Biologia plantarum 46:71-78, 2003 | DOI: 10.1023/A:1027332915500

The Activity of the Antioxidative System in Cadmium-Treated Arabidopsis thaliana

E. Skórzyńska-Polit1,*, M. Drążkiewicz1, Z. Krupa1
1 Department of Plant Physiology, Maria Curie-Skłodowska University, Lublin, Poland

Changes in the content of reactive oxygen species (ROS) and activity of the antioxidant system were measured in leaves of Arabidopsis thaliana (L.) Heynh exposed to Cd2+. Mature plants growing in the nutrient solution were treated with Cd2+ at different concentrations (0, 5, 25, 50, 100 μM). An increase of O2.- content in leaves was observed at 5, 25 and 50 μM Cd2+. A strong accumulation of H2O2 was found only at the lowest Cd2+ concentration. The content of OH*. was high at 50 and 100 μM Cd2+. Superoxide dismutase (SOD) activity was always higher in Cd2+-treated plants than in control. Catalase (CAT) activity decreased with increasing Cd2+ concentration in the nutrient solution. Guaiacol peroxidase (POX) activity was particularly high at the lowest and highest Cd2+ concentrations and ascorbate peroxidase (APX) activity additionally at 50 μM Cd2+. Enhanced activity of monodehydroascorbate reductase (MDHAR) and strong reduction in ascorbate (AA) content were observed at 25 μM Cd2+. Glutathione reductase (GR) activity was always higher than in control but decreased as Cd2+ concentration increased. However, it was accompanied by gradual content increase of SH-groups.

Keywords: ascorbate; catalase; glutathione; dehydroascorbate; peroxidases; reactive oxygen species; superoxide dismutase
Subjects: antioxidants; Arabidopsis thaliana; ascorbate peroxidase; cadmium, antioxidant enzymes; catalase; glutathione reductase; guaiacol peroxidase; heavy metals; monodehydroascorbate peroxidase; peroxidases; reactive oxygen species (ROS); superoxide dismutase

Published: July 1, 2003Show citation

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Skórzyńska-Polit, E., Drążkiewicz, M., & Krupa, Z. (2003). The Activity of the Antioxidative System in Cadmium-Treated Arabidopsis thaliana. Biologia plantarum, 46(1), 71-78. doi: 10.1023/A:1027332915500.
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    References

