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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Molecular characterization of glutathione peroxidase gene from the liver of silver carp, bighead carp and grass carp

  • Li, Guang-Zhao (College of Life Science and Technology, Jinan University) ;
  • Liang, Xu-Fang (College of Life Science and Technology, Jinan University) ;
  • Yao, Wei (College of Life Science and Technology, Jinan University) ;
  • Liao, Wan-Qin (College of Life Science and Technology, Jinan University) ;
  • Zhu, Wei-Feng (College of Life Science and Technology, Jinan University)
  • Received : 2007.07.02
  • Accepted : 2007.10.03
  • Published : 2008.03.31
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Abstract

The cDNAs encoding glutathione peroxidase (GPx) were cloned and sequenced from the liver of three Chinese carps with different tolerance to hepatotoxic microcystins, phyto-planktivorous silver carp (Hypophthalmichthys molitrix) and bighead carp (Aristichthys nobilis), and herbivorous grass carp (Ctenopharyngodon idellus). Using genome walker method, a 750 bp 5'-flanking region of the silver carp GPx gene was obtained, and several potential regulatory elements were identified in the promoter region of the GPx gene. The silver carp GPx gene was widely expressed in all tissues examined. Despite phylogenetic analysis, assigning this newly described carp GPx to the group of mammalian GPx2, the carp GPx seems more similar to GPx1 from a physiological point of view. The constitutive expression pattern of the three carp liver GPx gene, shows a positive relationship with their tolerance to microcystins.

