Sigma-class glutathione transferases

References

• Abraham, J. E., Harrington, P., Driver, K. E., Tyrer, J., Easton, D. F., Dunning, A. M., et al. (2009). Common polymorphisms in the prostaglandin pathway genes and their association with breast cancer susceptibility and survival. Clin Cancer Res 15:2181–2191.
   PubMed Web of Science ®Google Scholar
• Adler, V., Yin, Z., Fuchs, S. Y., Benezra, M., Rosario, L., Tew, K. D., et al. (1999). Regulation of JNK signaling by GSTp. EMBO J 18:1321–1334.
   PubMed Web of Science ®Google Scholar
• Agianian, B., Tucker, P. A., Schouten, A., Leonard, K., Bullard, B., Gros, P. (2003). Structure of a Drosophila sigma class glutathione S-transferase reveals a novel active site topography suited for lipid peroxidation products. J Mol Biol 326:151–165.
   PubMed Web of Science ®Google Scholar
• Alias, Z., Clark, A. G. (2007). Studies on the glutathione S-transferase proteome of adult Drosophila melanogaster: responsiveness to chemical challenge. Proteomics 7:3618–3628.
   PubMed Web of Science ®Google Scholar
• Allocati, N., Federici, L., Masulli, M., Di Ilio, C. (2009). Glutathione transferases in bacteria. FEBS J 276:58–75.
   PubMed Web of Science ®Google Scholar
• Angeli, V., Faveeuw, C., Roye, O., Fontaine, J., Teissier, E., Capron, A., Wolowczuk, I., et al. (2001). Role of the parasite-derived prostaglandin D2 in the inhibition of epidermal Langerhans cell migration during schistosomiasis infection. J Exp Med 193:1135–1147.
   PubMed Web of Science ®Google Scholar
• Angelucci, F., Baiocco, P., Brunori, M., Gourlay, L., Morea, V., Bellelli, A. (2005). Insights into the catalytic mechanism of glutathione S-transferase: the lesson from Schistosoma haematobium. Structure 13:1241–1246.
   PubMed Web of Science ®Google Scholar
• Aritake, K., Kado, Y., Inoue, T., Miyano, M., Urade, Y. (2006). Structural and functional characterization of HQL-79, an orally selective inhibitor of human hematopoietic prostaglandin D synthase. J Biol Chem 281:15277–15286.
   PubMed Web of Science ®Google Scholar
• Armstrong, R. N. (1997). Structure, catalytic mechanism, and evolution of the glutathione transferases. Chem Res Toxicol 10:2–18.
   PubMed Web of Science ®Google Scholar
• Beall, C., Fyrberg, C., Song, S., Fyrberg, E. (1992). Isolation of a Drosophila gene encoding glutathione S-transferase. Biochem Genet 30:515–527.
   PubMed Web of Science ®Google Scholar
• Bjornestedt, R., Stenberg, G., Widersten, M., Board, P. G., Sinning, I., Jones, T. A., et al. (1995). Functional significance of arginine 15 in the active site of human class alpha glutathione transferase A1-1. J Mol Biol 247:765–773.
   PubMed Web of Science ®Google Scholar
• Bochner, B. S., Charlesworth, E. N., Lichtenstein, L. M., Derse, C. P., Gillis, S., Dinarello, C. A., et al. (1990). Interleukin-1 is released at sites of human cutaneous allergic reactions. J Allergy Clin Immunol 86:830–839.
   PubMed Web of Science ®Google Scholar
• Buetler, T. M., Eaton, D. L. (1992). Glutathione S-transferases: amino acid sequence comparison, classification, and phylogenetic relationship. Environ Carcinogen Ecotoxicol Rev C 10:181–203.
   Web of Science ®Google Scholar
• Caccuri, A. M., Antonini, G., Board, P. G., Flanagan, J., Parker, M. W., Paolesse, R., et al. (2001). Human glutathione transferase T2-2 discloses some evolutionary strategies for optimization of the catalytic activity of glutathione transferases. J Biol Chem 276:5432–5437.
   PubMed Web of Science ®Google Scholar
• Cameron, A. D., Sinning, I., Lhermite, G., Olin, B., Board, P. G., Mannervik, B., et al. (1995). Structural-analysis of human alpha-class glutathione transferase a1-1 in the Apo-form and in complexes with ethacrynic-acid and its glutathione conjugate. Structure 3:717–727.
   PubMed Web of Science ®Google Scholar
• Capper, E. A., Roshak, A. K., Bolognese, B. J., Podolin, P. L., Smith, T., Dewitt, D. L., et al. (2000). Modulation of human monocyte activities by tranilast, SB 252218, a compound demonstrating efficacy in restenosis. J Pharmacol Exp Ther 295:1061–1069.
   PubMed Web of Science ®Google Scholar
• Carletti, E., De Luca, A., Urbani, A., Sacchetta, P., Di Ilio, C. (2003). Sigma-class glutathione transferase from Xenopus laevis: molecular cloning, expression, and site-directed mutagenesis. Arch Biochem Biophys 419:214–221.
   PubMed Web of Science ®Google Scholar
• Carron, C. P., Trujillo, J. I., Olson, K. L., Huang, W., Hamper, B. C., Dice, T., et al. (2010). Discovery of an oral potent selective inhibitor of hematopoietic prostaglandin D synthase (HPGDS). ACS Med Chem Lett 1:59–63.
   PubMed Web of Science ®Google Scholar
• Catala, A. (2009). Lipid peroxidation of membrane phospholipids generates hydroxy-alkenals and oxidized phospholipids active in physiological and/or pathological conditions. Chem Phys Lipids 157:1–11.
   PubMed Web of Science ®Google Scholar
• Charlesworth, E. N., Kagey-Sobotka, A., Schleimer, R. P., Norman, P. S., Lichtenstein, L. M. (1991). Prednisone inhibits the appearance of inflammatory mediators and the influx of eosinophils and basophils associated with the cutaneous late-phase response to allergen. J Immunol 146:671–676.
   PubMed Web of Science ®Google Scholar
• Chelvanayagam, G., Parker, M. W., Board, P. G. (2001). Fly fishing for GSTs: a unified nomenclature for mammalian and insect glutathione transferases. Chemico-Biol Interact 133:256–260.
