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Journal of Botany
Volume 2012 (2012), Article ID 985298, 22 pages
http://dx.doi.org/10.1155/2012/985298
Review Article

The Language of Reactive Oxygen Species Signaling in Plants

1Post Graduate Department of Botany, Hooghly Mohsin College, (West Bengal Education Service), Chinsurah, Hooghly, West Bengal 712 101, India
2Department of Botany, Krishnanagar Government College, (West Bengal Education Service), Krishnanagar, District—Nadia, West Bengal 741 101, India

Received 7 August 2011; Revised 16 October 2011; Accepted 1 November 2011

Academic Editor: Hiroyoshi Takano

Copyright © 2012 Soumen Bhattacharjee. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. R. Mittler and E. Blumwald, “Genetic engineering for modern agriculture: challenges and perspectives,” Annual Review of Plant Biology, vol. 61, pp. 443–462, 2010. View at Publisher · View at Google Scholar · View at Scopus
  2. S. Bhattacharjee, “Sites of generation and physicochemical basis of formation of reactive oxygen species in plant cell,” in Reactive Oxygen Species and Antioxidants in Higher Plants, S. Dutta Gupta, Ed., pp. 1–30, CRC Press, New York, NY, USA, 2010.
  3. G. Miller, V. Shulaev, and R. Mittler, “Reactive oxygen signaling and abiotic stress,” Physiologia Plantarum, vol. 133, no. 3, pp. 481–489, 2008. View at Publisher · View at Google Scholar · View at Scopus
  4. S. S. Gill and N. Tuteja, “Reactive oxygen species and antioxidant machinery in abiotic stress tolerance in crop plants,” Plant Physiology and Biochemistry, vol. 48, no. 12, pp. 909–930, 2010. View at Publisher · View at Google Scholar · View at Scopus
  5. G. Miller, K. Schlauch, R. Tam et al., “The plant NADPH oxidase RBOHD mediates rapid systemic signaling in response to diverse stimuli,” Science Signaling, vol. 2, no. 84, pp. 45–49, 2009. View at Publisher · View at Google Scholar · View at Scopus
  6. I. Kovalchuk, “Multiple roles of radicles in plants,” in Reactive Oxygen Species and Antioxidants in Higher Plants, S. Dutta Gupta, Ed., pp. 31–44, CRC Press, New York, NY, USA, 2010.
  7. E. F. Eltsner, “Metabolism of activated oxygen species,” in The Biochemistry of Plants, D. D. Davis, Ed., pp. 253–315, Academic Press, San Diego, Calif, USA, 1987.
  8. B. Halliwell and J. M. C. Gutteridge, Free Radicals in Biology and Medicine, Clarendon Press, Oxford, UK, 1989.
  9. J. Dat, S. Vandenabeele, E. Vranová, M. van Montagu, D. Inzé, and F. van Breusegem, “Dual action of the active oxygen species during plant stress responses,” Cellular and Molecular Life Sciences, vol. 57, no. 5, pp. 779–795, 2000. View at Publisher · View at Google Scholar
  10. C. H. Foyer and J. Harbinson, “Oxygen metabolism and regulation of photoelectron transport,” in Causes of Photooxidative Stress and Amelioration of Defense System in Plants, C. H. Foyer and P. M. Mullineauex, Eds., CRC Press, Boca Raton, Fla, USA, 1994.
  11. M. Dynowski, G. Schaaf, D. Loque, O. Moran, and U. Ludewig, “Plant plasma membrane water channels conduct the signalling molecule H2O2,” Biochemical Journal, vol. 414, no. 1, pp. 53–61, 2008. View at Publisher · View at Google Scholar · View at Scopus
  12. B. B. Buchanan and Y. Balmer, “Redox regulation: a broadening horizon,” Annual Review of Plant Biology, vol. 56, pp. 187–220, 2005. View at Publisher · View at Google Scholar · View at Scopus
  13. L. A. Del Rio, L. M. Sandalio, J. M. Palma, P. Bueno, and F. J. Corpas, “Metabolism of oxygen radicals in peroxisomes and cellular implications,” Free Radical Biology and Medicine, vol. 13, no. 5, pp. 557–580, 1992. View at Publisher · View at Google Scholar · View at Scopus
  14. K. Asada, “Production and scavenging of reactive oxygen species in chloroplasts and their functions,” Plant Physiology, vol. 141, no. 2, pp. 391–396, 2006. View at Publisher · View at Google Scholar · View at Scopus
  15. C. G. Bartoli, M. Simontacchi, E. Tambussi, J. Beltrano, E. Montaldi, and S. Puntarulo, “Drought and watering-dependent oxidative stress: effect on antioxidant content in Triticum aestivum L. leaves,” Journal of Experimental Botany, vol. 50, no. 332, pp. 375–383, 1999. View at Scopus
  16. E. Hideg, C. Barta, T. Kálai, I. Vass, K. Hideg, and K. Asada, “Detection of singlet oxygen and superoxide with fluorescent sensors in leaves under stress by photoinhibition or UV radiation,” Plant and Cell Physiology, vol. 43, no. 10, pp. 1154–1164, 2002.
  17. C. H. Foyer and G. Noctor, “Redox sensing and signaling associated with reactive oxygen in chloroplast, peroxysome and mitochondria,” Physiologia Plantarum, vol. 119, pp. 255–264, 2003.
  18. P. J. Nixon, “Chlororespiration,” Philosophical Transactions of the Royal Society B: Biological Sciences, vol. 355, no. 1402, pp. 1541–1547, 2000.