    1. Aebi, H.: Catalase in vitro.-Methods Enzymol. 105: 121-126, 1984. Go to original source...
    2. Anderson, M.E.: Glutathione and glutathione disulfide in biological samples.-Methods Enzymol. 113: 548-555, 1985. Go to original source...
    3. Arrigoni, O.: Ascorbate system in plant development.-J. Bioenerg. Biomem. 26: 407-419, 1994. Go to original source...
    4. Babbs, C.F., Pham, J.A., Coolbaugh, R.C.: Lethal hydroxyl radical production in paraquat-treated plants.-Plant Physiol. 90: 1267-1270, 1989.
    5. Barceló, J., Poschenrieder, C.: Plant water relations as affected by heavy metal stress: a review.-J. Plant Nutr. 13: 1-37, 1990. Go to original source...
    6. Bartosz, G.: Oxidative stress in plants.-Acta Physiol. Plant. 19: 47-64, 1997. Go to original source...
    7. Beauchamp, C., Fridovich, I.: Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels.-Anal. Biochem. 44: 276-287, 1971. Go to original source...
    8. Boo, Y.C., Jung, J.: Water deficit-induced oxidative stress and antioxidative defences in rice plants.-J. Plant Physiol. 155: 255-261, 1999.
    9. Bradford, M.: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.-Anal. Biochem. 72: 248-254, 1976. Go to original source...
    10. Cadenas, E.: Biochemistry of oxygen toxicity.-Annu. Rev. Biochem. 58: 79-110, 1989. Go to original source...
    11. Cakmak, I., Horst, W.J.: Effect of aluminium on lipid peroxidation, superoxide dismutase, catalase, and peroxidase activities in roots tips of soybean (Glycine max).-Physiol. Plant. 83: 463-468, 1991. Go to original source...
    12. Chaoui, A., Mazhoudi, S., Ghorbal, M.H., El Ferjani, E.: Cadmium and zinc induction of lipid peroxidation and effects on antioxidant enzyme activities in bean (Phaseolus vulgaris L).-Plant Sci. 127: 139-147, 1997. Go to original source...
    13. Chen, S., Schopfer, P.: Hydroxyl-radical production in physiological reactions, A novel function of peroxidases.-Eur. J. Biochem. 260: 726-735, 1999.
    14. Dalurzo, H.C., Sandalio, L.M., Gómez, M., del Rio, L.A.: Cadmium infiltratration of detached pea leaves: effect on its activated oxygen metabolism.-Phyton 37: 59-64, 1997.
    15. Fornazier, R.F., Ferreira, R.R., Vitória, A.P., Molina, S.M.G., Lea, P.J., Azevedo, R.A.: Effects of cadmium on antioxidant enzyme activities in sugar cane.-Biol. Plant. 45: 91-97, 2002. Go to original source...
    16. Foyer, C.H., Lopez-Delgado, H., Dat, J.F., Scott, I.M.: Hydrogen peroxide-and glutathione-associated mechanisms of acclimatory stress tolerance and signalling.-Physiol. Plant. 100: 241-254, 1997. Go to original source...
    17. Gallego, S.M., Benavides, M.P., Tomaro, M.L.: Effect of heavy metal ion excess on sunflower leaves: evidence for involvement of oxidative stress.-Plant Sci. 121: 151-159, 1996. Go to original source...
    18. González, A., Steffen, K.L., Lynch, J.P.: Light and excess manganese, Implications for oxidative stress in common bean.-Plant Physiol. 118: 493-504, 1998. Go to original source...
    19. Green, M.J., Hill, H.A.O.: Chemistry of dioxygen.-Methods Enzymol. 105: 3-22, 1984. Go to original source...
    20. Grill, E., Winnacker, E.L., Zenk, M.H.: Phytochelatins: The principal heavy-metal complexing peptides of higher plants.-Science 230: 674-676, 1985. Go to original source...
    21. Horemans, N., Foyer, C.H., Asard, H.: Transport and action of ascorbate at the plant plasma membrane.-Trends Plant Sci. 5: 263-267, 2000. Go to original source...
    22. Knörzner, O.C., Durner, J., Böger, P.: Alterations in the antioxidative system of suspension-cultured soybean cells (Glycine max) induced by oxidative stress.-Physiol. Plant. 97: 388-396, 1996. Go to original source...
    23. Krupa, Z.: Cadmium against higher plant photosynthesis-a variety of effects and where do they possibly come from?-Z. Naturforsch. 54c: 723-729, 1999. Go to original source...
    24. Krupa, Z., Baszyński, T.: Some aspects of heavy metals toxicity towards photosynthetic apparatus-direct and indirect effects on light and dark reactions.-Acta Physiol. Plant. 17: 177-190, 1995.
    25. Lidon, F.C., Teixeira, M.G.: Oxy radicals production and control in the chloroplast of Mn-treated rice.-Plant Sci. 152: 7-15, 2000. Go to original source...
    26. Loggini, B., Scartazza, A., Brugnoli, E., Navari-Izzo, F.: Antioxidative defence system, pigment composition, and photosynthetic efficiency in two wheat cultivars subjected to drought.-Plant Physiol. 199: 1091-1099, 1999. Go to original source...
    27. Mazhoudi, S., Chaoui, A., Ghorbal, M.H., Ferjani, E.E.: Response of antioxidant enzymes to excess copper in tomato (Lycopersicon esculentum, Mill.).-Plant Sci. 127: 129-137, 1997. Go to original source...
    28. Milosevic, N., Slusarenko, A.J.: Active oxygen metabolism and lignification in the hypersensitive response in bean.-Physiol. mol. Plant Pathol. 49: 148-158, 1996. Go to original source...
