Physiological and biochemical responses of Prorocentrum minimum to high light stress

被引:0
作者
Park S.Y. [1 ]
Choi E.S. [2 ]
Hwang J. [1 ]
Kim D. [3 ]
Ryu T.K. [4 ]
Lee T.-K. [1 ]
机构
[1] South Sea Environment Research Department, KORDI
[2] Department of Genetic Engineering, Sungkyunkwan University
[3] Department of Science Education, Kyungnam University Masan
[4] Environmental Health Risk Research Department, NFRDI
关键词
catalase; lipid peroxidation; Prorocentrum minimum; ROS; superoxide dismutase;
D O I
10.1007/s12601-009-0018-z
中图分类号
学科分类号
摘要
Prorocentrum minimum is a common bloomforming photosynthetic dinoflagellate found along the southern coast of Korea. To investigate the adaptive responses of P. minimum to high light stress, we measured growth rate, and generation of reactive oxidative species (ROS), superoxide dismutase (SOD), catalase (CAT), and malondialdehyde (MDA) in cultures exposed to normal (NL) and high light levels (HL). The results showed that HL (800 μmol m-2 s-1) inhibited growth of P. minimum, with maximal inhibition after 7-9 days. HL also increased the amount of ROS and MDA, suggesting that HL stress leads to oxidative damage and lipid peroxidation in this species. Under HL, we first detected superoxide on day 4 and H2O2 on day 5. We also detected SOD activity on day 5 and CAT activity on day 6. The level of lipid peroxidation, an indicator of cell death, was high on day 8. Addition of diphenyleneiodonium (DPI), an NAD(P)H inhibitor, decreased the levels of superoxide generation and lipid peroxidation. Our results indicate that the production of ROS which results from HL stress in P. minimum also induces antioxidative enzymes that counteract oxidative damage and allow P. minimum to survive. © 2009 Korea Ocean Research & Development Institute (KORDI) and the Korean Society of Oceanography (KSO) and Springer Netherlands.
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页码:199 / 204
页数:5
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共 32 条
  • [11] Halliwell B., Gutteridge J.M., Oxygen toxicity, oxygen radicals, transition metals and disease, Biochem J, 19, pp. 1-14, (1984)
  • [12] Ishimatsu A., Sameshima M., Tamura A., Oda T., Histological analysis of the mechanisms of Chattonella-induced hypoxemia in yellowtail, Fisheries Sci, 62, pp. 50-58, (1996)
  • [13] Johnson K.J., Fantone J.C., Kaplan J., Ward P.A., In vivo damage of rat lungs by oxygen metabolites, J Clin Invest, 67, pp. 983-993, (1981)
  • [14] Johnston Jr. R.B., Godzik C.A., Cohn Z.A., Increased superoxide anion production by immunologically activated and chemically elicited macrophages, J Exp Med, 148, pp. 115-127, (1978)
  • [15] Kakinuma K., Minakami S., Effects of fatty acids on superoxide radical generation in leukocytes, Biochim Biophys Acta, 538, pp. 50-59, (1978)
  • [16] Kawano I., Oda T., Ishimatsu A., Muramatsu T., Inhibitory effect of the iron chelator desferrioxamine (Desferal) on the generation of activated oxygen species by Chattonella marina, Mar Biol, 126, pp. 765-771, (1996)
  • [17] Kim C.S., Lee S.G., Lee C.K., Kim H.G., Jung J., Reactive oxygen species as causative agents in the ichthyotoxicity of the red tide dinoflagellate Cochlodinium polykrikoides, J Plankton Res, 21, pp. 2105-2115, (1999)
  • [18] Kumar G., Knowles N.R., Changes in lipid peroxidation and lipolytic and free-radical scavenging enzyme activities during aging and sprouting of potato (Solanum tuberosum) seedtubers, Plant Physiol, 102, pp. 115-124, (1993)
  • [19] Levine A., Tenhaken R., Dixon R., Lamb C., H<sub>2</sub>O<sub>2</sub> from the oxidative burst orchestrates the plant hypersensitive disease resistance response, Cell, 79, pp. 583-593, (1994)
  • [20] McCord J.M., Fridovich I., Superoxide dismutase: An enzymic function for erythrocuprein (hemocuprein), J Biol Chem, 244, pp. 6049-6055, (1969)