  19. E. Vranova, F. Van Breusegerm, J. Dat, E. Belles-Bolx, and D. Inze, “Role of reactive oxygen species in signal transduction,” in Plant Signal Transduction, D. Scheel and C. Wasternack, Eds., pp. 41–73, Oxford University Press, Oxford, UK, 2002.
  20. D. P. Maxwell, R. Nickels, and L. McIntos, “Evidence of mitochondrial involvement in the transduction of signals required for the induction of genes associated with pathogen attack and senescence,” Plant Journal, vol. 29, no. 3, pp. 269–279, 2002. View at Publisher · View at Google Scholar · View at Scopus
  21. T. G. Gabig, “NADPH-dependent superoxide generating oxidase from human nutrophils,” Journal of Biological Chemistry, vol. 258, pp. 6352–6356, 1983.
  22. A. W. Segal and A. Abo, “The biochemical basis of the NADPH oxidase of phagocytes,” Trends in Biochemical Sciences, vol. 18, no. 2, pp. 43–47, 1993. View at Publisher · View at Google Scholar · View at Scopus
  23. G. P. Bolwell, V. S. Butt, D. R. Davies, and A. Zimmerlin, “The origin of the oxidative burst in plants,” Free Radical Research, vol. 23, no. 6, pp. 517–532, 1995. View at Scopus
  24. S. Bhattacharjee, “Reactive oxygen species and oxidative burst: roles in stress, senescence and signal transduction in plants,” Current Science, vol. 89, no. 7, pp. 1113–1121, 2005. View at Scopus
  25. B. Halliwell, “Reactive species and antioxidants. Redox biology is a fundamental theme of aerobic life,” Plant Physiology, vol. 141, no. 2, pp. 312–322, 2006. View at Publisher · View at Google Scholar · View at Scopus
  26. L. A. Del Río, L. M. Sandalio, F. J. Corpas, J. M. Palma, and J. B. Barroso, “Reactive oxygen species and reactive nitrogen species in peroxisomes. Production, scavenging, and role in cell signaling,” Plant Physiology, vol. 141, no. 2, pp. 330–335, 2006. View at Publisher · View at Google Scholar · View at Scopus
  27. T. Gechev, V. Petrov, and I. Minkov, “Reactive oxygen species and programmed cell death,” in Reactive Oxygen Species and Antioxidants in Higher Plants, S. Dutta Gupta, Ed., pp. 65–78, CRC Press, New York, NY, USA, 2010.
  28. K. Apel and H. Hirt, “Reactive oxygen species: metabolism, oxidative stress, and signal transduction,” Annual Review of Plant Biology, vol. 55, pp. 373–399, 2004. View at Publisher · View at Google Scholar · View at Scopus
  29. S. Karpinski, C. Escobar, B. Karpinska, G. Creissen, and P. M. Mullineaux, “Photosynthetic electron transport regulates the expression of cytosolic ascorbate peroxidase genes in arabidopsis during excess light stress,” Plant Cell, vol. 9, no. 4, pp. 627–640, 1997. View at Publisher · View at Google Scholar · View at Scopus
  30. V. Locato, M. C. Pinto de, A. Paradiso, and L. Gara de, “Reactive oxygen species and ascorbate—glutathione interplay in signaling and stress responses,” in Reactive Oxygen Species and Antioxidants in Higher Plants, S. Dutta Gupta, Ed., pp. 45–64, CRC Press, New York, NY, USA, 2010.
  31. M. Santos, H. Gousseau, C. Lister, C. Foyer, G. Creissen, and P. Mullineaux, “Cytosolic ascorbate peroxidase from Arabidopsis thaliana L. is encoded by a small multigene family,” Planta, vol. 198, no. 1, pp. 64–69, 1996. View at Scopus
  32. S. Karpinski, C. Escobar, B. Karpinska, G. Creissen, and P. M. Mullineaux, “Photosynthetic electron transport regulates the expression of cytosolic ascorbate peroxidase genes in Arabidopsis during excess light stress,” Plant Cell, vol. 9, no. 4, pp. 627–640, 1997. View at Publisher · View at Google Scholar · View at Scopus
  33. F. Åslund, M. Zheng, J. Beckwith, and G. Storz, “Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol—disulfide status,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 11, pp. 6161–6165, 1999. View at Publisher · View at Google Scholar · View at Scopus
  34. A. Goyer, C. Haslekås, M. Miginiac-Maslow et al., “Isolation and characterization of a thioredoxin-dependent peroxidase from Chlamydomonas reinhardtii,” European Journal of Biochemistry, vol. 269, no. 1, pp. 272–282, 2002. View at Publisher · View at Google Scholar · View at Scopus
  35. P. Spiteller, W. Kern, J. Reiner, and G. Spiteller, “Aldehydic lipid peroxidation products derived from linoleic acid,” Biochimica et Biophysica Acta, vol. 1531, no. 3, pp. 188–208, 2001. View at Publisher · View at Google Scholar
  36. L. Nagy, P. Tontonoz, J. G. A. Alvarez, H. Chen, and R. M. Evans, “Oxidized LDL regulates macrophage gene expression through ligand activation of PPARγ,” Cell, vol. 93, no. 2, pp. 229–240, 1998. View at Publisher · View at Google Scholar · View at Scopus
  37. H. Kuhn, R. Wiesner, L. Alder, and T. Schewe, “Occurrence of free and esterified lipoxygenase products in leaves of Glechoma hederacea L. and other Labiatae,” European Journal of Biochemistry, vol. 186, no. 1-2, pp. 155–162, 1989. View at Publisher · View at Google Scholar · View at Scopus
  38. C. Foyer, “Oxygen metabolism and electron transport in photosynthesis,” in The Molecular Biology of Free Radical Scavenging Systems, J. Scandalios, Ed., ISBN 0-87969-502, pp. 587–621, Cold Spring Harbor Laboratory Press, New York, NY, USA, 1997.