    29. Miyake, Ch., Asada, K.: Thylakoid-bound ascorbate peroxidase in spinach chloroplasts and photoreduction of its primary oxidation product monodehydroascorbate radicals in thylakoids.-Plant Cell Physiol. 33: 541-553, 1992.
    30. Nakano, Y., Asada, K.: Purification of ascorbate peroxidase in spinach chloroplasts; its inactivation in ascorbate depleted medium and reactivation by monodehydroascorbate radical.-Plant Cell Physiol. 28: 131-140, 1987.
    31. Navari-Izzo, F., Quartacci, M.F., Pinzino, C., Vecchia, F.D., Sgherri, C.L.M.: Thylakoid-bound and stromal antioxidative enzymes in wheat treated with excess copper.-Physiol. Plant. 104: 630-638, 1998. Go to original source...
    32. Niewiadomska, E., Gaucher-Veilleux, C., Chevrier, N., Mauffette, Y., Dizengremel, P.: Elevated CO2 does not provide protection against ozone considering the activity of several antioxidant enzymes in leaves of sugar maple.-J. Plant Physiol. 155: 70-77, 1999. Go to original source...
    33. Noctor, G., Foyer, C.H.: Ascorbate and glutathione: keeping active oxygen under control.-Annu. Rev. Plant Physiol. Plant mol. Biol. 49: 249-279, 1998. Go to original source...
    34. Pell, E., Schlanghaufer, C.D., Arteca, R.N.: Ozone-induced oxidative stress: Mechanism of action and reaction.-Physiol. Plant. 100: 264-273, 1997. Go to original source...
    35. Pick, E.: Microassays for superoxide and hydrogen peroxide production and nitroblue tetrazolium reduction using an enzyme immunoassay microplate reader.-Methods Enzymol. 132: 407-421, 1986. Go to original source...
    36. Prasad, M.N.V.: Trace elements.-In: Prasad, M.N.V. (ed.): Plant Ecophysiology. Pp. 207-249. John Wiley & Sons, New York 1996.
    37. Rao, M.V., Hale, B.A., Ormrod, D.P.: Amelioration of ozone-induced oxidative damage in wheat plants grown under high carbon dioxide.-Physiol. Plant. 109: 421-432, 1995. Go to original source...
    38. Rucińska, R., Waplak, S., Gwóźdź, E.A.: Free radical formation and activity of antioxidant enzymes in lupin roots exposed to lead.-Plant Physiol. Biochem. 37: 187-194, 1999. Go to original source...
    39. Salin, M.L.: Toxic oxygen species and protective systems of the chloroplast.-Physiol. Plant. 72: 681-689, 1987.
    40. Scandalios, J.G.: Oxygen stress and superoxide dismutases.-Plant Physiol. 101: 7-12, 1993. Go to original source...
    41. Schickler, H., Caspi, H.: Response of antioxidative enzymes to nickel and cadmium stress in hyperaccumulator plants of the genus Alyssum.-Physiol. Plant. 105: 39-44, 1999. Go to original source...
    42. Shaw, B.P.: Effect of mercury and cadmium on the activities of antioxidative enzymes in the seedlings of Phaseolus aureus.-Biol. Plant. 37: 587-596, 1995. Go to original source...
    43. Siedlecka, A., Krupa, Z., Tukendorf, A. Skórzyńska-Polit, E., Maksymiec, W., Wójcik, M., Baszyński, T.: Angiosperms (Asteraceae, Convolvulaceae, Fabaceae and Poaceae; other than Brassicaceae).-In: Prasad, M.N.V. (ed.): Metals in the Environment: Analysis by Biodiversity. Pp. 171-217. Marcel Dekker, New York-Basel 2000.
    44. Sies, H.: Strategies of antioxidant defence.-Eur. J. Biochem. 215: 213-219, 1993. Go to original source...
    45. Smirnoff, N., Colombé, S. Drought influences the activity of enzymes of the chloroplast hydrogen peroxide scavenging system.-J. exp. Bot. 39: 1097-1108, 1988. Go to original source...
    46. Stroiński, A.: Some physiological and biochemical aspects of plant resistance to cadmium effect. I. Antioxidative system.-Acta Physiol. Plant. 21: 175-188, 1999. Go to original source...
    47. Vácha, F.: The role of oxygen in photosynthesis.-Photosynthetica 31: 321-334, 1995.
    48. Wang, S.Y., Jiao, H.J., Faust M.: Changes in ascorbate, glutathione, and related enzyme activities during thidiazuron-induced bud break of apple.-Physiol. Plant. 82: 231-236, 1991. Go to original source...
    49. Weckx, J.E.J., Clijsters, H.M.M.: Oxidative damage and defence mechanisms in primary leaves of Phaseolus vulgaris as a result of root assimilation of toxic amounts of copper.-Physiol. Plant. 96: 506-512, 1996. Go to original source...
    50. Weckx, J.E.J., Clijsters, H.M.M.: Zn phytotoxicity induces oxidative stress in primary leaves of Phaseolus vulgaris.-Plant Physiol. Biochem. 35: 405-410, 1997.
    51. Wójcik, M., Tukendorf, A.: Cd-tolerance of wild type of Arabidopsis thaliana.-Plant Physiol. Biochem. 38(Suppl.): 181, 2000.
    52. Woźny, A., Stroiński, A., Gwóźdź, E.: Plant Cell Responses to Cadmium.-Wydawnictwo Naukowe Uniwersytetu Im. Adama Mickiewicza, Poznań 1990.
    53. Xiang, C., Oliver, D.J.: Glutathione metabolic genes coordinatelly responded to heavy metals and jasmonic acid in Arabidopsis.-Plant Cell 10: 1539-1550, 1998.

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