theta glutathione s-transferase T1-1." IUBMB Life 39, no. 1 (1996): 21–29. http://dx.doi.org/10.1080/15216549600201021.

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Zhang, Yuesheng, Veronica Gonzalez, and Min Jian Xu. "Expression and regulation of glutathione S-transferase P1-1 in cultured human epidermal cells." Journal of Dermatological Science 30, no. 3 (2002): 205–14. http://dx.doi.org/10.1016/s0923-1811(02)00107-x.

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37

Liu, Xiyuan, Byoung Ha An, Min Jung Kim, Jong Hoon Park, Young Sook Kang та Minsun Chang. "Human glutathione S-transferase P1-1 functions as an estrogen receptor α signaling modulator". Biochemical and Biophysical Research Communications 452, № 3 (2014): 840–44. http://dx.doi.org/10.1016/j.bbrc.2014.09.017.

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Van Haaften, Rachel I. M., Chris T. A. Evelo, John Penders, Miguel P. F. Eijnwachter, Guido R. M. M. Haenen та Aalt Bast. "Inhibition of human glutathione S-transferase P1-1 by tocopherols and α-tocopherol derivatives". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1548, № 1 (2001): 23–28. http://dx.doi.org/10.1016/s0167-4838(01)00211-4.

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Wu, Y., Y. Fan, B. Xue, et al. "Human glutathione S-transferase P1-1 interacts with TRAF2 and regulates TRAF2–ASK1 signals." Oncogene 25, no. 42 (2006): 5787–800. http://dx.doi.org/10.1038/sj.onc.1209576.

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40

MAINWARING, Guy W., Sally M. WILLIAMS, John R. FOSTER, Jonathan TUGWOOD, and Trevor GREEN. "The distribution of theta-class glutathione S-transferases in the liver and lung of mouse, rat and human." Biochemical Journal 318, no. 1 (1996): 297–303. http://dx.doi.org/10.1042/bj3180297.

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Two murine Theta-class glutathione S-transferases (GSTs), mGSTT1 and mGSTT2, have been cloned and sequenced. The murine cDNAs, together with the published sequences of the rat and human enzymes, were used to design oligonucleotide probes in order to determine the distribution of mRNA for these enzymes in the liver and lung of rat, mouse and human. The mRNA distribution was compared with that of enzyme protein determined with an antibody to rat GSTT2–2. Both the antibody and the oligonucleotide probes gave the same distribution patterns. Both enzymes were present at significantly higher concent

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41

Xia, C., J. B. Taylor, S. R. Spencer, and B. Ketterer. "The human glutathione S-transferase P1-1 gene: modulation of expression by retinoic acid and insulin." Biochemical Journal 292, no. 3 (1993): 845–50. http://dx.doi.org/10.1042/bj2920845.

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Glutathione S-transferases (GSTs) are a group of enzymes which play an important role in the detoxication of xenobiotics. It is shown that the expression of human glutathione S-transferase P1-1 (GSTP1-1) is suppressed by retinoic acid (RA) as the result of decreased transcription from its gene, GSTP1. Chloramphenicol acetyltransferase (CAT) assays indicate that the effect of RA on the transcription of a GSTP1 promoter-CAT fusion gene is mediated by the region -99 to +72 of GSTP1. A consensus activator protein 1-binding site, located at nucleotide position -59 to -65 of GSTP1, is suggested to b

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42

Waterboer, Tim, Peter Sehr, Kristina M. Michael, et al. "Multiplex Human Papillomavirus Serology Based on In Situ–Purified Glutathione S-Transferase Fusion Proteins." Clinical Chemistry 51, no. 10 (2005): 1845–53. http://dx.doi.org/10.1373/clinchem.2005.052381.

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Abstract Background: More than 100 different human papillomaviruses (HPVs) can cause proliferative diseases, many of which are malignant, such as cervical cancer. HPV serology is complex because infection and disease lead to distinct type-specific antibody responses. Using bead-based technology, we have developed an assay platform that allows the simultaneous detection of antibodies against up to 100 in situ affinity–purified recombinant HPV proteins. Methods: Twenty-seven HPV proteins were expressed as glutathione S-transferase fusion proteins and affinity-purified in one step by incubation o

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ROUIMI, Patrick, Patricia ANGLADE, Anne BENZEKRI, et al. "Purification and characterization of a glutathione S-transferase Omega in pig: evidence for two distinct organ-specific transcripts." Biochemical Journal 358, no. 1 (2001): 257–62. http://dx.doi.org/10.1042/bj3580257.