  39. A. Arora, R. K. Sairam, and G. C. Srivastava, “Oxidative stress and antioxidative system in plants,” Current Science, vol. 82, no. 10, pp. 1221–1235, 2002. View at Scopus
  40. R. G. Alscher and J. L. Hess, Antioxidant in higher plants, ISBN O-8493-6328-4, CRC Press, Boca Raton, Fla, USA, 1993.
  41. C. J. Dougles, “Phenyl propanoid metabolism and lignin bio-synthesis: from weeds to trees,” Trends in Plant Science, vol. 1, pp. 171–178, 1987.
  42. A. Levine, R. Tenhaken, R. Dixon, and C. Lamb, “H2O2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response,” Cell, vol. 79, no. 4, pp. 583–593, 1994. View at Publisher · View at Google Scholar · View at Scopus
  43. S. Karpinski, C. Escobar, B. Karpinska, G. Creissen, and P. M. Mullineaux, “Photosynthetic electron transport regulates the expression of cytosolic ascorbate peroxidase genes in arabidopsis during excess light stress,” Plant Cell, vol. 9, no. 4, pp. 627–640, 1997. View at Publisher · View at Google Scholar · View at Scopus
  44. C. H. Foyer, P. Descourvieres, and K. J. Kunert, “Protection against oxygen radicals : an important defence mechanism studied in transgenic plants,” Plant, Cell & Environment, vol. 17, pp. 507–523, 1994.
  45. R. D. Allen, “Dissection of oxidative stress tolerance using transgenic plants,” Plant Physiology, vol. 107, no. 4, pp. 1049–1054, 1995. View at Scopus
  46. H. Lopez-Delgado, J. F. Dat, C. H. Foyer, and I. M. Scott, “Induction of thermotolerance in potato microplants by acetylsalicylic acid and H2O2,” Journal of Experimental Botany, vol. 49, no. 321, pp. 713–720, 1998. View at Scopus
  47. T. Okuda, Y. Matsuda, A. Yamanaka, and S. Sagisaka, “Abrupt increase in the level of hydrogen peroxide in leaves of winter wheat is caused by cold treatment,” Plant Physiology, vol. 97, no. 3, pp. 1265–1267, 1991. View at Scopus
  48. Z. Chen, H. Silva, and R. F. Klessig, “Active oxygen species in the induction of plant systemic acquired resistance by salicylic acid,” Science, vol. 262, no. 5141, pp. 1883–1886, 1993. View at Scopus
  49. T. K. Prasad, M. D. Anderson, B. A. Martin, and C. R. Stewart, “Evidence for chilling-induced oxidative stress in maize seedlings and a regulatory role for hydrogen peroxide,” Plant Cell, vol. 6, no. 1, pp. 65–74, 1994. View at Publisher · View at Google Scholar · View at Scopus
  50. C. H. Foyer, “Oxygen metabolism and electron transport in photosynthesis,” in Oxidative Stress and the Molecular Biology of Antioxidant Defenses, J. Scandalios, Ed., pp. 587–621, Cold Spring Harbor Laboratory Press, New York, NY, USA, 1996.
  51. N. P. A. Huner, G. Öquist, and F. Sarhan, “Energy balance and acclimation to light and cold,” Trends in Plant Science, vol. 3, no. 6, pp. 224–230, 1998. View at Publisher · View at Google Scholar · View at Scopus
  52. G. H. Krause, “The role of oxygen in photoinhibition and photosynthesis,” in Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants, C. H. Foyer and P.M. Mullineaux, Eds., pp. 43–76, CRC Press, Boca Raton, Fla, USA, 1994.
  53. C. H. Foyer, H. Lopez-Delgado, J. F. Dat, and I. M. Scott, “Hydrogen peroxide- and glutathione-associated mechanisms of acclimatory stress tolerance and signalling,” Physiologia Plantarum, vol. 100, no. 2, pp. 241–254, 1997. View at Publisher · View at Google Scholar · View at Scopus
  54. G. H. Krause, “Photoinhibition of photosynthesis. An evaluation of damaging and protective mechanisms,” Physiologia Plantarum, vol. 74, pp. 566–574, 1988.
  55. A. W. Russell, C. Critchley, S. A. Robinson et al., “Photosystem II regulation and dynamics of the chloroplast D1 protein in Arabidopsis leaves during photosynthesis and photoinhibition,” Plant Physiology, vol. 107, no. 3, pp. 943–952, 1995. View at Scopus
  56. M. Santos, H. Gousseau, C. Lister, C. Foyer, G. Creissen, and P. Mullineaux, “Cytosolic ascorbate peroxidase from Arabidopsis thaliana L. is encoded by a small multigene family,” Planta, vol. 198, no. 1, pp. 64–69, 1996. View at Scopus
  57. G. Noctor, A. C. M. Arisi, L. Jouanin, K. J. Kunert, H. Rennenberg, and C. H. Foyer, “Glutathione: biosynthesis, metabolism and relationship to stress tolerance explored in transformed plants,” Journal of Experimental Botany, vol. 49, no. 321, pp. 623–647, 1998. View at Scopus
  58. Y. Matsuda, T. Okuda, and S. Sagisaka, “Regulation of protein synthesis by hydrogen peroxide in crowns of winter wheat,” Bioscience, Biotechnology and Biochemistry, vol. 58, no. 5, pp. 906–909, 1994. View at Scopus
  59. T. K. Prasad, M. D. Anderson, and C. R. Stewart, “Localization and characterization of peroxidases in the mitochondria of chilling-acclimated maize seedlings,” Plant Physiology, vol. 108, no. 4, pp. 1597–1605, 1995.
