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Elevation of lipid peroxide level and production of hydroxy lipids in cultured Hepa-T1 cells by oxidative stressors

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A Correction to this article was published on 15 June 2018

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Abstract

In order to investigate the relationships between levels of lipid peroxides (LPO), hydroxy lipids (L-OH) and of antioxidative enzymes in live fish, cultured cells from tilapia liver (Hepa-T1) were treated with oxidative stressors, 2,2′-azobios(2-amidino-propane) dihydrochloride (AAPH) and H2O2. By treating with 5 mM AAPH, LPO and L-OH of the cells significantly increased time-dependently. In particular, L-OH increased from 7.6±0.7 to 23.6±1.8 nmol/mg protein after 2 h of treatment, and synchronously the glutathione peroxidase (GPx) activity of the cells increased from 259±106 to 1970±135 mU/mg protein. In the case of H2O2, however, no elevation of L-OH was observed. In this case, catalase (CAT) and superoxide dismutase (SOD) activities increased time-dependently. Especially, after 2 h exposure, the CAT activity increased remarkably from 217±21 to 2510±120 mU/mg protein, though the GPx activity did not change significantly. These results suggest that the elevation of the L-OH level is closely associated with the elevation of GPx activity, but not with that of CAT or SOD. However, when vitamin E-enriched Hepa-T1 cells were treated with AAPH and H2O2, the production of LPO and L-OH was suppressed significantly. The findings suggest that vitamin E also plays an important role in the levels of the oxidation products in vivo.

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Change history

  • 15 June 2018

    "The original article was corrected. We had used a cell line, Hepa-T1, in the article as a cell line derived from tilapia liver. However, in April 2018 the provider of Hepa-T1, RIKEN BioResource Research Center (RIKEN BRC), informed us that Hepa-T1 was derived from eel but not tilapia. RIKEN BRC found this misidentification by DNA barcoding of the mitochondrial gene cytochrome c oxidase subunit 1 (COI) (Fig.��1) in a course of pursuing more precise method for species identification of cell lines (Almeida et al. 2016). RIKEN BRC suggested a possibility that Hepa-T1 was replaced with Hepa-E1 cell line which was derived from eel and was deposited from the same scientist. RIKEN BRC accepted the deposition of these two cell lines simultaneously in March 1995 and could not detect this misidentification by the method available at that time, i.e. isozyme analysis with lactate dehydrogenase and nucleotide phosphorylase."

  • 15 June 2018

    "The original article was corrected. We had used a cell line, Hepa-T1, in the article as a cell line derived from tilapia liver. However, in April 2018 the provider of Hepa-T1, RIKEN BioResource Research Center (RIKEN BRC), informed us that Hepa-T1 was derived from eel but not tilapia. RIKEN BRC found this misidentification by DNA barcoding of the mitochondrial gene cytochrome c oxidase subunit 1 (COI) (Fig.��1) in a course of pursuing more precise method for species identification of cell lines (Almeida et al. 2016). RIKEN BRC suggested a possibility that Hepa-T1 was replaced with Hepa-E1 cell line which was derived from eel and was deposited from the same scientist. RIKEN BRC accepted the deposition of these two cell lines simultaneously in March 1995 and could not detect this misidentification by the method available at that time, i.e. isozyme analysis with lactate dehydrogenase and nucleotide phosphorylase."

References

  1. Christen Y. Oxidative stress and Alzheimer disease. Am. J. Clin. Nutr. 2000; 71: 621–629.

    Google Scholar 

  2. Yagi K. Lipid peroxides, free radicals, and diseases. In: Yagi K (ed.). Active Oxygen. Scientific Societies Press. Tokyo. 1993; 39–67.

    Google Scholar 

  3. Halliwell BB, Gutterridge JMC. Free Radicals in Biology and Medicine. Clarendon Press, Oxford. 1989.

    Google Scholar 

  4. Cross CE, Halliwell B, Borish ET, Pryor WA, Ames WA, Saul RL, MacCord JM, Harman D. Oxygen radicals and human diseases. Ann. Intern. Med. 1987; 107: 526–545.

    PubMed  CAS  Google Scholar 

  5. Sevenian A, Muakkaah-Kelly SF, Montetruque S. The influence of phospholipase A2 glutathione peroxidase on the membrane lipid peroxidase. Arch. Biochem. Biophys. 1983; 223: 441–452.

    Article  Google Scholar 

  6. Tanaka R, Higo Y, Murata H, Nakamura T. Accumulation of hydroxy lipids in live fish with oxidative stress. Fish. Sci. 1999; 65: 796–797.

    CAS  Google Scholar 

  7. Tanaka R, Higo Y, Shibata T, Suzuki N, Hatate H, Nagayama K, Nakamura T. Accumulation of hydroxy lipids in live fish infected with fish diseases. Aquaculture 2002; 211: 341–351.

