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Effect of transition metals on stress, lipid peroxidation and antioxidant enzyme activities in tobacco cell cultures

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Abstract

to-baccoBright Yellow 2 (BY-2) suspension culture to understand the mechanisms of metal resistance in plant cells.We have analysed superoxide dismutase, catalase, and ascorbate peroxidase enzyme activities and superoxidedismutase-isoforms by isoelectric focusing gels in tobacco cells grown at two different toxic concentrations ofeach of the transition metals: copper, iron, manganese and zinc. Exposure of tobacco cells to these metals causedchanges in total superoxide dismutase activity in a different manner, depending on the metal assayed: after cop-perand manganese treatments, total superoxide dismutase activity was enhanced, while it was reduced after ironand zinc exposure. Superoxide dismutase-isoforms were affected by the metal used, and a Fe-SOD band with thesame isoelectric point as a Cu, Zn-SOD from non-treated cells, was induced after iron and zinc treatments. Cu,Zn-SODs were present in all metal-treatments whereas Mn-SOD was not detected in any case. Concerning otherantioxidant enzymes tested, such as catalase and ascorbate peroxidase, the latter showed a remarkable increase inactivity in response to copper treatments and catalase activity was enhanced after iron and with the lowest man-ganeseconcentration. Lipid peroxidation was increased after each metal treatment, as an indication of the oxi-dativedamage caused by metal concentration assayed in tobacco cells. These results suggest that an activation ofsome antioxidant enzymes in response to oxidative stress induced by transition metals is not enough to confertolerance to metal accumulation.

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References

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

    Google Scholar 

  • Amako K., Chen G.-X. and Asada K. 1994. Separate assays specific for ascorbate peroxidase and guaiacol peroxidase and for the chloroplastic and cytosolic isozymes of ascorbate peroxidase in plants. Plant Cell. Physiol. 35: 497–504.

    Google Scholar 

  • Beauchamp C.O. and Fridovich I. 1971. Superoxide dismutase. Improved assays and assay aplicable to acrylamide gels. Anal. Biochem. 44: 276–287.

    Google Scholar 

  • Becana M., Moran J.F. and Iturbe-Ormaetxea I. 1998. Iron-dependent oxygen free radical generation in plants subjected to environmental stress: toxicity and antioxidant protection. Plant and Soil 201: 137–147.

    Google Scholar 

  • Bowler C., Van Camp W., Van Montagu M. and Inzé D. 1994. Superoxide dismutase in plants. Crit. Revs. in Plant Sci. 13: 199–218.

    Google Scholar 

  • Buege J.A. and Aust S.D. 1978. Microsomal lipid peroxidation. Methods Enzymol. 52: 302–310.

    Google Scholar 

  • Chaoui A., Mazhoudi S., Ghorbal M.H. and ElFerjani E. 1997. Cadmium and zinc induction of lipid peroxidation and effects on antioxidant enzyme activities in bean (Phaseolus vulgaris L.). Plant Sci. 127: 139–147.

    Google Scholar 

  • Chongpraditnun P., Mori S. and Chino M. 1992. Excess copper induces a cytosolic Cu, Zn-SOD in soybean root. Plant Cell Physiol. 33: 239–244.

    Google Scholar 

  • Foyer C.H., Descourvieres P. and Kunert K.J. 1994. Protection against oxygen radicals: an important defense mechanism studied in transgenic plants. Plant Cell Environ. 17: 517–523.

    Google Scholar 

  • Herbik A., Giritch A., Horstmann C., Becker R., Balzer H.-J., Bäumlein H. et al. 1996. Iron and copper nutrition-dependent changes in protein expression in a tomato wild type and the nicotianamine-free mutant Chloronerva. Plant Physiol. 111: 533–540.

    Google Scholar 

  • Kampfenkel K.-H., Van Montagu M. and Inzé D. 1995. Effects of iron excess in Nicotiana plumbaginifolia plants. Plant Physiol. 107: 725–735.