  60. U. Neuenschwander, B. Vernooij, L. Friedrich, S. Uknes, H. Kessmann, and J. Ryals, “Is hydrogen peroxide a second messenger of salicylic acid in systemic acquired resistance?” Plant Journal, vol. 8, no. 2, pp. 227–233, 1995. View at Publisher · View at Google Scholar · View at Scopus
  61. Y. Doke, N. Miura, M. S. Leandro, and K. Kawakita, “Involvement of superoxide in signal transduction: responses to attack by pathogens, physical and chemical shocks, and UV irradiation,” in Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants, C. H. Foyer and P. M. Mullineaux, Eds., ISBN 0-8493-5443-9, pp. 177–197, CRC Press, Boca Raton, Fla, USA, 1994.
  62. H. Knight, A. J. Trewavas, and M. R. Knight, “Cold calcium signaling in Arabidopsis involves two cellular pools and a change in calcium signature after acclimation,” Plant Cell, vol. 8, no. 3, pp. 489–503, 1996. View at Scopus
  63. R. Desikan, S. J. Neill, and J. T. Hancock, “Generation of active oxygen in Arabidopsis thaliana,” Phyton—Annales Rei Botanicae, vol. 37, no. 3, pp. 65–70, 1997. View at Scopus
  64. R. Desikan, J. T. Hancock, M. J. Coffey, and S. J. Neill, “Generation of active oxygen in elicited cells of Arabidopsis thaliana is mediated by a NADPH oxidase-like enzyme,” FEBS Letters, vol. 382, no. 1-2, pp. 213–217, 1996. View at Publisher · View at Google Scholar · View at Scopus
  65. R. Desikan, A. Reynolds, J. T. Hancock, and S. J. Neill, “Harpin and hydrogen peroxide both initiate programmed cell death but have differential effects on defence gene expression in Arabidopsis thaliana suspension cultures,” Biochemical Journal, vol. 330, no. 1, pp. 115–120, 1998.
  66. Y. K. Sharma, J. León, I. Raskin, and K. R. Davis, “Ozone-induced responses in Arabidopsis thaliana: the role of salicylic acid in the accumulation of defense-related transcripts and induced resistance,” Proceedings of the National Academy of Sciences of the United States of America, vol. 93, no. 10, pp. 5099–5104, 1996. View at Publisher · View at Google Scholar · View at Scopus
  67. J. J. Burke, P. E. Gamble, J. L. Hartfield, and J. E. Quisenberry, “Plant morphological and biochemical responses to field water deficit. I. Responses of glutathione reductase activity and paraquat sensitivity,” Plant Physiology, vol. 79, pp. 415–419, 1985.
  68. C. Bowler, M. Van Montagu, and D. Inzé, “Superoxide dismutase and stress tolerance,” Annual Review of Plant Physiology and Plant Molecular Biology, vol. 43, no. 1, pp. 83–116, 1992. View at Scopus
  69. A. Levine, R. Tenhaken, R. Dixon, and C. Lamb, “H2O2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response,” Cell, vol. 79, no. 4, pp. 583–593, 1994. View at Publisher · View at Google Scholar · View at Scopus
  70. F. Mauch and R. Dudler, “Differential induction of distinct glutathione-S-transferases of wheat by xenobiotics and by pathogen attack,” Plant Physiology, vol. 102, no. 4, pp. 1193–1201, 1993. View at Scopus
  71. R. Schupp, T. Schatten, J. Willenbrink, and H. Rennenberg, “Long-distance transport of reduced sulphur in spruce (Picea abies L.),” Journal of Experimental Botany, vol. 43, no. 9, pp. 1243–1250, 1992. View at Publisher · View at Google Scholar · View at Scopus
  72. R. Desikan, E. C. Burnett, J. T. Hancock, and S. J. Neill, “Harpin and hydrogen peroxide induce the expression of a homologue of gp91-phox in Arabidopsis thaliana suspension cultures,” Journal of Experimental Botany, vol. 49, no. 327, pp. 1767–1771, 1998. View at Scopus
  73. Z. Chen, H. Silva, and D. F. Klessig, “Active oxygen species in the induction of plant systemic acquired resistance by salicylic acid,” Science, vol. 262, no. 5141, pp. 1883–1886, 1993. View at Scopus
  74. H. Lopez-Delgado, J. F. Dat, C. H. Foyer, and I. M. Scott, “Induction of thermotolerance in potato microplants by acetylsalicylic acid and H2O2,” Journal of Experimental Botany, vol. 49, no. 321, pp. 713–720, 1998. View at Scopus
  75. G. Wu, B. J. Shortt, E. B. Lawrence et al., “Activation of host defense mechanisms by elevated production of H2O2 in transgenic plants,” Plant Physiology, vol. 115, no. 2, pp. 427–435, 1997. View at Scopus
  76. S. Chamnongpol, H. Willekens, W. Moeder et al., “Defense activation and enhanced pathogen tolerance induced by H2O2 in transgenic tobacco,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 10, pp. 5818–5823, 1998. View at Publisher · View at Google Scholar · View at Scopus
  77. M. E. Alvarez, R. I. Pennell, P. J. Meijer, A. Ishikawa, R. A. Dixon, and C. Lamb, “Reactive oxygen intermediates mediate a systemic signal network in the establishment of plant immunity,” Cell, vol. 92, no. 6, pp. 773–784, 1998. View at Publisher · View at Google Scholar · View at Scopus
  78. H. J. Park, Y. Miura, K. Kawakita, H. Yoshioka, and N. Doke, “Physiological mechanisms of a sub-systemic oxidative burst triggered by elicitor-induced local oxidative burst in potato tuber slices,” Plant and Cell Physiology, vol. 39, no. 11, pp. 1218–1225, 1998.