   Web of Science ®Google Scholar
• Chelvanayagam, G., Wilce, M. C., Parker, M. W., Tan, K. L., Board, P. G. (1997). Homology model for the human GSTT2 theta class glutathione transferase. Proteins 27:118–130.
   PubMed Web of Science ®Google Scholar
• Chemale, G., Morphew, R., Moxon, J. V., Morassuti, A. L., Lacourse, E. J., Barrett, J., et al. (2006). Proteomic analysis of glutathione transferases from the liver fluke parasite, Fasciola hepatica. Proteomics 6:6263–6273.
   PubMed Web of Science ®Google Scholar
• Chevalier, E., Stock, J., Fisher, T., Dupont, M., Fric, M., Fargeau, H., et al. (2005). Cutting edge: chemoattractant receptor-homologous molecule expressed on Th2 cells plays a restricting role on IL-5 production and eosinophil recruitment. J Immunol 175:2056–2060.
   PubMed Web of Science ®Google Scholar
• Chiou, S. H., Yu, C. W., Lin, C. W., Pan, F. M., Lu, S. F., Lee, H. J., et al. (1995). Octopus S-crystallins with endogenous glutathione S-transferase (GST) activity: sequence comparison and evolutionary relationships with authentic GST enzymes. Biochem J 309:793–800.
   PubMed Web of Science ®Google Scholar
• Cho, S. G., Lee, Y. H., Park, H. S., Ryoo, K., Kang, K. W., Park, J., et al. (2001). Glutathione S-transferase mu modulates the stress-activated signals by suppressing apoptosis signal-regulating kinase 1. J Biol Chem 276:12749–12755.
   PubMed Web of Science ®Google Scholar
• Christ-Hazelhof, E., Nugteren, D. H. (1979). Purification and characterisation of prostaglandin endoperoxide D-isomerase, a cytoplasmic, glutathione-requiring enzyme. Biochim Biophys Acta 572:43–51.
   PubMed Web of Science ®Google Scholar
• Christ-Hazelhof, E., Nugteren, D. H., Van Dorp, D. A. (1976). Conversions of prostaglandin endoperoxides by glutathione-S-transferases and serum albumins. Biochim Biophys Acta 450:450–461.
   PubMed Web of Science ®Google Scholar
• Christ, A. N., Labzin, L., Bourne, G. T., Fukunishi, H., Weber, J. E., Sweet, M. J., et al. (2010). Development and characterization of new inhibitors of the human and mouse hematopoietic prostaglandin D(2) synthases. J Med Chem 53:5536–5548.
   PubMed Web of Science ®Google Scholar
• Clayton, J. D., Cripps, R. M., Sparrow, J. C., Bullard, B. (1998). Interaction of troponin-H and glutathione S-transferase-2 in the indirect flight muscles of Drosophila melanogaster. J Muscle Res Cell Motil 19:117–127.
   PubMed Web of Science ®Google Scholar
• Corona, M., Robinson, G. E. (2006). Genes of the antioxidant system of the honey bee: annotation and phylogeny. Insect Mol Biol 15:687–701.
   PubMed Web of Science ®Google Scholar
• Ding, Y., Ortelli, F., Rossiter, L. C., Hemingway, J., Ranson, H. (2003). The Anopheles gambiae glutathione transferase supergene family: annotation, phylogeny, and expression profiles. BMC Genomics 4:35.
   PubMed Web of Science ®Google Scholar
• Dixon DP, Lapthorn A and Edwards R. (2002). Plant glutathione transferases. Genome Biol: 3:REVIEWS3004.
   Google Scholar
• Dowling, D. J., Hamilton, C. M., Donnelly, S., La Course, J., Brophy, P. M., Dalton, J., et al. (2010). Major secretory antigens of the helminth Fasciola hepatica activate a suppressive dendritic cell phenotype that attenuates Th17 cells but fails to activate Th2 immune responses. Infect Immun 78:793–801.
   PubMed Web of Science ®Google Scholar
• Duchen, L. W., Eicher, E. M., Jacobs, J. M., Scaravilli, F., Teixeira, F. (1980). Hereditary leucodystrophy in the mouse: the new mutant twitcher. Brain 103:695–710.
   PubMed Web of Science ®Google Scholar
• Eguchi, N., Minami, T., Shirafuji, N., Kanaoka, Y., Tanaka, T., Nagata, A., et al. (1999). Lack of tactile pain (allodynia) in lipocalin-type prostaglandin D synthase-deficient mice. Proc Natl Acad Sci U S A 96:726–730.
   PubMed Web of Science ®Google Scholar
• Fernandez-Funez, P., Nino-Rosales, M. L., de Gouyon, B., She, W. C., Luchak, J. M., Martinez, P., et al. (2000). Identification of genes that modify ataxin-1-induced neurodegeneration. Nature 408:101–106.
   PubMed Web of Science ®Google Scholar
• Flanagan, J. U., Rossjohn, J., Parker, M. W., Board, P. G., Chelvanayagam, G. (1999). Mutagenic analysis of conserved arginine residues in and around the novel sulfate binding pocket of the human theta class glutathione transferase T2-2. Prot Sci 8:2205–2212.
   PubMed Web of Science ®Google Scholar
• Fournier, D., Bride, J. M., Poirie, M., Berge, J. B., Plapp, F. W. Jr. (1992). Insect glutathione S-transferases. Biochemical characteristics of the major forms from houseflies susceptible and resistant to insecticides. J Biol Chem 267:1840–1845.
   Google Scholar
• Franciosa, H., Berge, J. B. (1995). Glutathione S-transferases in housefly (Musca domestica): location of GST-1 and GST-2 families. Insect Biochem Mol Biol 25:311–317.
   PubMed Web of Science ®Google Scholar
• Fujimori, K., Kanaoka, Y., Sakaguchi, Y., Urade, Y. (2000). Transcriptional activation of the human hematopoietic prostaglandin D synthase gene in megakaryoblastic cells. Roles of the oct-1 element in the 5′-flanking region and the AP-2 element in the untranslated exon 1. J Biol Chem 275:40511–40516.
   PubMed Web of Science ®Google Scholar
• Fujitani, Y., Kanaoka, Y., Aritake, K., Uodome, N., Okazaki-Hatake, K., Urade, Y. (2002). Pronounced eosinophilic lung inflammation and Th2 cytokine release in human lipocalin-type prostaglandin D synthase transgenic mice. J Immunol 168:443–449.