    Google Scholar 

  • Koppenol W.H. 1994. Chemistry of iron and copper in radical reactions. In: Rice-Evans C. and Burton R.H. (eds), Free Radical Damage and its Control. Elsevier Science.

  • Kurepa J., Van Montagu M. and Inzé D. 1997. Expression of sodCp and sodB genes in Nicotiana tabacum: effects of light and copper excess. J. Exp. Bot. 48: 2007–2014.

    Google Scholar 

  • Lowry O.H., Rosebrough N.J., Farr A.L. and Randall R.J. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193: 265–275.

    Google Scholar 

  • Mazhoudi S., Chaoui A., Ghorbal M.R. and El Ferjani E. 1997. Response of antioxidant enzymes to excess copper in tomato (Lycopersicon esculentum, Mill). Plant Sci. 127: 129–137.

    Google Scholar 

  • McCord J.M. and Fridovich I. 1969. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244: 6049–6055.

    Google Scholar 

  • Mead J.F., Wu G.-S., Stein R.A., Gelmont D., Sevanian A., Sohlberg E. et al. 1982. Mechanism of protection against membrane peroxidation. In: Kunio Y. (ed.), Lipid Peroxides in Biology and Medicine. Academic Press, London, pp. 161–173.

    Google Scholar 

  • Nagata T., Nemoto Y. and Hasezawa S. 1992. Tobacco BY-2 cell line as the “Hela” cell in the Cell Biology of higher plants. Int. Rev. Cytol. 132: 1–35.

    Google Scholar 

  • Palma J.M., Gómez M., Yáñez J. and del Río L.A. 1987. Increased levels of peroxisomal active oxygen-related enzymes in coppertolerant pea plants. Plant Physiology 85: 570–574.

    Google Scholar 

  • Piqueras A., Olmos E., Martínez-Solano J.R. and Hellín E. 1999. Cd-induced oxidative burst in tobacco BY-2 cell cultures: time course, subcellular location and antioxidant response. Free Rad. Res. 31: 533–538.

    Google Scholar 

  • Devi S. Rama and Prasad M.N.V. 1998. Copper toxicity in Ceratophyllum demersumL.(coontail) a free floating macrophyte: Response of antioxidant enzymes and antioxidants. Plant Sci. 138: 157–165.

    Google Scholar 

  • Robinson N.J., Tommey A.M., Kuske C. and Jackson P.J. 1993. Plant metallothioneins. Biochem. J. 295: 1–10.

    Google Scholar 

  • Savouré A., Thorin D., Davey M., Hua X., Mauro M., VanMontagu M. et al. 1999. NaCl and CuSO4 treatments trigger distinct oxidative defence mechanisms in Nicotiana plumbaginifolia L. Plant Cell Environm. 22: 387–396.

    Google Scholar 

  • Willekens H., Langebartels C., Tiré C., Van Montagu M., Inzé D. and Van Camp W. 1994. Differential regulation of catalase gene expression in Nicotiana plumbaginifolia L. Proc. Natl. Acad. Sci. USA 91: 10450–10454.

    Google Scholar 

  • Yamamoto Y., Hachiya A. and Matsumoto H. 1997. Oxidative damage to membranes by a combination of aluminium and iron in suspension-cultured tobacco cells. Plant Cell Physiol. 38: 1333–1339.

    Google Scholar 

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Authors and Affiliations

  1. Dept. Bioquimica Biologia Molecular y Celular de Plantas, Estacion Experimental Zaidin (C.S.I.C.), P.O. Box 419, 18080, Granada, Spain

    Pablo Bueno

  2. Dept. Nutrición y Fisiología Vegetal, Centro Edafología y Biología Aplicada del Segura (C.S.I.C.), 30080, Murcia, Spain

    Abel Piqueras

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  1. Pablo Bueno
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  2. Abel Piqueras
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Correspondence to Pablo Bueno.

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Bueno, P., Piqueras, A. Effect of transition metals on stress, lipid peroxidation and antioxidant enzyme activities in tobacco cell cultures. Plant Growth Regulation 36, 161–167 (2002). https://doi.org/10.1023/A:1015044705137

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