  79. T. Jabs, “Reactive oxygen intermediates as mediators of programmed cell death in plants and animals,” Biochemical Pharmacology, vol. 57, no. 3, pp. 231–245, 1999. View at Publisher · View at Google Scholar · View at Scopus
  80. T. Jabs, R. A. Dietrich, and J. L. Dangl, “Initiation of runaway cell death in an Arabidopsis mutant by extracellular superoxide,” Science, vol. 273, no. 5283, pp. 1853–1856, 1996. View at Scopus
  81. J. P. Wisniewski, P. Cornille, J. P. Agnel, and J. L. Montillet, “The extensin multigene family responds differentially to superoxide or hydrogen peroxide in tomato cell cultures,” FEBS Letters, vol. 447, no. 2-3, pp. 264–268, 1999. View at Publisher · View at Google Scholar · View at Scopus
  82. T. Vellosillo, J. Vicente, S. Kulasekaran, M. Hamberg, and C. Castresana, “Emerging complexity in reactive oxygen species production and signaling during the response of plants to pathogens,” Plant Physiology, vol. 154, no. 2, pp. 444–448, 2010. View at Publisher · View at Google Scholar · View at Scopus
  83. R. I. Pennell and C. Lamb, “Programmed cell death in plants,” Plant Cell, vol. 9, no. 7, pp. 1157–1168, 1997. View at Publisher · View at Google Scholar · View at Scopus
  84. R. Desikan, J. T. Hancock, K. Ichimura, K. Shinozaki, and S. J. Neill, “Harpin induces activation of the arabidopsis mitogen-activated protein kinases AtMPK4 and AtMPK6,” Plant Physiology, vol. 126, no. 4, pp. 1579–1587, 2001. View at Publisher · View at Google Scholar · View at Scopus
  85. H. Hirt, “MAP kinases in plant signal transduction,” in Results and Problems of Cell Differentiation, vol. 27, Springer, Berlin, Germany, 2000.
  86. M. E. Alveraz and C. Lamb, “Oxidative burst-mediated defense responses in plant disease resistance,” in Oxidative Stress and the Molecular Biology of Antioxidant Defenses, J. G. Scandalios, Ed., pp. 815–839, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, USA, 1997.
  87. R. Mittler and B. A. Zilinskas, “Molecular cloning and characterization of a gene encoding pea cytosolic ascorbate peroxidase,” Journal of Biological Chemistry, vol. 267, no. 30, pp. 21802–21807, 1992. View at Scopus
  88. S. Neill, R. Desikan, A. Clarke, and J. Harcock, “H2O2 signaling in plant cells,” in Plant Responses to Environmental Stress, M. F. Smallwood, C. M. Calvert, and D. J. Bowles, Eds., pp. 59–64, BIOS Scientific Publishers, Oxford, UK, 1999.
  89. R. I. Pennell and C. Lamb, “Programmed cell death in plants,” Plant Cell, vol. 9, no. 7, pp. 1157–1168, 1997. View at Publisher · View at Google Scholar · View at Scopus
  90. K. Overmyer, H. Tuominen, R. Kettunen et al., “Ozone-sensitive Arabidopsis rcd1 mutant reveals opposite roles for ethylene and jasmonate signaling pathways in regulating superoxide-dependent cell death,” Plant Cell, vol. 12, no. 10, pp. 1849–1862, 2000. View at Publisher · View at Google Scholar · View at Scopus
  91. J. P. Reichheld, T. Vernoux, F. Lardon, M. Van Montagu, and D. Inzé, “Specific checkpoints regulate plant cell cycle progression in response to oxidative stress,” Plant Journal, vol. 17, no. 6, pp. 647–656, 1999. View at Publisher · View at Google Scholar · View at Scopus
  92. R. Sánchez-Fernández, M. Fricker, L. B. Corben et al., “Cell proliferation and hair tip growth in the Arabidopsis root are under mechanistically different forms of redox control,” Proceedings of the National Academy of Sciences of the United States of America, vol. 94, no. 6, pp. 2745–2750, 1997. View at Publisher · View at Google Scholar · View at Scopus
  93. C. Kairong, X. Gengsheng, L. Xinmin, X. Gengmei, and W. Yafu, “Effect of hydrogen peroxide on somatic embryogenesis of Lycium barbarum L.,” Plant Science, vol. 146, no. 1, pp. 9–16, 1999. View at Publisher · View at Google Scholar · View at Scopus
  94. J. H. Joo, Y. S. Bae, and J. S. Lee, “Role of auxin-induced reactive oxygen species in root gravitropism,” Plant Physiology, vol. 126, no. 3, pp. 1055–1060, 2001. View at Publisher · View at Google Scholar · View at Scopus
  95. R. Mahalingam and N. Fedoroff, “Stress response, cell death and signalling: the many faces of reactive oxygen species,” Physiologia Plantarum, vol. 119, no. 1, pp. 56–68, 2003. View at Publisher · View at Google Scholar
  96. P. V. Mylona and A. N. Polidoros, “ROS regulation and antioxidant genes,” in Reactive Oxygen Species and Antioxidants in Higher Plants, S. Dutta Gupta, Ed., pp. 1–30, CRC Press, New York, NY, USA, 2010.
