Modulation of endogenous peroxidase by exogenous peroxidase in chinese red radish seedling

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Abstract

To investigate the peroxidase function and its signal pathway, activity and isozyme pattern of peroxidase and transcription level of the peroxidase gene rsprx1 and rsprx2 in Chinese red radish seedling (Raphanus sativus L.) were investigated after administration of the exogenous peroxidase (extract of radish). The activity and isozyme pattern of peroxidases were increased, among cotyledon, hypocotyl and root, the most significant increase of peroxidases activity was observed in hypocotyls, the activity of phenylalanine ammonialyase was also increased, but the pelargonidin content was decreased. Although the exogenous application of horseradish peroxidase and the extract of radish could both affect the activity of endogenous enzyme and metabolites of Chinese red radish seedlings, the latter was more effective than the former. Nifedipine, as L-calcium channel blocker, affected the activity of peroxidase and pelargonidin content in Chinese red radish seedling. Exogenously added nifedipine with the extract caused reversal of the effects. It is concluded that calcium was involved in the signal pathway of the extract of radish in Chinese red radish seedling.

Additional key words

horseradish peroxidase nifedipine pelargonidin Raphanus sativus L. 
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Literature Cited

  1. Abrahams, S., G.J. Tanner, P.J. Larkin, and A.R. Ashton. 2002. Identification and biochemical characterization of mutants in the proanthocyanidin pathway in Arabidopsis. Plant Physiol. 130:561–576.PubMedCrossRefGoogle Scholar
  2. Andrews, J., S.R. Adams, K.S. Burton, and R.N. Edmondson. 2002. Partial purification of tomato fruit peroxidase and its effect on the mechanical properties of tomato fruit skin. J. Exp. Bot. 53:2393–2399.PubMedCrossRefGoogle Scholar
  3. Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of proteindye binding. Anal. Biochem. 72:248–254.PubMedCrossRefGoogle Scholar
  4. Carpin, S., M. Crèvecoeur, H. Greppin, and C. Penel. 1999. Molecular cloning and tissue-specific expression of an anionic peroxidase in zucchini. Plant Physiol. 120:799–810.PubMedCrossRefGoogle Scholar
  5. Clementi, F. 1970. Effect of horseradish peroxidase on mice lung capillaries’ permeability. J. Histochem. Cytochem. 18:887–892.PubMedCrossRefGoogle Scholar
  6. Cosio, C., L. Vuillemin, M. De Meyer, C. Kevers, C. Penel, and C. Dunand. 2009. An anionic class III peroxidase from zucchini may regulate hypocotyl elongation through its auxin oxidase activity. Planta 229:823–836.PubMedCrossRefGoogle Scholar
  7. Fagerstedt, K.V., E.M. Kukkola, V.V. Koistinen, J. Takahashi, and K. Marjamaa. 2010. Cell wall lignin is polymerised by class III secretable plant peroxidases in Norway spruce. J. Integr. Plant Biol. 52:186–194.PubMedCrossRefGoogle Scholar
  8. Garrido, I., F. Espinosa, and M.C. álvarez-Tinaut. 2009. Oxidative defence reactions in sunflower roots induced by methyl-jasmonate and methyl-salicylate and their relation with calcium signalling. Protoplasma 237:27–39.PubMedCrossRefGoogle Scholar
  9. Gill, S.S. and N. Tuteja. 2010. Reactive oxygen species and antioxidant machinery in abiotic stress tolerance in crop plants. Plant Physiol. Biochem. 48:909–930.PubMedCrossRefGoogle Scholar
  10. González-Verdejo, C.I., X. Barandiaran, M.T. Moreno, J.I. Cubero, and A.D. Pietro. 2006. A peroxidase gene expressed during early developmental stages of the parasitic plant Orobanche ramosa. J. Exp. Bot. 57:185–192.PubMedCrossRefGoogle Scholar
  11. Han, W. and M. He. 2010. The application of exogenous cellulase to improve soil fertility and plant growth due to acceleration of straw decomposition. Bioresour. Technol. 101:3724–3731.PubMedCrossRefGoogle Scholar
  12. Hara, M., K. Oki, K. Hoshino, and T. Kuboi. 2003. Enhancement of anthocyanin biosynthesis by sugar in radish (Raphanus sativus) hypocotyl. Plant Sci. 164:259–265.CrossRefGoogle Scholar
  13. Kawano, T. 2003. Roles of the reactive oxygen species-generating peroxidase reactions in plant defense and growth induction. Plant Cell Rep. 21:829–837.PubMedGoogle Scholar
  14. Kim, H.J., F. Chen, X. Wang, and J.H. Choi. 2006. Effect of methyl jasmonate on phenolics, isothiocyanate, and metabolic enzymes in radish sprout (Raphanus sativus L.). J. Agric. Food Chem. 54:7263–7269.PubMedCrossRefGoogle Scholar
  15. Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685.PubMedCrossRefGoogle Scholar