   PubMed Web of Science ®Google Scholar
• Gao, W., Schmidtko, A., Lu, R., Brenneis, C., Angioni, C., Schmidt, R., et al. (2009a). Prostaglandin D(2) sustains the pyrogenic effect of prostaglandin E(2). Eur J Pharmacol 608:28–31.
   PubMed Web of Science ®Google Scholar
• Gao, W., Schmidtko, A., Wobst, I., Lu, R., Angioni, C., Geisslinger, G. (2009b). Prostaglandin D2 produced by hematopoietic prostaglandin D synthase contributes to LPS-induced fever. J Physiol Pharmacol 60:145–150.
   PubMed Web of Science ®Google Scholar
• Gildenhuys, S., Dobreva, M., Kinsley, N., Sayed, Y., Burke, J., Pelly, S., et al. (2010). Arginine 15 stabilizes an SNAr reaction transition state and the binding of anionic ligands at the active site of human glutathione transferase A1-1. Biophys Chem 146:118–125.
   PubMed Web of Science ®Google Scholar
• Gilroy, D. W., Colville-Nash, P. R., Willis, D., Chivers, J., Paul-Clark, M. J., Willoughby, D. A. (1999). Inducible cyclooxygenase may have anti-inflammatory properties. Nat Med 5:698–701.
   PubMed Web of Science ®Google Scholar
• Harris, J., Coles, B., Meyer, D. J., Ketterer, B. (1991). The isolation and characterization of the major glutathione S-transferase from the squid Loligo vulgaris. Comp Biochem Physiol B 98:511–515.
   PubMed Web of Science ®Google Scholar
• Hebert, H., Jegerschold, C. (2007). The structure of membrane associated proteins in eicosanoid and glutathione metabolism as determined by electron crystallography. Curr Opin Struct Biol 17:396–404.
   PubMed Web of Science ®Google Scholar
• Herve, M., Angeli, V., Pinzar, E., Wintjens, R., Faveeuw, C., Narumiya, S., et al. (2003). Pivotal roles of the parasite PGD2 synthase and of the host D prostanoid receptor 1 in schistosome immune evasion. Eur J Immunol 33:2764–2772.
   PubMed Web of Science ®Google Scholar
• Herve, C., de Franco, P. O., Groisillier, A., Tonon, T., Boyen, C. (2008). New members of the glutathione transferase family discovered in red and brown algae. Biochem J 412:535–544.
   PubMed Web of Science ®Google Scholar
• Hesterkamp, T., Barker, J., Davenport, A., Whittaker, M. (2007). Fragment based drug discovery using fluorescence correlation: spectroscopy techniques: challenges and solutions. Curr Top Med Chem 7:1582–1591.
   PubMed Web of Science ®Google Scholar
• Hohwy, M., Spadola, L., Lundquist, B., Hawtin, P., Dahmen, J., Groth-Clausen, I., et al. (2008). Novel prostaglandin D synthase inhibitors generated by fragment-based drug design. J Med Chem 51:2178–2186.
   PubMed Web of Science ®Google Scholar
• Hong, S. J., Kang, S. Y., Chung, Y. B., Chung, M. H., Oh, Y. J., Kang, I., et al. (2000). Paragonimus westermani: a cytosolic glutathione S-transferase of a sigma-class in adult stage. Exp Parasitol 94:180–189.
   PubMed Web of Science ®Google Scholar
• Huang, Y., Krell, P. J., Ladd, T., Feng, Q., Zheng, S. (2009). Cloning, characterization, and expression of two glutathione S-transferase cDNAs in the spruce budworm, Choristoneura fumiferana. Arch Insect Biochem Physiol 70:44–56.
   PubMed Web of Science ®Google Scholar
• Huang, Z. L., Urade, Y., Hayaishi, O. (2007). Prostaglandins and adenosine in the regulation of sleep and wakefulness. Curr Opin Pharmacol 7:33–38.
   PubMed Web of Science ®Google Scholar
• Ikai, K., Ujihara, M., Fujii, K., Urade, Y. (1989). Inhibitory effect of tranilast on prostaglandin D synthetase. Biochem Pharmacol 38:2673–2676.
   PubMed Web of Science ®Google Scholar
• Inoue, T., Irikura, D., Okazaki, N., Kinugasa, S., Matsumura, H., Uodome, N., et al. (2003). Mechanism of metal activation of human hematopoietic prostaglandin D synthase. Nat Struct Biol 10:291–296.
   PubMedGoogle Scholar
• Ito, S., Narumiya, S., Hayaishi, O. (1989). Prostaglandin D2: a biochemical perspective. Prostaglandins Leukot Essent Fatty Acids 37:219–234.
   PubMed Web of Science ®Google Scholar
• Ji, X., von Rosenvinge, E. C., Johnson, W. W., Armstrong, R. N., Gilliland, G. L. (1996). Location of a potential transport binding site in a sigma class glutathione transferase by X-ray crystallography. Proc Natl Acad Sci U S A 93:8208–8213.
   PubMed Web of Science ®Google Scholar
• Ji, X., von Rosenvinge, E. C., Johnson, W. W., Tomarev, S. I., Piatigorsky, J., Armstrong, R. N., et al. (1995). Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods. Biochemistry 34:5317–5328.
   PubMed Web of Science ®Google Scholar
• Joachim, A., Ruttkowski, B. (2008). Cytosolic glutathione S-transferases of Oesophagostomum dentatum. Parasitology 135:1215–1223.
   PubMed Web of Science ®Google Scholar
• Johnson, KA, Angelucci, F, Bellelli, A, Herve, M, Fontaine, J, Tsernoglou, D, et al. (2003). Crystal structure of the 28 kDa glutathione S-transferase from Schistosoma haematobium. Biochemistry 42:10084–10094.
   PubMed Web of Science ®Google Scholar
• Johnson, W. W., Liu, S. X., Ji, X. H., Gilliland, G. L., Armstrong, R. N. (1993). Tyrosine-115 participates both in chemical and physical steps of the catalytic mechanism of a glutathione-S-transferase. J Biol Chem 268:11508–11511.
   PubMed Web of Science ®Google Scholar
• Johnston, S. L., Bardin, P. G., Harrison, J., Ritter, W., Joubert, J. R., Holgate, S. T. (1992). The effects of an oral thromboxane TP receptor antagonist BAY u 3405, on prostaglandin D2- and histamine-induced bronchoconstriction in asthma, and relationship to plasma drug concentrations. Br J Clin Pharmacol 34:402–408.