  97. B. N. Kunkel and D. M. Brooks, “Cross talk between signaling pathways in pathogen defense,” Current Opinion in Plant Biology, vol. 5, no. 4, pp. 325–331, 2002. View at Publisher · View at Google Scholar · View at Scopus
  98. R. G. Allen and M. Tresini, “Oxidative stress and gene regulation,” Free Radical Biology & Medicine, vol. 28, pp. 463–499, 2002.
  99. R. Desikan, S. J. Neill, J. Slinn, and J. T. Hancock, “Tools to investigate reaction oxygen species-sensitive signaling proteins,” Methods in Molecular Biology, vol. 476, pp. 87–99, 2008. View at Scopus
  100. G. Noctor and C. H. Foyer, “Ascorbate and glutathione: keeping active oxygen species under control,” Annual Review of Plant Physiology and Plant Molecular Biology, vol. 49, pp. 249–279, 1999.
  101. N. Rouhier, S. D. Lemaire, and J. P. Jacquot, “The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation,” Annual Review of Plant Biology, vol. 59, pp. 143–166, 2008. View at Publisher · View at Google Scholar · View at Scopus
  102. A. Nishiyama, H. Masutani, H. Nakamura, Y. Nishinaka, and J. Yodoi, “Redox regulation by thioredoxin and thioredoxin-binding proteins,” IUBMB Life, vol. 52, no. 1-2, pp. 29–33, 2001. View at Publisher · View at Google Scholar · View at Scopus
  103. S. Kuge, N. Jones, and A. Nomoto, “Regulation of yAP-1 nuclear localization in response to oxidative stress,” EMBO Journal, vol. 16, no. 7, pp. 1710–1720, 1997. View at Publisher · View at Google Scholar · View at Scopus
  104. E. Rulland and M. Miginiac-Maslow, “Regulation of chloroplast enzyme activities by thioredoxins: activation nor relief from inhibition?” Trends in Plant Science, vol. 4, pp. 136–144, 1993.
  105. V. Daniel, “Glutathione S-transferases: gene structure and regulation of expression,” Critical Reviews in Biochemistry and Molecular Biology, vol. 28, no. 3, pp. 173–178, 1993.
  106. K. A. Marrs, “The functions and regulation of glutathione s-transferases in plants,” Annual Review of Plant Physiology and Plant Molecular Biology, vol. 47, no. 1, pp. 127–158, 1996. View at Scopus
  107. J. Chen and P. B. Goldborough, “Increased activity of γ—glutamylcystine synthetase in tomato cells selected for cadmium tolerance,” Plant Physiology, vol. 106, pp. 233–239, 1994.
  108. M. J. May and C. J. Leaver, “Oxidative stimulation of glutathione synthesis in Arabidopsis thaliana suspension cultures,” Plant Physiology, vol. 103, no. 2, pp. 621–627, 1993. View at Scopus
  109. R. C. Leegood, “Enzymes of Calvin cycle,” in Methods in Plant Biochemistry, P. J. Lea, Ed., vol. 3, pp. 15–38, Academic Press, New York, NY, USA, 1990.
  110. C. Godon, G. Lagniel, J. Lee et al., “The H2O2 stimulon in Saccharomyces cerevisiae,” Journal of Biological Chemistry, vol. 273, no. 35, pp. 22480–22489, 1998. View at Publisher · View at Google Scholar · View at Scopus
  111. E. Varnová, F. Van Brcusegem, J. Dat, E. Belles-Bolx, and D. Inzé, The role of reactive oxygen species in signal transduction, Oxford University Press, New York, NY, USA, 2002.
  112. G. Storz and J. A. Imlay, “Oxidative stress,” Current Opinion in Microbiology, vol. 2, no. 2, pp. 188–194, 1999. View at Publisher · View at Google Scholar
  113. J. F. Allen, “Redox control of transcription: sensors, response regulators, activators and repressors,” FEBS Letters, vol. 332, no. 3, pp. 203–207, 1993. View at Publisher · View at Google Scholar · View at Scopus
  114. D. J. Jamieson, “Oxidative stress responses of the yeast Saccharomyces cerevisiae,” Yeast, vol. 14, no. 16, pp. 1511–1527, 1998. View at Publisher · View at Google Scholar · View at Scopus
  115. S. Kuge, N. Jones, and A. Nomoto, “Regulation of yAP-1 nuclear localization in response to oxidative stress,” EMBO Journal, vol. 16, no. 7, pp. 1710–1720, 1997. View at Publisher · View at Google Scholar · View at Scopus
  116. A. P. Arrigo, “Gene expression and the thiol redox state,” Free Radical Biology and Medicine, vol. 27, no. 9-10, pp. 936–944, 1999. View at Publisher · View at Google Scholar · View at Scopus
  117. R. Desikan, S. J. Neill, and J. T. Hancock, “Hydrogen peroxide-induced gene expression in Arabidopsis thaliana,” Free Radical Biology and Medicine, vol. 28, no. 5, pp. 773–778, 2000. View at Publisher · View at Google Scholar
  118. R. Desikan, A. Clarke, J. T. Hancock, and S. J. Neill, “H2O2 activates a MAP kinase-like enzyme in Arabidopsis thaliana suspension cultures,” Journal of Experimental Botany, vol. 50, no. 341, pp. 1863–1866, 1999. View at Scopus
  119. V. Daniel, “Glutathione S-transferases: gene structure and regulation of expression,” Critical Reviews in Biochemistry and Molecular Biology, vol. 28, no. 3, pp. 173–207, 1993.