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References

  1. Carmichael, W. W. (2001) Health effects of toxin-producing cyanobacteria: "the CyanoHABs". Hum. Ecol. Risk Assess 7, 1393-1407 https://doi.org/10.1080/20018091095087
  2. Pouria, S., Andrade, A. D., Barbosa, J., Cavalcanti, R. L., Barreto, V. T. S., Ward, C. J., Preiser, W., Poon, G. K., Neild, G. H. and Codd, G. A. (1998) Fatal microcystin intoxication in haemodialysis unit in Caruaru, Brazil. Lancet 352, 21-26 https://doi.org/10.1016/S0140-6736(97)12285-1
  3. Falconer, I. R. (2001) Toxic cyanobacterial bloom problems in Australian waters: risks and impacts on human health. Phycologia 40, 228-233 https://doi.org/10.2216/i0031-8884-40-3-228.1
  4. Jochimsen, E. M., Carmichael, W. W., An, J. S., Cardo, D. M., Cookson, S. T., Holmes, C. E., Antunes, M. B., de Melo Filho, D. A., Lyra, T. M., Barreto, V. S., Azevedo, S. M. and Jarvis, W. R. (1998) Liver failure and death after exposure to microcystins at a haemodialysis center in Brazil N. Engl. J. Med. 338, 873-878 https://doi.org/10.1056/NEJM199803263381304
  5. Ding, W. X., Shen, H. M. and Ong, C. N. (2001) Critical role of reactive oxygen species formation in microcystin-induced cytoskeleton disruption in primary cultured hepatocytes. J. Toxicol. Environ. Health, Part A 64, 507-519 https://doi.org/10.1080/152873901753215966
  6. Halliwell, B. and Gutteridge, J. M. C. (1999) Free Radicals in Biology and Medicine, Oxford University Press, Oxford, USA
  7. Almar, M., Otero, L., Santos, C. and Gallegho, J. G. (1998) Liver glutathione content and glutathione-dependent enzymes of two species of freshwater fishes as bioindicators of chemical pollution. J. Environ. Sci. Health 33, 769-783 https://doi.org/10.1080/03601239809373177
  8. Chu, F. F., Doroshow, J. H. and Esworhty, R. S. (1993) Expression, characterization and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI. J. Biol. Chem. 268, 2571-2576
  9. Flohe, L., Gunzler, W. A. and Schock, H. H. (1973) Glutathione peroxidase: a selenoenzyme. FEBS Lett. 32, 132-134 https://doi.org/10.1016/0014-5793(73)80755-0
  10. Kryukov, G. V., Castellano, S., Novoselov, S. V., Lobanov, A. V., Zehtab, O., Guigo, R. and Gladyshev1, V. N. (2003) Characterization of mammalian selenoproteomes. Science 300, 1439-1443 https://doi.org/10.1126/science.1083516
  11. Takahashi, K., Avissar, N., Whitin, J. and Cohen, H. (1987) Purification and characterization of human plasma glutathione peroxidase: a selenoglycoprotein distinct from the known cellular enzyme. Arch. Biochem. Biophys. 256, 677-686 https://doi.org/10.1016/0003-9861(87)90624-2
  12. Ursini, F., Maiorino, M., Valente, M., Ferri, L. and Gregolin, C. (1982) Purification from pig liver of a protein which protects liposomes and biomembranes from peroxidative degradation and exhibits glutathione peroxidase activity on phosphatidylcholine hydroperoxides. Biochim. Biophys. Acta. 710, 197-211 https://doi.org/10.1016/0005-2760(82)90150-3
  13. Ghyselinck, N. B. and Dufaure, J. P. (1990) A mouse cDNA sequence for epididymal androgen-regulated proteins related to glutathione peroxidase. Nucleic Acids Res. 18, 7144 https://doi.org/10.1093/nar/18.23.7144
  14. Xie, P. and Liu, J. K. (2001) Practical success of biomanipulation using filter-feeding fish to control cyanobacteria blooms: a synthesis of decades of research and application in a subtropical hypereutrophic lake. The Scientific World 1, 337-356 https://doi.org/10.1100/tsw.2001.67
  15. Xie, L. Q., Xie, P., Ozawa, K., Honma, T., Yokoyama, A. and Park, H. D. (2004) Dynamics of microcystins-LR and -RR in the phytoplanktivorous silver carp in a sub-chronic toxicity experiment. Environ. Pollut. 127, 431-439 https://doi.org/10.1016/j.envpol.2003.08.011
  16. Cazenave, J., Bistoni, M. A., Pesce, S. F. and Wunderlin, D. A. (2006) Differential detoxification and antioxidant response in diverse organs of Corydoras paleatus experimentally exposed to microcystin-RR. Aquat. Toxicol. 76, 1-12 https://doi.org/10.1016/j.aquatox.2005.08.011
  17. Jos, A., Pichardo, S., Prieto, A. I., Repetto, G., Vazquez, C. M., Moreno, I., Camean, A. M. (2005). Toxic cyanobacterial cells containing microcystins induce oxidative stress in exposed tilapia fish (Oreochromis sp.) under laboratory conditions. Aquat. Toxicol. 72, 261-271 https://doi.org/10.1016/j.aquatox.2005.01.003
  18. Li, X., Liu, Y., Song, L. and Liu J. (2003) Responses of anti-oxidant systems in the hepatocytes of common carp (Cyprinus carpio L.) to the toxicity of microcystin-LR. Toxicon. 42, 85-89 https://doi.org/10.1016/S0041-0101(03)00104-1