   PubMed Web of Science ®Google Scholar
• Jones, R. L., Giembycz, M. A., Woodward, D. F. (2009). Prostanoid receptor antagonists: development strategies and therapeutic applications. Br J Pharmacol 158:104–145.
   PubMed Web of Science ®Google Scholar
• Joo, M., Kwon, M., Cho, Y. J., Hu, N., Pedchenko, T. V., Sadikot, R. T., et al. (2009). Lipopolysaccharide-dependent interaction between PU.1 and c-Jun determines production of lipocalin-type prostaglandin D synthase and prostaglandin D2 in macrophages. Am J Physiol Lung Cell Mol Physiol 296:L771–L779.
   PubMedGoogle Scholar
• Jowsey, IR, Thomson, AM, Flanagan, JU, Murdock, PR, Moore, GB, Meyer, DJ, et al. (2001). Mammalian class sigma glutathione S-transferases: catalytic properties and tissue-specific expression of human and rat GSH-dependent prostaglandin D2 synthases. Biochem J 359:507–516.
   PubMed Web of Science ®Google Scholar
• Jowsey, I. R., Murdock, P. R., Moore, G. B., Murphy, G. J., Smith, S. A., Hayes, JD. (2003). Prostaglandin D2 synthase enzymes and PPARgamma are co-expressed in mouse 3T3-L1 adipocytes and human tissues. Prostaglandins Other Lipid Mediat 70:267–284.
   PubMed Web of Science ®Google Scholar
• Kanaoka, Y., Ago, H., Inagaki, E., Nanayama, T., Miyano, M., Kikuno, R., et al. (1997). Cloning and crystal structure of hematopoietic prostaglandin D synthase. Cell 90:1085–1095; erratum in: 96:449.
   PubMed Web of Science ®Google Scholar
• Kanaoka, Y., Ago, H., Inagaki, E., Nanayama, T., Miyano, M., Kikuno, R., et al. (1999). Cloning and crystal structure of hematopoietic prostaglandin D synthase (vol 90, pp. 1085, 1997). Cell 96:U25–U25.
   Google Scholar
• Kanaoka, Y., Fujimori, K., Kikuno, R., Sakaguchi, Y., Urade, Y., Hayaishi, O. (2000). Structure and chromosomal localization of human and mouse genes for hematopoietic prostaglandin D synthase. Conservation of the ancestral genomic structure of sigma-class glutathione S-transferase. Eur J Biochem 267:3315–3322.
   PubMedGoogle Scholar
• Kanaoka, Y., Urade, Y. (2003). Hematopoietic prostaglandin D synthase. Prostaglandins Leukot Essent Fatty Acids 69:163–167.
   PubMed Web of Science ®Google Scholar
• Krause, S., Sommer, A., Fischer, P., Brophy, P. M., Walter, R. D., Liebau, E. (2001). Gene structure of the extracellular glutathione S-transferase from Onchocerca volvulus and its overexpression and promoter analysis in transgenic Caenorhabditis elegans. Mol Biochem Parasitol 117:145–154.
   PubMed Web of Science ®Google Scholar
• LaCourse, E. J., Hernandez-Viadel, M., Jefferies, J. R., Svendsen, C., Spurgeon, D. J., Barrett, J., et al. (2009). Glutathione transferase (GST) as a candidate molecular-based biomarker for soil toxin exposure in the earthworm Lumbricus rubellus. Environ Pollut 157:2459–2469.
   PubMed Web of Science ®Google Scholar
• Ladner, J. E., Parsons, J. F., Rife, C. L., Gilliland, G. L., Armstrong, R. N. (2004). Parallel evolutionary pathways for glutathione transferases: structure and mechanism of the mitochondrial class kappa enzyme rGSTK1-1. Biochemistry 43:352–361.
   PubMed Web of Science ®Google Scholar
• Lee, Y. M., Lee, K. W., Park, H., Park, H. G., Raisuddin, S., Ahn, I. Y., et al. (2007). Sequence, biochemical characteristics and expression of a novel sigma-class of glutathione S-transferase from the intertidal copepod, Tigriopus japonicus, with a possible role in antioxidant defense. Chemosphere 69:893–902.
   PubMed Web of Science ®Google Scholar
• Li, L., Yang, Y., Stevens, R. L. (2003). RasGRP4 regulates the expression of prostaglandin D2 in human and rat mast cell lines. J Biol Chem 278:4725–4729.
   PubMed Web of Science ®Google Scholar
• Li, X., Schuler, M. A., Berenbaum, M. R. (2007). Molecular mechanisms of metabolic resistance to synthetic and natural xenobiotics. Annu Rev Entomol 52:231–253.
   PubMed Web of Science ®Google Scholar
• Li, X., Zhang, X., Zhang, J., Zhang, X., Starkey, S. R., Zhu, K. Y. (2009). Identification and characterization of eleven glutathione S-transferase genes from the aquatic midge Chironomus tentans (Diptera: Chironomidae). Insect Biochem Mol Biol 39:745–754.
   PubMed Web of Science ®Google Scholar
• Liebau, E., Eckelt, V. H., Wildenburg, G., Teesdale-Spittle, P., Brophy, P. M., Walter, R. D., et al. (1997). Structural and functional analysis of a glutathione S-transferase from Ascaris suum. Biochem J 324:659–666.
   PubMed Web of Science ®Google Scholar
• Liebau, E., Schonberger, O. L., Walter, R. D., Henkle-Duhrsen, K. J. (1994a). Molecular cloning and expression of a cDNA encoding glutathione S-transferase from Ascaris suum. Mol Biochem Parasitol 63:167–170.
   PubMed Web of Science ®Google Scholar
• Liebau, E., Walter, R. D., Henkle-Duhrsen, K. (1994b). Isolation, sequence, and expression of an Onchocerca volvulus glutathione S-transferase cDNA. Mol Biochem Parasitol 63:305–309.
   PubMed Web of Science ®Google Scholar
• Liebau, E., Wildenburg, G., Walter, R. D., Henkle-Duhrsen, K. (1994c). A novel type of glutathione S-transferase in Onchocerca volvulus. Infect Immun 62:4762–4767.
