Abstract
Temporal changes in the oxidative stress and antioxidant system in Ulva pertusa Kjellman collected in July, September, and November was evaluated. The lipid peroxidation was decreased in September and re-increased in November. Glutathione, the major thiol antioxidant molecule, was mostly in reduced form in September, but the glutathione was more oxidized and the content was significantly decreased in November. Glutamylcysteine ligase (GCL), the rate limiting enzyme for glutathione synthesis, activity was increased in September and November. Among the enzymes for glutathione recycling, the glutathione peroxidase (GPx) activity was highest in September, while the glutathione reductase (GRd) activity was highest in November. The superoxide dismutase (SOD) activity was significantly increased after September. The results suggest that reduced oxidative stress in September was due to the increased ROS scavenging capacity. The elevated oxidative stress in November indicates that the ROS generation should be exceedingly high despite the adaptively increased GCL, GRd, and SOD activities in cold season. Catalase activity was decreased after September, which might be relevant to the control of hydrogen peroxide concentration as a signaling molecule to modulate intrinsic seasonal changes in the algal metabolism rather than to the antioxidant function.
Similar content being viewed by others
References
Fridovich, I. Fundamental aspects of reactive oxygen species, or what’s the matter with oxygen? Ann. N. Y. Acad. Sci. 893, 13–18 (1999).
Asada, K. The water cycle in chloroplast: scavenging of active oxygen and dissipation of excess photon. Annu. Rev. Plant. Physiol. Plant. Mol. Biol. 50, 601–639 (1999).
Lohrmann, N. L., Logan, B. A. & Johson, A. S. Seasonal acclimation of antioxidants and photosynthesis in chondrus cripus and Mastocarpus stellatus, Two cooccuring red algae with differing stress tolerances. Biol. Bull. 207, 225–232 (2004).
Vrablikova, H., Bartak, M. & Wonisch, A. Changes in glutathione and xanthophyll cycle pigments in the high light-stressed lichens Umbilicaria antarctica and Lasallia pustulata. J. Photochem. Photobiol. B. 79, 35–41 (2005).
Pätsikkä, E., Aro, E.-M. & Tyystjärvi, E. Increase in the quantum yield of photoinhibition contributes to copper toxicity in vivo. Plant Physio. 117, 619–627 (1998).
Noctor, G. & Foyer, C. H. Ascorbate and glutathione: keeping active oxygen under control. Annu. Rev. Plant. Physiol. Plant. Mol. Biol. 49, 249–279 (1998).
Burritt, D. J., Larkindale, J. & Hurd, C. L. Antioxidant metabolism in the intertidal red seaweed Stictosiphonia arbuscula following desiccation. Planta 215, 829–838 (2002).
Cavas, L. & Yurdakoc, K. A. Comparative study: assessment of the antioxidant system in the invasive green alga Caulerpa racemosa and some macrophtes from the Mediterranean. J. Exp. Mar. Biol. Ecol. 321, 35–41 (2005).
Niyogi, K. K. Photoprotection revisited: genetic and molecular approaches. Annu. Rev. Plant. Physiol. Plant. Mol. Biol. 50, 333–359 (1999).
Baker, N. R. in Causes of Photooxidative Stress and Amelioration of Defense System in Plant (eds Foyer, C & Mullineaux, P.) 127–154 (CRC Press, Boca Raton, FL, 1994).
Wise, R. R. Chilling-enhanced photooxidation: The production, action, and study of reactive oxygen species produced during chilling in the light. Photosynth. Res. 45, 79–97 (1995).
Logan, B. A., Demmig-Adams, B., Adams, W. W. & Grace, S. C. Antioxidation and xanthopgyll cycle-dependent energy dissipation in Cucurbita pepo and Vinca major acclimates to four growth irradiances in the field. J. Exp. Bot. 49, 1869–1879 (1998).
Lyons, N. M. & O’Brien, N. M. Modulatory effects of an algal extract containing astaxanthin on UVA-irradiated cells in culture. J. Dermatol. Sci. 30, 73–84 (2002).
Han, T., Kang, S. H., Park, J. S., Lee, H. K. & Brown, M. T. Physiological responses of Ulva pertusa and U. armoricana to copper exposure. Aquat. Toxicol. 86, 176–184 (2008).
Margis, R., Dunand, C., Teixeira, F. K. & Margis-Pinheiro, M. Glutathione peroxidase family — an evolutionary overview. Febs J. 275, 3959–3970 (2008).
Bandyopadhyay, S., Starke, D. W., Mieyal, J. J. & Gronostajski, R. M. Thioltransferase (glutaredoxin) reactivates the DNA-binding activity of oxidationinactivated nuclear factor I. J. Biol. Chem. 273, 392–397 (1998).
Klatt, P. et al. Redox regulation of c-Jun DNA binding by reversible S-glutathiolation. Faseb J. 13, 1481–1490 (1999).
Rokutan, K. et al. Glutathione depletion inhibits oxidant-induced activation of nuclear factor-kappa B, AP-1, and c-Jun/ATF-2 in cultured guinea-pig gastric epithelial cells. J. Gastroenterol. 33, 646–655 (1998).
Slesak, I., Libik, M., Karpinska, B., Karpinski, S. & Miszalski, Z. The role of hydrogen peroxide in regulation of plant metabolism and cellular signaling in response to environmental atresses. Acta. Biochem. Pol. 54, 39–50 (2007).
Noctor, G., Veljovic-Jovanovic, S. & Foyer, C. H. Peroxide processing in photosynthesis: antioxidant coupling and redox signaling. Phil. Trans R. Soc. Lond B. 355, 1465–1475 (2000).
Shao, N., Beck, C. F., Lemaire, S. D., & Krieger-Liszkay, A. Photosynthetic electron flow affects H2O2 signaling by inactivation of catalase in Chlamydomonas reinhardtii. Planta 2008, 1055–1066 (2008).
Ohkawa, H., Ohishi, N. & Yagi, K. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal. Biochem. 95, 351–358 (1979).
Park, E. M., Park, Y. M. & Gwak, Y. S. Oxidative damage in tissues of rats exposed to cigarette smoke. Free Radic. Biol. Med. 25, 79–86 (1998).
Reed, D. J. et al. High-performance liquid chromatography analysis of nanomole levels of glutathione, glutathione disulfide, and related thiols and disulfides. Anal. Biochem. 106, 55–62 (1980).
Seelig, G. F. & Meister, A. Gamma-glutamylcysteine synthetase from erythrocytes. Anal. Biochem. 141, 510–514 (1984).
Paglia, D. E. & Valentine, W. N. Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J. Lab. Clin. Med. 70, 158–169 (1967).
Cohen, M. B. & Duvel, D. L. Characterization of the inhibition of glutathione reductase and the recovery of enzyme activity in exponentially growing murine leukemia (L1210) cells treated with 1,3-bis (2-chloroethyl)-1-nitrosourea. Biochem. Pharmacol. 37, 3317–3320 (1988).
McCord, J. M. & Fridovich, I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244, 6049–6055 (1969).
Aebi, H. Catalase in vitro. Methods Enzymol. 105, 121–126 (1984).
Bradford, M. 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).
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265–275 (1951).
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Choi, EM., Park, JJ. & Han, T. Temporal changes in oxidative stress and antioxidant activities in Ulva pertusa Kjellman. Toxicol. Environ. Health Sci. 3, 206–212 (2011). https://doi.org/10.1007/s13530-011-0106-1
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s13530-011-0106-1