    Article  CAS  Google Scholar 

  8. Evans JJ, Shoemaker C, Klesius PH. Experimental Streptococcus iniae infection of hybrid striped bass (Morone chrysops X Morone saxatilis) and tilapia (Oreochromis niloticus) by nares inoculation. Aquaculture 2000; 189: 197–210.

    Article  Google Scholar 

  9. Quabius ES, Balm DTN, Paul HM, Bonga W, Sjoerd E. The influence of polychlorinated biphenyl 126 on tilapia (Oreochromis mossambicus) liver. Comp. Biochem. Phys. Part A 1998; 120: 57–63.

    Article  Google Scholar 

  10. Bainy ACD, Saito E, Carvalho PSM, Junqueira VBC. Oxidative stress in gill, erythrocytes, liver and kidney of Nile tilapia (Oreochromis niloticus) from a polluted site. Aqua. Toxicol. 1996; 34: 151–162.

    Article  CAS  Google Scholar 

  11. Ursini F, Maiorino M, Brigelius-Flohé R, Aumann KD, Roveri A, Schomburg D, Flohé L. Diversity of glutathione peroxidases. Methods Enzymol. 1995; 252: 38–53.

    Article  PubMed  CAS  Google Scholar 

  12. Aebi H. Catalase in vitro. Methods Enzymol. 1984; 105: 121–126.

    Article  PubMed  CAS  Google Scholar 

  13. Garcia Ma. XU, Foote C, Saskia Es Devreotes PN, Alexander S, Alexander H. Differential developmental expression and cell type specificity of dictyostelium catalases and their response to oxidative stress and UV-light. Biochim. Biophy. Acta 2000; 1492: 295–310.

    CAS  Google Scholar 

  14. Oberley LW, Spitz DR. Assay of superoxide dismutase activity in tumor tissue. Methods Enzymol. 1984; 105: 457–464.

    Article  PubMed  CAS  Google Scholar 

  15. Nakamura T, Maeda H. A simple assay for hydroperoxides based on triphenylphosphine oxidation and high performance liquid chromatography. Lipids 1991; 26: 765–768.

    Article  CAS  Google Scholar 

  16. William WC. The preparation of volatile derivatives of lipids. In: William WC (ed.) Lipid Analysis. Pergamon, Oxford. 1973; 88–89.

    Google Scholar 

  17. Zhang LP, Maiorino M, Roveri A, Ursini F. Phospholipid hydroperoxide glutathione peroxidase: specific activity in tissues of rats of different age and comparison with other glutathione peroxidases. Biochim. Biophy. Acta 1989; 1006: 140–143.

    CAS  Google Scholar 

  18. Imaia H, Sumia D, Sakamoto H, Hanamoto A, Arai M, Chiba N, Nakagawa Y. Overexpression of phospholipid hydroperoxide glutathione peroxidase suppressed cell death due to oxidative damage in rat basophile leukemia cells (RBL-2H3). Biochem. Biophys. Res. Comm 1996; 222: 432–438.

    Article  Google Scholar 

  19. Sakai T, Murata H, Yamauchi K, Sekiya T, Ukawa M. Effect of dietary lipid peroxides contents on in vivo lipid peroxidation, alpha-tocopherol contents, and superoxide dismutase and glutathione peroxidase activities in the liver of yellowtail. Nippon Suisan Gakkaishi 1992; 58: 1483–1486.

    CAS  Google Scholar 

  20. Murata H, Sakai T, Yamauchi K, Ito, T, Tsuda T, Yoshida T, Fukudome M. In vivo lipid peroxidation levels and antioxidant activities of cultured and wild yellowtail. Fish. Sci. 1996; 62: 64–68.

    CAS  Google Scholar 

  21. Frankel EN. Biological systems. In: Frankel EN (ed). Lipid Oxidation. The Oily Press, Glasgow, 1998; 249–256.

    Google Scholar 

  22. Yoshikawa T. Free radical and elemination of active oxygen. In: Yoshikawa T (ed). Science of Free Radical. Kodansha, Tokyo. 1997; 45.

    Google Scholar 

  23. Niki E. Free radical initiators as source of water or lipid-soluble peroxyl radicals. Methods Enzymol. 1990; 186: 101–108.

    Google Scholar 

  24. Esterbauer H, Dieber-Rotheneder M, Striegl G, Waeg G. Role of vitamin E in preventing the oxidation of low density lipoproteine. Am. J. Clin. Nutr. 1991; 53: 314–321.

    Google Scholar 

  25. Burton GW, Traber MG. Vitamin E: antioxidant activity, biokinetics and bioavailability. Ann. Rev. Nutr. 1990; 10: 357–382.

    Article  CAS  Google Scholar 

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Correspondence to Ryusuke Tanaka.

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Tanaka, R., Hatate, H., Ito, M. et al. Elevation of lipid peroxide level and production of hydroxy lipids in cultured Hepa-T1 cells by oxidative stressors. Fish Sci 72, 665–672 (2006). https://doi.org/10.1111/j.1444-2906.2006.01197.x

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  • DOI: https://doi.org/10.1111/j.1444-2906.2006.01197.x

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