   PubMed Web of Science ®Google Scholar
• Littler, D. R., Harrop, S. J., Goodchild, S. C., Phang, J. M., Mynott, A. V., Jiang, L., et al. (2010). The enigma of the CLIC proteins: ion channels, redox proteins, enzymes, scaffolding proteins? FEBS Lett 584:2093–2101.
   PubMed Web of Science ®Google Scholar
• Liu, D., Hewawasam, R., Pace, S. M., Gallant, E. M., Casarotto, M. G., Dulhunty, A. F., et al. (2009a). Dissection of the inhibition of cardiac ryanodine receptors by human glutathione transferase GSTM2-2. Biochem Pharmacol 77:1181–1193.
   PubMed Web of Science ®Google Scholar
• Liu, J., Fu, Z., Wang, Y., Schmitt, M., Huang, A., Marshall, D., et al. (2009b). Discovery and optimization of CRTH2 and DP dual antagonists. Bioorg Med Chem Lett 19:6419–6423.
   PubMed Web of Science ®Google Scholar
• Mahajan, S., Atkins, W. M. (2005). The chemistry and biology of inhibitors and pro-drugs targeted to glutathione S-transferases. Cell Mol Life Sci 62:1221–1233.
   PubMed Web of Science ®Google Scholar
• Mahmud, I., Ueda, N., Yamaguchi, H., Yamashita, R., Yamamoto, S., Kanaoka, Y., et al. (1997). Prostaglandin D synthase in human megakaryoblastic cells. J Biol Chem 272:28263–28266.
   PubMed Web of Science ®Google Scholar
• Manevich, Y., Feinstein, S. I., Fisher, A. B. (2004). Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST. Proc Natl Acad Sci U S A 101:3780–3785.
   PubMed Web of Science ®Google Scholar
• Martin, J. L. (1995). Thioredoxin—a fold for all reasons. Structure 3:245–250.
   PubMed Web of Science ®Google Scholar
• Matsuoka, T., Hirata, M., Tanaka, H., Takahashi, Y., Murata, T., Kabashima, K., et al. (2000). Prostaglandin D2 as a mediator of allergic asthma. Science 287:2013–2017.
   PubMed Web of Science ®Google Scholar
• Matsushita, N., Aritake, K., Takada, A., Hizue, M., Hayashi, K., Mitsui, K., et al. (1998a). Pharmacological studies on the novel antiallergic drug HQL-79: II. Elucidation of mechanisms for antiallergic and antiasthmatic effects. Jpn J Pharmacol 78:11–22.
   PubMedGoogle Scholar
• Matsushita, N., Hizue, M., Aritake, K., Hayashi, K., Takada, A., Mitsui, K., et al. (1998b). Pharmacological studies on the novel antiallergic drug HQL-79: I. Antiallergic and antiasthmatic effects in various experimental models. Jpn J Pharmacol 78:1–10.
   PubMedGoogle Scholar
• McIlwain, C. C., Townsend, D. M., Tew, K. D. (2006). Glutathione S-transferase polymorphisms: cancer incidence and therapy. Oncogene 25:1639–1648.
   PubMed Web of Science ®Google Scholar
• Meyer, D. J., Muimo, R., Thomas, M., Coates, D., Isaac, R. E. (1996). Purification and characterization of prostaglandin-H E-isomerase, a sigma-class glutathione S-transferase, from Ascaridia galli. Biochem J 313:223–227.
   PubMed Web of Science ®Google Scholar
• Meyer, D. J., Thomas, M. (1995). Characterization of rat spleen prostaglandin H D-isomerase as a sigma-class GSH transferase. Biochem J 311:739–742.
   PubMed Web of Science ®Google Scholar
• Minami, T., Okuda-Ashitaka, E., Nishizawa, M., Mori, H., Ito, S. (1997). Inhibition of nociceptin-induced allodynia in conscious mice by prostaglandin D2. Br J Pharmacol 122:605–610.
   PubMed Web of Science ®Google Scholar
• Mohri, I., Aritake, K., Taniguchi, H., Sato, Y., Kamauchi, S., Nagata, N., et al. (2009). Inhibition of prostaglandin D synthase suppresses muscular necrosis. Am J Pathol 174:1735–1744.
   PubMed Web of Science ®Google Scholar
• Mohri, I., Eguchi, N., Suzuki, K., Urade, Y., Taniike, M. (2003). Hematopoietic prostaglandin D synthase is expressed in microglia in the developing postnatal mouse brain. Glia 42:263–274.
   PubMed Web of Science ®Google Scholar
• Mohri, I., Kadoyama, K., Kanekiyo, T., Sato, Y., Kagitani-Shimono, K., Saito, Y., et al. (2007). Hematopoietic prostaglandin D synthase and DP1 receptor are selectively upregulated in microglia and astrocytes within senile plaques from human patients and in a mouse model of Alzheimer disease. J Neuropathol Exp Neurol 66:469–480.
   PubMed Web of Science ®Google Scholar
• Mohri, I., Taniike, M., Taniguchi, H., Kanekiyo, T., Aritake, K., Inui, T., et al. (2006). Prostaglandin D2-mediated microglia/astrocyte interaction enhances astrogliosis and demyelination in twitcher. J Neurosci 26:4383–4393.
   PubMed Web of Science ®Google Scholar
• Morii, E., Oboki, K. (2004). MITF is necessary for generation of prostaglandin D2 in mouse mast cells. J Biol Chem 279:48923–48929.
   PubMed Web of Science ®Google Scholar
• Murakami, M., Matsumoto, R., Urade, Y., Austen, K. F., Arm, J. P. (1995). c-kit ligand mediates increased expression of cytosolic phospholipase A2, prostaglandin endoperoxide synthase-1, and hematopoietic prostaglandin D2 synthase and increased IgE-dependent prostaglandin D2 generation in immature mouse mast cells. J Biol Chem 270:3239–3246.
   PubMed Web of Science ®Google Scholar
• Murray, J. J., Tonnel, A. B., Brash, A. R., Roberts, L. J. 2nd, Gosset, P., Workman, R., et al. (1986). Release of prostaglandin D2 into human airways during acute antigen challenge. NEJM 315:800–804.