  120. R. S. Friling, S. Bergelson, and V. Daniel, “Two adjacent AP-1-like binding sites form the electrophile-responsive element of the murine glutathione S-transferase Ya subunit gene,” Proceedings of the National Academy of Sciences of the United States of America, vol. 89, no. 2, pp. 668–672, 1992. View at Scopus
  121. W. Chen, G. Chao, and K. B. Singh, “The promoter of a H2O2-inducible, Arabidopsis glutathione S-transferase gene contains closely linked OBF- and OBP1-binding sites,” Plant Journal, vol. 10, no. 6, pp. 955–966, 1996. View at Scopus
  122. W. Chen and K. B. Singh, “The auxin, hydrogen peroxide and salicylic acid induced expression of the Arabidopsis GST6 promoter is mediated in part by an ocs element,” Plant Journal, vol. 19, no. 6, pp. 667–677, 1999. View at Publisher · View at Google Scholar · View at Scopus
  123. A. N. Polidoros and J. G. Scandalios, “Role of hydrogen peroxide and different classes of antioxidants in the regulation of catalase and glutathione S-transferase gene expression in maize (Zea mays L.),” Physiologia Plantarum, vol. 106, no. 1, pp. 112–120, 1999. View at Publisher · View at Google Scholar
  124. K. C. Lin, P. C. Sun, and P. L. Lin, “Production of reactive oxygen species and induction of signaling pathways for the ACO gene expressions in tomato plants triggered by the volatile organic compound ether,” Plant Cell Reports, vol. 30, no. 4, pp. 599–611, 2011. View at Publisher · View at Google Scholar · View at Scopus
  125. A. E. Menkens, U. Schindler, and A. R. Cashmore, “The G-box: a ubiquitous regulatory DNA element in plants bound by the GBF family of bZlP proteins,” Trends in Biochemical Sciences, vol. 20, no. 12, pp. 506–510, 1995. View at Publisher · View at Google Scholar · View at Scopus
  126. V. P. M. Wingate, M. A. Lawton, and C. J. Lamb, “Glutathione causes a massive and selective induction of plant defense genes,” Plant Physiology, vol. 87, pp. 206–211, 1988.
  127. E. Mayda, P. Tornero, V. Conejero, and P. Vera, “A tomato homeobox gene (HD-Zip) is involved in limiting the spread of programmed cell death,” Plant Journal, vol. 20, no. 5, pp. 591–600, 1999. View at Publisher · View at Google Scholar · View at Scopus
  128. A. P. Arrigo, “Gene expression and the thiol redox state,” Free Radical Biology and Medicine, vol. 27, no. 9-10, pp. 936–944, 1999. View at Publisher · View at Google Scholar · View at Scopus
  129. B. B. Buchanon, “Role of light in regulation of chloroplastic enzymes,” Annual Review of Plant Physiology, vol. 31, pp. 341–374, 1980.
  130. P. J. Hogg, “Disulfide bonds as switches for protein function,” Trends in Biochemical Sciences, vol. 28, no. 4, pp. 210–214, 2003. View at Publisher · View at Google Scholar · View at Scopus
  131. J. Imsande, “Iron-sulfur clusters: formation, perturbation, and physiological functions,” Plant Physiology and Biochemistry, vol. 37, no. 2, pp. 87–97, 1999. View at Scopus
  132. A. V. Vener, I. Ohad, and B. Andersson, “Protein phosphorylation and redox sensing in chloroplast thylakoids,” Current Opinion in Plant Biology, vol. 1, no. 3, pp. 217–223, 1998. View at Scopus
  133. T. Pfannschmidt, A. Nilsson, and J. F. Allen, “Photosynthetic control of chloroplast gene expression,” Nature, vol. 397, no. 6720, pp. 625–628, 1999. View at Publisher · View at Google Scholar · View at Scopus
  134. S. Karpinski, C. Escobar, B. Karpinska, G. Creissen, and P. M. Mullineaux, “Photosynthetic electron transport regulates the expression of cytosolic ascorbate peroxidase genes in arabidopsis during excess light stress,” Plant Cell, vol. 9, no. 4, pp. 627–640, 1997. View at Publisher · View at Google Scholar · View at Scopus
  135. D. V. Lynch and J. E. Thompson, “Lipoxygenase-mediated production of superoxide anion in senescing plant tissue,” FEBS Letters, vol. 173, no. 1, pp. 251–254, 1984. View at Scopus
  136. G. W. Winston, “Physicochemical basis of free radical formation in cells: production and defenses,” in Stress Responses in Plants: Adaptation and Acclimation Mechanisms, W. Smallwood, Ed., pp. 57–86, Willey Liss, 1990.