  19. Wang, L., Liang, X. F., Liao, W. Q., Lei,L. M. and Han, B. P. (2006) Structural and functional characterization of microcystin detoxification-related liver genes in a phytoplanktivorous fish, Nile tilapia (Oreochromis niloticus). Comp. Biochem. and Physiol. Part C: Toxicol. & Pharmacol. 144, 216-227 https://doi.org/10.1016/j.cbpc.2006.08.009
  20. He, J. W., He, Z. R. and Guo, Q. L. (1997) The toxicity of microcystis aeruginosa to fish and daphnia. Journal of Lake Sciences 9, 49-56 https://doi.org/10.18307/1997.0108
  21. Prabhakar, R., Vreven, T., Morokuma, K. and Musaev, D. G. (2005) Elucidation of the mechanism of selenoprotein glutathione peroxidase (GPx)-catalyzed hydrogen peroxide reduction by two glutathione molecules: a density functional study. Biochemistry 44, 11864-11871 https://doi.org/10.1021/bi050815q
  22. Aumann, K. D., Bedorf, N., Brigelius-Flohe, R., Schomburg, D. and Flohe, L. (1997) Glutathione peroxidase revisited-simulation of the catalytic cycle by computer-assisted molecular modelling. Biomed. Environ. Sci. 10, 136-155
  23. Ursini, F., Maiorino, M., Brigelius-Flohe, R., Aumann, K. D., Roveri, A., Schomburg, D. and Flohe, L. (1995) Diversity of glutathione peroxidases. Methods Enzymol. 252, 38-53 https://doi.org/10.1016/0076-6879(95)52007-4
  24. de Haan, J. B., Bladier, C., Griffiths, P., Kelner, M., O'Shea, R. D., Cheung, N. S., Bronson, R. T., Silvestro, M. J., Wild, S., Zheng, S. S., P. M., Hertzog, P. J. and Kola, I. (1998) Mice with a homozygous null mutation for the most abundant glutathione peroxidase, Gpx1, show increased susceptibility to the oxidative stress-inducing agents paraquat and hydrogen peroxide. J. Biol. Chem. 273, 22528-22536 https://doi.org/10.1074/jbc.273.35.22528
  25. Kelner, M. J., Bagnell, R. D., Montoya, M. A. and Lanham, K. A. (2000) Structural organization of the human gastrointestinal glutathione peroxidase (GPx2) promoter and 3'-nontranscribed region: transcriptional response to exogenous redox agents. Gene 248, 109-116 https://doi.org/10.1016/S0378-1119(00)00137-2
  26. Chu, F. F., Esworthy, R. S., Akman, S. and Doroshow, J. H. (1990) Modulation of glutathione peroxidase expression by selenium: effect on human MCF-7 breast cancer cell transfectants expressing a cellular glutathione peroxidase cDNA and doxorubicin-resistant MCF-7 cells. Nucl. Acids Res. 18, 1531-1539 https://doi.org/10.1093/nar/18.6.1531
  27. Moscow, J. A., Morrow, C. S., He, R., Mullenbach, G. T. and Cowan, K. H. (1992) Structure and function of the 5'-flanking sequence of the human cytosolic selenium-dependent glutathione peroxidase gene (hgpx1). J. Biol. Chem. 267, 5949-5958
  28. Chu, F. F. and Esworthy, R. S. (1995) The expression of an intestinal form of glutathione peroxidase (GSHPx-GI) in rat intestinal epithelium. Arch. Biochem. Biophys. 323, 288-294 https://doi.org/10.1006/abbi.1995.9962
  29. Brigelius-Flohe, R. (2006) Glutathione peroxidases and redox-regulated transcription factors. Biol. Chem. 387, 1329-1335 https://doi.org/10.1515/BC.2006.166
  30. Gehringer, M. M., Downs, K. S., Downing, T. G., Naude, R. J. and Shephard, E. G. (2003) An investigation into the effect of selenium supplementation on microcystin hepatotoxicity. Toxicon. 41, 451-458 https://doi.org/10.1016/S0041-0101(02)00362-8
  31. Yin, L., Huang, J., Huang, W., Li, D., Wang, G. and Liu, Y. (2005) Microcystin-RR-induced accumulation of reactive oxygen species and alteration of antioxidant systems in tobacco BY-2 cells. Toxicon. 46, 507-512 https://doi.org/10.1016/j.toxicon.2005.06.015
  32. Li, X. Y., Chung, I. K., Kim, J. I. and Lee, J. A. (2005) Oral exposure to Microcystis increases activity-augmented antioxidant enzymes in the liver of loach (Misgurnus mizolepis) and has no effect on lipid peroxidation. Comp. Biochem. and Physiol. Part C: Toxicol. & Pharmacol. 141, 292-296 https://doi.org/10.1016/j.cca.2005.07.004
  33. Liu, J. (1990) Lake Donghu Ecological Research, Science Press, Beijing, 1-407
  34. Liao, W. Q., Liang, X. F., Wang, L., Fang, L., Lin, X., Bai, J., Jian, Q. (2006) Structural conservation and food habit-related liver expression of uncoupling protein 2 gene in five major Chinese carps. J. Biochem. Mol. Biol. 39, 346-354 https://doi.org/10.5483/BMBRep.2006.39.4.346
  35. Tsunoda, T. and Takagi,T. (1999) Estimating transcription factor bindability on DNA. Bioinformatics 115, 622-630

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