   PubMed Web of Science ®Google Scholar
• Naclerio, R. M., Meier, H. L., Kagey-Sobotka, A., Adkinson, N. F., Jr., Meyers, D. A., Norman, P. S., et al. (1983). Mediator release after nasal airway challenge with allergen. Am Rev Respir Dis 128:597–602.
   PubMed Web of Science ®Google Scholar
• Nantel, F., Fong, C., Lamontagne, S., Wright, D. H., Giaid, A., Desrosiers, M., et al. (2004). Expression of prostaglandin D synthase and the prostaglandin D2 receptors DP and CRTH2 in human nasal mucosa. Prostaglandins Other Lipid Mediat 73:87–101.
   PubMed Web of Science ®Google Scholar
• Nguyen, H. A., Bae, Y. A., Lee, E. G., Kim, S. H., Diaz-Camacho, S. P., Nawa, Y., et al. (2010). A novel sigma-like glutathione transferase of Taenia solium metacestode. Int J Parasitol 40:1097–1106.
   PubMed Web of Science ®Google Scholar
• Noguchi, E., Yokouchi, Y., Shibasaki, M., Inudou, M., Nakahara, S., Nogami, T., et al. (2002). Association between TNFA polymorphism and the development of asthma in the Japanese population. Am J Respir Crit Care Med 166:43–46.
   PubMed Web of Science ®Google Scholar
• Oakley, A. J. (2005). Glutathione transferases: new functions. Curr Opin Struct Biol 15:716–723.
   PubMed Web of Science ®Google Scholar
• Oakley, A. J., Lo Bello, M., Nuccetelli, M., Mazzetti, A. P., Parker, M. W. (1999). The ligandin (non-substrate) binding site of human pi class glutathione transferase is located in the electrophile binding site (H-site). J Mol Biol 291:913–926.
   PubMed Web of Science ®Google Scholar
• Oakley, A. J., Rossjohn, J., Lo Bello, M., Caccuri, A. M., Federici, G., Parker, M. W. (1997). The three-dimensional structure of the human pi class glutathione transferase P1-1 in complex with the inhibitor ethacrynic acid and its glutathione conjugate. Biochemistry 36:576–585.
   PubMed Web of Science ®Google Scholar
• Okano, M., Fujiwara, T., Sugata, Y., Gotoh, D., Masaoka, Y., Sogo, M., et al. (2006). Presence and characterization of prostaglandin D2-related molecules in nasal mucosa of patients with allergic rhinitis. Am J Rhinol 20:342–348.
   PubMedGoogle Scholar
• Paolini, JF, Mitchel, YB, Reyes, R, Kher, U, Lai, E, Watson, DJ, et al. (2008). Effects of laropiprant on nicotinic acid-induced flushing in patients with dyslipidemia. Am J Cardiol 101:625–630.
   PubMed Web of Science ®Google Scholar
• Park, J. M., Kanaoka, Y., Eguchi, N., Aritake, K., Grujic, S., Materi, A. M., et al. (2007). Hematopoietic prostaglandin D synthase suppresses intestinal adenomas in ApcMin/+ mice. Cancer Res 67:881–889.
   PubMed Web of Science ®Google Scholar
• Pearson, W. R. (2005). Phylogenies of glutathione transferase families. Meth Enzymol 401:186–204.
   PubMed Web of Science ®Google Scholar
• Pennelli, A., Ortolano, S., Miele, R., Renda, T., Sacchetta, P., Di Ilio, C., et al. (2000). Glutathione S-transferase, similar to sigma class, from skin secretions of Xenopus laevis. IUBMB Life 50:203–207.
   PubMed Web of Science ®Google Scholar
• Perbandt, M., Hoppner, J., Burmeister, C., Luersen, K., Betzel, C., Liebau, E. (2008). Structure of the extracellular glutathione S-transferase OvGST1 from the human pathogenic parasite Onchocerca volvulus. J Mol Biol 377:501–511.
   PubMed Web of Science ®Google Scholar
• Pettipher, R. (2008). The roles of the prostaglandin D(2) receptors DP(1) and CRTH2 in promoting allergic responses. Br J Pharmacol 153(Suppl 1):S191–S199.
   PubMed Web of Science ®Google Scholar
• Pettipher, R., Hansel, T. T., Armer, R. (2007). Antagonism of the prostaglandin D2 receptors DP1 and CRTH2 as an approach to treat allergic diseases. Nat Rev Drug Discov 6:313–325.
   PubMed Web of Science ®Google Scholar
• Pinzar, E., Kanaoka, Y., Inui, T., Eguchi, N., Urade, Y., Hayaishi, O. (2000a). Prostaglandin D synthase gene is involved in the regulation of non-rapid eye movement sleep. Proc Natl Acad Sci U S A 97:4903–4907.
   PubMed Web of Science ®Google Scholar
• Pinzar, E., Miyano, M., Kanaoka, Y., Urade, Y., Hayaishi, O. (2000b). Structural basis of hematopoietic prostaglandin D synthase activity elucidated by site-directed mutagenesis. J Biol Chem 275:31239–31244.
   PubMed Web of Science ®Google Scholar
• Proud, D., Sweet, J., Stein, P., Settipane, R. A., Kagey-Sobotka, A., Friedlaender, M. H., et al. (1990). Inflammatory mediator release on conjunctival provocation of allergic subjects with allergen. J Allergy Clin Immunol 85:896–905.
   PubMed Web of Science ®Google Scholar
• Rajakariar, R., Hilliard, M., Lawrence, T., Trivedi, S., Colville-Nash, P., Bellingan G., et al. (2007). Hematopoietic prostaglandin D2 synthase controls the onset and resolution of acute inflammation through PGD2 and 15-deoxyDelta12 14 PGJ2. Proc Natl Acad Sci U S A 104:20979–20984.
   PubMed Web of Science ®Google Scholar
• Ranson, H., Rossiter, L., Ortelli, F., Jensen, B., Wang, X., Roth, C. W., et al. (2001). Identification of a novel class of insect glutathione S-transferases involved in resistance to DDT in the malaria vector Anopheles gambiae. Biochem J 359:295–304.
   PubMed Web of Science ®Google Scholar
• Rauch, N., Nauen, R. (2004). Characterization and molecular cloning of a glutathione S-transferase from the whitefly Bemisia tabaci (Hemiptera: Aleyrodidae). Insect Biochem Mol Biol 34:321–329.