  137. S. D. Aust, C. E. Moorehouse, and C. EThomas, “Role of metals in oxygen radical reactions,” Free Radical Biology & Medicine, vol. 1, pp. 3–25, 1995.
  138. I. Feussner and C. Wasternack, “The lipoxygenase pathway,” Annual Review of Plant Biology, vol. 53, pp. 275–297, 2004.
  139. G. Spiteller, “The relationship between changes in the cell wall, lipid peroxidation, proliferation, senescence and cell death,” Physiologia Plantarum, vol. 119, no. 1, pp. 5–18, 2003. View at Publisher · View at Google Scholar · View at Scopus
  140. J. J. M. C. deGroot, G. A. Veldink, J. F. C. Velegenthart, J. J. Boldingh, R. Wever, and B. F. van Gelder, “Demonstration of EPR spectroscopy of the functional role of iron in soyabean lipoxygenase,” Biochimica et Biophysica Acta, vol. 377, pp. 71–79, 1975.
  141. T. Jabs, “Reactive oxygen intermediates as mediators of programmed cell death in plants and animals,” Biochemical Pharmacology, vol. 57, no. 3, pp. 231–245, 1999. View at Publisher · View at Google Scholar · View at Scopus
  142. H. Spreitzer, J. Schmidt, and G. Spiteller, “Comparative analysis of fatty acid fraction of vegetables in dependence on preliminary treatment,” Fett Wissenschaft Technologie, vol. 91, pp. 108–113, 1989.
  143. K. D. Chapman, “Phospholipase activity during plant growth and development and in response to environmental stress,” Trends in Plant Science, vol. 3, no. 11, pp. 419–426, 1998. View at Publisher · View at Google Scholar · View at Scopus
  144. S. Dhondt, P. Geoffroy, B. A. Stelmach, M. Legrand, and T. Heitz, “Soluble phospholipase A2 activity is induced before oxylipin accumulation in tobacco mosaic virus-infected tobacco leaves and is contributed by patatin-like enzymes,” Plant Journal, vol. 23, no. 4, pp. 431–440, 2000. View at Publisher · View at Google Scholar · View at Scopus
  145. A. Banaś', I. Johansson, and S. Stymne, “Plant microsomal phospholipases exhibit preference for phosphatidylcholine with oxygenated acyl groups,” Plant Science, vol. 84, no. 2, pp. 137–144, 1992. View at Scopus
  146. A. Miralto, G. Barone, G. Romano et al., “The insidious effect of diatoms on copepod reproduction,” Nature, vol. 402, no. 6758, pp. 173–176, 1999. View at Publisher · View at Google Scholar · View at Scopus
  147. J. E. Thompson, R. E. Legge, and R. F. Barber, “Role of free radicals in senescence and wounding,” New Phytologist, vol. 105, pp. 313–344, 1987.
  148. G. Spiteller, “Lipid peroxidation in aging and age-dependent diseases,” Experimental Gerontology, vol. 36, no. 9, pp. 1425–1457, 2001. View at Publisher · View at Google Scholar · View at Scopus
  149. Q. F. Gan, G. L. Witkop, D. L. Sloane, K. M. Straub, and E. Sigal, “Identification of a specific methionine in mammalian 15-lipoxygenase which is oxygenated by the enzyme product 13-HPODE: dissociation of sulfoxide formation from self-inactivation,” Biochemistry, vol. 34, no. 21, pp. 7069–7079, 1995. View at Publisher · View at Google Scholar · View at Scopus
  150. C. Fuchs and G. Spiteller, “Iron release from the active site of lipoxygenase,” Zeitschrift fur Naturforschung, vol. 55, no. 7-8, pp. 643–648, 2000. View at Scopus
  151. P. Spiteller and G. Spiteller, “9-Hydroxy-10,12-octadecadienoic acid (9-HODE) and 13-hydroxy-9,11-octadecadienoic acid (13-HODE): excellent markers for lipid peroxidation,” Chemistry and Physics of Lipids, vol. 89, no. 2, pp. 131–139, 1997. View at Publisher · View at Google Scholar · View at Scopus
  152. T. Wang and W. S. Powell, “Increased levels of monohydroxy metabolites of arachidonic acid and linoleic acid in LDL and aorta from atherosclerotic rabbits,” Biochimica et Biophysica Acta, vol. 1084, no. 2, pp. 129–138, 1991. View at Publisher · View at Google Scholar
  153. H. Kuhn, R. Wiesner, L. Alder, and T. Schewe, “Occurrence of free and esterified lipoxygenase products in leaves of Glechoma hederacea L. and other Labiatae,” European Journal of Biochemistry, vol. 186, no. 1-2, pp. 155–162, 1989. View at Publisher · View at Google Scholar · View at Scopus
  154. A. Miralto, G. Barone, G. Romano et al., “The insidious effect of diatoms on copepod reproduction,” Nature, vol. 402, no. 6758, pp. 173–176, 1999. View at Publisher · View at Google Scholar · View at Scopus
  155. W. Grosch, “Lipid degradation products and flavor,” in Food Flavours, I. D. Morton and A. J. Mac Leod, Eds., pp. 325–398, Elsevier, Amsterdam, The Netherlands, 1982.
  156. K. E. Stremler, D. M. Stafforini, S. M. Prescott, G. A. Zimmerman, and T. M. McIntyre, “An oxidized derivative of phosphatidylcholine is a substrate for the platelet-activating factor acetylhydrolase from human plasma,” Journal of Biological Chemistry, vol. 264, no. 10, pp. 5331–5334, 1989. View at Scopus