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A cytosolic glutathione S-transferase (GST, EC 2.5.1.18) from the recently characterized Omega class [GSTO; Board et al. 2000, J. Biol. Chem. 275, 24798–24806] has been identified in pig organs. It was found widely distributed in the different tissues investigated and especially abundant in liver and muscle. The hepatic enzyme has been purified to homogeneity by using its selective affinity for S-hexylglutathione over GSH, thus providing a simple method to isolate mammalian GSTO. The dimeric protein has a subunit molecular mass of 27328Da as measured by electrospray ionization MS. Internal pep

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Li, Yang, Qi Zhang, Bo Peng, Qing Shao, Wei Qian, and Jian-Ying Zhang. "Identification of glutathione S-transferase omega 1 (GSTO1) protein as a novel tumor-associated antigen and its autoantibody in human esophageal squamous cell carcinoma." Tumor Biology 35, no. 11 (2014): 10871–77. http://dx.doi.org/10.1007/s13277-014-2394-y.

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Takamatsu, Y., and T. Inaba. "Inter-individual variability of human hepatic glutathione S-transferase isozymes assessed by inhibitory capacity." Toxicology 88, no. 1-3 (1994): 191–200. http://dx.doi.org/10.1016/0300-483x(94)90120-1.

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KOLOBE, Doris, Yasien SAYED, and Heini W. DIRR. "Characterization of bromosulphophthalein binding to human glutathione S-transferase A1-1: thermodynamics and inhibition kinetics." Biochemical Journal 382, no. 2 (2004): 703–9. http://dx.doi.org/10.1042/bj20040056.

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Abstract:

In addition to their catalytic functions, GSTs (glutathione S-transferases) bind a wide variety of structurally diverse non-substrate ligands. This ligandin function is known to result in the inhibition of catalytic function. The interaction between hGSTA1-1 (human class Alpha GST with two type 1 subunits) and a non-substrate anionic ligand, BSP (bromosulphophthalein), was studied by isothermal titration calorimetry and inhibition kinetics. The binding isotherm is biphasic, best described by a set of two independent sites: a high-affinity site and a low-affinity site(s). The binding stoichiome

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Klöne, A., R. Hussnätter, and H. Sies. "Cloning, sequencing and characterization of the human Alpha glutathione S-transferase gene corresponding to the cDNA clone pGTH2." Biochemical Journal 285, no. 3 (1992): 925–28. http://dx.doi.org/10.1042/bj2850925.

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Abstract:

The human Alpha glutathione S-transferase gene corresponding to the human liver cDNA clone pGTH2 was isolated from a cosmid genome library. The gene, represented by the clone cosGTH2, spans nearly 12 kb and contains seven exons. The intron/exon borders conform to the standard rules, and an open reading frame is present, starting at position 67 in exon 2, the double-stop codon being at position 733 in exon 7. Exons 1, 2 and 7 differ in length from the known rat gene coding for the Ya enzyme. A 209 bp 5′-upstream region contains TATA and CAT boxes and, in addition, motifs for Sp1-, NF1- and HNFI

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van Iersel, Marlou L. P. S., Jan-Peter H. T. M. Ploemen, Mario Lo Bello, Giorgio Federici та Peter J. van Bladeren. "Interactions of α, β-unsaturated aldehydes and ketones with human glutathione S-transferase P1-1". Chemico-Biological Interactions 108, № 1-2 (1997): 67–78. http://dx.doi.org/10.1016/s0009-2797(97)00096-3.

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Martos-Maldonado, Manuel C., Indalecio Quesada-Soriano, Federico García-Maroto, Antonio Vargas-Berenguel, and Luís García-Fuentes. "Ferrocene labelings as inhibitors and dual electrochemical sensors of human glutathione S-transferase P1-1." Bioorganic & Medicinal Chemistry Letters 22, no. 23 (2012): 7256–60. http://dx.doi.org/10.1016/j.bmcl.2012.09.022.

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Hussey, A. J., and J. D. Hayes. "Characterization of a human class-Theta glutathione S-transferase with activity towards 1-menaphthyl sulphate." Biochemical Journal 286, no. 3 (1992): 929–35. http://dx.doi.org/10.1042/bj2860929.

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Abstract:

A purification scheme is described for a glutathione S-transferase (GST) from human liver that catalyses the conjugation of 1-menaphthyl sulphate (MS) with GSH; the method devised results in an approx. 500-fold increase in specific activity towards MS. The human enzyme which metabolizes MS is a homodimer comprising subunits of M(r) 25,100, and immunochemical experiments have shown it to be a member of the class-Theta GSTs. Automated Edman degradation of this enzyme has confirmed that it is a Theta-class GST bu the amino acid sequence obtained differs from that of GST theta described previously

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