   PubMed Web of Science ®Google Scholar
• Ren, H. L., Xu, D. D., Gopalakrishnan, S., Qiao, K., Huang, W. B., Wang, K. J. (2009). Gene cloning of a sigma class glutathione S-transferase from abalone (Haliotis diversicolor) and expression analysis upon bacterial challenge. Dev Comp Immunol 33:980–990.
   PubMed Web of Science ®Google Scholar
• Robinson, A., Huttley, G. A., Booth, H. S., Board, P. G. (2004). Modelling and bioinformatics studies of the human kappa-class glutathione transferase predict a novel third glutathione transferase family with similarity to prokaryotic 2-hydroxychromene-2-carboxylate isomerases. Biochem J 379:541–552.
   PubMed Web of Science ®Google Scholar
• Rossjohn, J., McKinstry, W. J., Oakley, A. J., Verger, D., Flanagan, J., Chelvanayagam, G., et al. (1998). Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site. Structure 6:309–322.
   PubMed Web of Science ®Google Scholar
• Satoh, T., Moroi, R., Aritake, K., Urade, Y., Kanai, Y., Sumi, K., et al. (2006). Prostaglandin D2 plays an essential role in chronic allergic inflammation of the skin via CRTH2 receptor. J Immunol 177:2621–2629.
   PubMed Web of Science ®Google Scholar
• Sau, A., Pellizzari Tregno, F., Valentino, F., Federici, G., Caccuri, A. M. (2010). Glutathione transferases and development of new principles to overcome drug resistance. Arch Biochem Biophys 500:116–122.
   PubMed Web of Science ®Google Scholar
• Shimura, C., Satoh, T., Igawa, K., Aritake, K., Urade, Y., Nakamura, M., et al. (2010). Dendritic cells express hematopoietic prostaglandin D synthase and function as a source of prostaglandin D2 in the skin. Am J Pathol 176:227–237.
   PubMed Web of Science ®Google Scholar
• Singh, S. P., Coronella, J. A., Benes, H., Cochrane, B. J., Zimniak, P. (2001). Catalytic function of Drosophila melanogaster glutathione S-transferase DmGSTS1-1 (GST-2) in conjugation of lipid peroxidation end products. Eur J Biochem 268:2912–2923.
   PubMedGoogle Scholar
• Snyder MJ, Walding JK and Feyereisen R. (1995). Glutathione S-transferases from larval manduca-sexta midgut: sequence of two cDNAs and enzyme-induction. Insect Biochem Mol Biol 25:455–465.
   PubMed Web of Science ®Google Scholar
• Sommer, A., Nimtz, M., Conradt, H. S., Brattig, N., Boettcher, K., Fischer, P., et al. (2001). Structural analysis and antibody response to the extracellular glutathione S-transferases from Onchocerca volvulus. Infect Immun 69:7718–7728.
   PubMed Web of Science ®Google Scholar
• Sommer, A., Rickert, R., Fischer, P., Steinhart, H., Walter, R. D., Liebau, E. (2003). A dominant role for extracellular glutathione S-transferase from Onchocerca volvulus is the production of prostaglandin D2. Infect Immun 71:3603–3606.
   PubMed Web of Science ®Google Scholar
• Sonoda, S., Ashfaq, M., Tsumuki, H. (2006). Genomic organization and developmental expression of glutathione S-transferase genes of the diamondback moth, Plutella xylostella. J Insect Sci 6:1–9.
   PubMedGoogle Scholar
• Straus, D. S., Glass, C. K. (2001). Cyclopentenone prostaglandins: new insights on biological activities and cellular targets. Med Res Rev 21:185–210.
   PubMed Web of Science ®Google Scholar
• Tanaka, K., Ogawa, K., Sugamura, K., Nakamura, M., Takano, S., Nagata, K. (2000). Cutting edge: differential production of prostaglandin D2 by human helper T cell subsets. J Immunol 164:2277–2280.
   PubMed Web of Science ®Google Scholar
• Tang, S. S., Lin, C. C., Chang, G. G. (1994). Isolation and characterization of octopus hepatopancreatic glutathione S-transferase. Comparison of digestive gland enzyme with lens S-crystallin. J Prot Chem 13:609–618.
   PubMedGoogle Scholar
• Taylor, JB, Vidal, A, Torpier, G, Meyer, DJ, Roitsch, C, Balloul, JM, et al. (1988). The glutathione transferase activity and tissue distribution of a cloned Mr28K protective antigen of Schistosoma mansoni. EMBO J 7:465–472.
   PubMed Web of Science ®Google Scholar
• Thomson, A. M., Meyer, D. J., Hayes, J. D. (1998). Sequence, catalytic properties, and expression of chicken glutathione-dependent prostaglandin D2 synthase, a novel class sigma glutathione S-transferase. Biochem J 333:317–325.
   PubMed Web of Science ®Google Scholar
• Tomarev, S. I., Chung, S., Piatigorsky, J. (1995). Glutathione S-transferase and S-crystallins of cephalopods: evolution from active enzyme to lens-refractive proteins. J Mol Evol 41:1048–1056.
   PubMed Web of Science ®Google Scholar
• Tomarev, S. I., Zinovieva, R. D. (1988). Squid major lens polypeptides are homologous to glutathione S-transferases subunits. Nature 336:86–88.
   PubMed Web of Science ®Google Scholar
• Tomarev, S. I., Zinovieva, R. D., Guo, K., Piatigorsky, J. (1993). Squid glutathione S-transferase. Relationships with other glutathione S-transferases and S-crystallins of cephalopods. J Biol Chem 268:4534–4542.
   PubMed Web of Science ®Google Scholar
• Tomarev, S. I., Zinovieva, R. D., Piatigorsky, J. (1991). Crystallins of the octopus lens. Recruitment from detoxification enzymes. J Biol Chem 266:24226–24231.
   PubMed Web of Science ®Google Scholar
• Trivedi, S. G., Newson, J., Rajakariar, R., Jacques, T. S., Hannon, R., Kanaoka, Y., et al. (2006). Essential role for hematopoietic prostaglandin D2 synthase in the control of delayed type hypersensitivity. Proc Natl Acad Sci U S A 103:5179–5184.
   PubMed Web of Science ®Google Scholar
• Trottein, F., Godin, C., Pierce, R. J., Sellin, B., Taylor, M. G., Gorillot, I., et al. (1992). Inter-species variation of schistosome 28-kDa glutathione S-transferases. Mol Biochem Parasitol 54:63–72.