  16. Lee, M.Y. and S.S. Kim. 1994. Characteristics of six isoperoxidases from Korean radish root. Phytochem. 35:287–290.CrossRefGoogle Scholar
  17. Manzoorim, J.L., M. Amjadi, and M. Orooji. 2006. Application of crude extract of Kohlrabi (Brassica oleracea gongylodes) as a rich source of peroxidase in the spectrofluorometric determination of hydrogen peroxide in honey samples. Anal. Sci. 22:1201–1206.CrossRefGoogle Scholar
  18. Mura, A., R. Medda, S. Longu, G. Floris, A.C. Rinaldi, and A. Padiglia. 2005. A Ca2+/calmodulin-binding peroxidase from Euphorbia latex: Novel aspects of calcium-hydrogen peroxide cross-talk in the regulation of plant defenses. Biochem. 44:14120–14130.CrossRefGoogle Scholar
  19. O’Farrell, P.H. 1975. High-resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250:4007–4021.PubMedGoogle Scholar
  20. Oren-Shamir, M. 2009. Does anthocyanin degradation play a significant role in determining pigment concentration in plants? Plant Sci. 177:310–316.CrossRefGoogle Scholar
  21. Passardi, F., C. Cosio, C. Penel, and C. Dunand. 2005. Peroxidases have more functions than a Swiss army knife. Plant Cell Rep. 24:255–265.PubMedCrossRefGoogle Scholar
  22. Pedreira J., M.T. Herrera, I. Zarra, and G. Revilla. 2011. The overexpression of AtPrx37, an apoplastic peroxidase, reduces growth in Arabidopsis. Physiol. Plant 141:177–187.PubMedCrossRefGoogle Scholar
  23. Reiss, H.D. and W. Herth. 1985. Nifedipine-sensitive calcium channels are involved in polar growth of lily pollen tubes. J. Cell Sci. 76:247–254.PubMedGoogle Scholar
  24. Scialabba, A., L.M. Bellani, and A. Dell’Aquila. 2002. Effects of aging on peroxidase activity and localization in radish (Raphanus sativus L.) seeds. Eur. J. Histochem. 46:351–358.PubMedGoogle Scholar
  25. Sreelakshmi, Y. and R. Sharma. 2008. Differential regulation of phenylalanine ammonia lyase activity and protein level by light in tomato seedlings. Plant Physiol. Biochem. 46:444–451.PubMedCrossRefGoogle Scholar
  26. Sun, Q.P., Y. Guo, Y. Sun, D.Y. Sun, and X.J. Wang. 2006. Influx of extracellular Ca2+ involved in jasmonic-acid-induced elevation of [Ca2+]cyt and JR1 expression in Arabidopsis thaliana. J. Plant Res. 119:343–350.PubMedCrossRefGoogle Scholar
  27. Tai, M.H. and B. Zipser. 2003. Extracellularly applied horseradish peroxidase increases the number of dense core vesicles in leech sensory neurons. Brain Res. 967:301–305.PubMedCrossRefGoogle Scholar
  28. Vaknin, H., A. Bar-Akiva, R. Ovadia, A. Nissim-Levi, I. Forer, D. Weiss, and M. Oren-Shamir. 2005. Active anthocyanin degradation in Brunfelsia calycina (yesterday-today-tomorrow) flowers. Planta 222:19–26.PubMedCrossRefGoogle Scholar
  29. Van der Want, J.J.L., J. Klooster, B.N. Cardozo, H. de Weerd, and R.S.B. Liem. 1997. Tract-tracing in the nervous system of vertebrates using horseradish peroxidase and its conjugates: Tracers, chromogens, and stabilization for light and electron microscopy. Brain Res. Protocols 1:269–279.CrossRefGoogle Scholar
  30. Van-Tunen, A.J. and J.N.M. Mol. 1991. Control of flavonoids synthesis and manipulation of flower color. Plant Biotechnol. 2:94–125.Google Scholar
  31. Vitrac, X., F. Larrondem, S. Krisa, A. Decendit, G. Deffieux, and J.M. Mérillon. 2000. Sugar sensing and Ca2+ -calmodulin requirement in Vitis vinifera cells producing anthocyanins. Phytochem. 53:659–665.CrossRefGoogle Scholar
  32. Waar, W.B., J.S. de Olmos, and L. Heimer. 1981. Horseradish peroxidase: The basic procedure. p. 207–262, In: L. Heimer and M.J Robards. (eds.). Neuroanatomical tract-tracing methods. Plenum Press, New York, USA.Google Scholar
  33. Wang, L., K. Burhenne, B.K. Kristensen, and S.K. Rasmussen. 2004. Purification and cloning of a Chinese red radish peroxidase that metabolise pelargonidin and forms a gene family in Brassicaceae. Gene 343:323–335.PubMedCrossRefGoogle Scholar
  34. Welinder, K.G. 1992. Superfamily of plant, fungal and bacterial peroxidases. Curr. Opin. Struc. Biol. 2:388–393.CrossRefGoogle Scholar
  35. White, P.J., H.C. Bowen, V. Demidchik, C. Nichols, and J.M. Davies. 2002. Genes for calcium-permeable channels in the plasma membrane of plant root cells. Biochim. Biophys. Acta. 1564:299–309.PubMedCrossRefGoogle Scholar

Copyright information

© Korean Society for Horticultural Science 2011

Authors and Affiliations

  1. 1.College of Life ScienceHenan Normal UniversityHenan Province, XinxiangPR China
  2. 2.Department of Medical Biotechnology, College of Biomedical ScienceKangwon National UniversityChuncheonKorea

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