   PubMed Web of Science ®Google Scholar
• Tu, C. P., Akgul, B. (2005). Drosophila glutathione S-transferases. Meth Enzymol 401:204–226.
   PubMed Web of Science ®Google Scholar
• Ueno, N., Murakami, M., Tanioka, T., Fujimori, K., Tanabe, T., Urade, Y., et al. (2001). Coupling between cyclooxygenase, terminal prostanoid synthase, and phospholipase A2. J Biol Chem 276:34918–34927.
   PubMed Web of Science ®Google Scholar
• Ueno, N., Taketomi, Y., Koga, K., Atsumi, Y., Kikuchi-Yanoshita, R., Kudo, I., et al. (2008). A negative regulator of delayed prostaglandin D-2 production in mouse mast cells. Biochim Biophy Acta Mol Cell Biol Lipids 1781:415–421.
   PubMed Web of Science ®Google Scholar
• Ujihara, M., Horiguchi, Y., Ikai, K., Urade, Y. (1988a). Characterization and distribution of prostaglandin D synthetase in rat skin. J Invest Dermatol 90:448–451.
   PubMed Web of Science ®Google Scholar
• Ujihara, M., Tsuchida, S., Satoh, K., Sato, K., Urade, Y. (1988b). Biochemical and immunological demonstration of prostaglandin D2, E2, and F2 alpha formation from prostaglandin H2 by various rat glutathione S-transferase isozymes. Arch Biochem Biophys 264:428–437.
   PubMed Web of Science ®Google Scholar
• Ujihara, M., Urade, Y., Eguchi, N., Hayashi, H., Ikai, K., Hayaishi, O. (1988c). Prostaglandin D2 formation and characterization of its synthetases in various tissues of adult rats. Arch Biochem Biophys 260:521–531.
   PubMed Web of Science ®Google Scholar
• Urade, Y., Fujimoto, N., Ujihara, M., Hayaishi, O. (1987). Biochemical and immunological characterization of rat spleen prostaglandin D synthetase. J Biol Chem 262:3820–3825.
   PubMed Web of Science ®Google Scholar
• Urade, Y., Ujihara, M., Horiguchi, Y., Ikai, K., Hayaishi, O. (1989). The major source of endogenous prostaglandin D2 production is likely antigen-presenting cells. Localization of glutathione-requiring prostaglandin D synthetase in histiocytes, dendritic, and Kupffer cells in various rat tissues. J Immunol 143:2982–2989.
   PubMed Web of Science ®Google Scholar
• Valles, S. M., Perera, O. P., Strong, C. A. (2003). Purification, biochemical characterization, and cDNA cloning of a glutathione S-transferase from the red imported fire ant, Solenopsis invicta. Insect Biochem Mol Biol 33:981–988.
   PubMed Web of Science ®Google Scholar
• Wan, Q., Whang, I., Lee, J. (2008). Molecular cloning and characterization of three sigma glutathione S-transferases from disk abalone (Haliotis discus discus). Comp Biochem Physiol B Biochem Mol Biol 151:257–267.
   PubMed Web of Science ®Google Scholar
• Weber, J. E., Oakley, A. J., Christ, A. N., Clark, A. G., Hayes, J. D., Hall, R., et al. (2010). Identification and characterisation of new inhibitors for the human hematopoietic prostaglandin D2 synthase. Eur J Med Chem 45:447–454.
   PubMed Web of Science ®Google Scholar
• Whitbread, A. K., Masoumi, A., Tetlow, N., Schmuck, E., Coggan, M., Board, P. G. (2005). Characterization of the omega class of glutathione transferases. Meth Enzymol 401:78–99.
   PubMed Web of Science ®Google Scholar
• Wilce, M. C. J., Parker, M. W. (1994). Structure and function of glutathione S-transferases. Biochim Biophys Acta Prot Struct Mol Enzymol 1205:1–18.
   PubMed Web of Science ®Google Scholar
• Wildenburg, G., Liebau, E., Henkle-Duhrsen, K. (1998). Onchocerca volvulus: ultrastructural localization of two glutathione S-transferases. Exp Parasitol 88:34–42.
   PubMed Web of Science ®Google Scholar
• Wistow, G., Piatigorsky, J. (1987). Recruitment of enzymes as lens structural proteins. Science 236:1554–1556.
   PubMed Web of Science ®Google Scholar
• Wu, Y., Fan, Y., Xue, B., Luo, L., Shen, J., Zhang, S., et al. (2006). Human glutathione S-transferase P1-1 interacts with TRAF2 and regulates TRAF2-ASK1 signals. Oncogene 25:5787–5800.
   PubMed Web of Science ®Google Scholar
• Yamada, T., Komoto, J., Watanabe, K., Ohmiya, Y., Takusagawa, F. (2005). Crystal structure and possible catalytic mechanism of microsomal prostaglandin E synthase type 2 (mPGES-2). J Mol Biol 348:1163–1176.
   PubMed Web of Science ®Google Scholar
• Yamamoto, K., Fujii, H., Aso, Y., Banno, Y., Koga, K. (2007). Expression and characterization of a sigma-class glutathione S-transferase of the fall webworm, Hyphantria cunea. Biosci Biotechnol Biochem 71:553–560.
   PubMed Web of Science ®Google Scholar
• Yamamoto, K., Zhang, P. B., Banno, Y., Fujii, H. (2006). Identification of a sigma-class glutathione-S-transferase from the silkworm, Bombyx mori. J Appl Entomol 130:515–522.
   Google Scholar
• Yang, Y., Li, L., Wong, G. W., Krilis, S. A., Madhusudhan, M. S., Sali, A., et al. (2002b). RasGRP4, a new mast cell-restricted Ras guanine nucleotide-releasing protein with calcium- and diacylglycerol-binding motifs. Identification of defective variants of this signaling protein in asthma, mastocytosis, and mast cell leukemia patients and demonstration of the importance of RasGRP4 in mast cell development and function. J Biol Chem 277:25756–25774.
   PubMed Web of Science ®Google Scholar
• Yang, H., Nie, L., Zhu, S., Zhou, X. (2002a). Purification and characterization of a novel glutathione S-transferase from Asaphis dichotoma. Arch Biochem Biophys 403:202–208.
   PubMed Web of Science ®Google Scholar