Korean Journal of Medicinal Crop Science (한국약용작물학회지)

The Korean Society of Medicinal Crop Science (한국약용작물학회)
권호 표지

Antioxidant Enzyme Responses against Abiotic and Biotic Stresses in Rehmannia glutinosa L. and Glycine max L.

  • Moon, Yu-Ran (Division of Biological Resources Sci., and Institute of Agricultural Sci. and Tech., Chonbuk Natl. Univ.) ;
  • Lim, Jeong-Hyun (Division of Biological Resources Sci., and Institute of Agricultural Sci. and Tech., Chonbuk Natl. Univ.) ;
  • Park, Myoung-Ryoul (Division of Biological Resources Sci., and Institute of Agricultural Sci. and Tech., Chonbuk Natl. Univ.) ;
  • Yu, Chang-Yeon (Division of Applied Plant Sci., Kangwon Natl. Univ.) ;
  • Chung, Ill-Min (College of Agriculture & Life Sci., Konkuk Univ.) ;
  • Yang, Deok-Chun (College of Life Sci., Kyung Hee University) ;
  • Yun, Song-Joong (Division of Biological Resources Sci., and Institute of Agricultural Sci. and Tech., Chonbuk Natl. Univ.)
  • Published : 2004.11.01
Download PDF
⟨ Previous Next ⟩

Abstract

Rehmannia glutinosa shows a high level of resistance to the non-selective herbicide paraquat. To characterize the antioxidant enzyme system of R. glutinosa, we comparatively examined the responses of antioxidant enzymes to UV, wounding and a general elicitor yeast extract in R. glutinosa and soybean. The levels of enzyme activities of the two plant species were drastically different between those per fresh weight (general activity) and per protein (specific activity) bases. The general activities of superoxide dismutase (SOD), peroxidase (POX), catalase (CAT), and glutathione reductase (GR) were lower, but that of ascorbate peroxidase (APX) was higher in R. glutinosa than in soybean. The specific activities of the enzymes, however, were about two- to seven-fold higher in R. glutinosa than in soybean, except that of CAT, which was about 12-fold higher in soybean. The general and specific enzyme activities of R. glutinosa relative to those of soybean showed a consistent increase in responses to the stresses only in SOD. The specific activities of SOD and APX were higher in R. glutinosa in all stress treatments. The results might suggest a relatively higher contribution of SOD and APX to the stress tolerance.

Keywords

References

  1. Allen RD, Webb RP, Schake SA (1997) Use of transgenic plants to study antioxidant defense. Free Rad. Biol, Med. 23:73-479
  2. Aono M, Saji H, Sakamoto A, Tanaka K, Kondo N, Tanaka K (1995) Paraquat tolerance of transgenic Nicotiana tabacum with enhanced activities of glutathione reductase and superoxide dismutase. Plant Cell Physiol. 36:1687-1691
  3. Beers RF, Sizer IW (1952) A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J. Biol, Chem. 195:133-140
  4. Bradford MM (1979) 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 https://doi.org/10.1016/0003-2697(76)90527-3
  5. Chance B, Maehly AC (1955) Assay of catalase and peroxidase. Methods Enzymol. 2:764-775 https://doi.org/10.1016/S0076-6879(55)02300-8
  6. Choi DG, Yoo NH, Yu CY, de los Reyes B, Yun SJ (2004) The activities of antioxidant enzymes in response to oxidative stresses and hormones in paraquat-tolerant Rehmannia glutinosa plants. JBMB 37(5): 618-624
  7. Chun JC, Kim JC, Hwang IT, Kim SE (2002) Acteoside from Rehmannia glutinosa nullifies paraquat activity in Cucumis sativus. Pestic. Biochem. Physiol. 72:153-159 https://doi.org/10.1016/S0048-3575(02)00008-1
  8. Chung IM, Park MR, Chun JC, Yun SJ (2003) Resveratrol accumulation and resveratrol synthase gene expression in response to abiotic stresses and hormones in peanut plants. Plant Sci. 164:103-109 https://doi.org/10.1016/S0168-9452(02)00341-2
  9. Duke JA (2002) Handbook of Medicinal Herbs. CRC Press, Boca Raton
  10. Fuerst EP, Vaughn KC (1990) Mechanisms of paraquat resistance. Weed Technol. 4:150-156
  11. Gao JJ, Igalashi K, Nukina M (1999) Radical scavenging activity of phenylpropanoid glycosides in Caryopteris incana. Biosci. Biotech. Biochem. 63:983-988 https://doi.org/10.1271/bbb.63.983
  12. Hodges DM, Forney CF (2000) The effects of ethylene, depressed oxygen and elevated carbon dioxide on antioxidant profiles of senescing spinach leaves. J. Exp. Bot. 51:645-55 https://doi.org/10.1093/jexbot/51.344.645
  13. Kurepa J, Herouart D, Van Montagu M, Inze D (1997) Differential expression of CuZn- and Fe-superoxide dismutase genes of tobacco during development, oxidative stress, and hormonal treatments. Plant Cell Physiol. 38:463-470 https://doi.org/10.1093/oxfordjournals.pcp.a029190
  14. Melhorn H (1990) Ethylene-promoted ascorbate peroxidase activity protects plants against hydrogen peroxide, ozone and paraquat. Plant Cell Environ. 13:971-976 https://doi.org/10.1111/j.1365-3040.1990.tb01988.x
  15. Mittler R (2002) Oxidative stress, antioxidants and stress tolerance, Trends Plant Sci. 7:405-410 https://doi.org/10.1016/S1360-1385(02)02312-9
  16. Nakano Y, Asada K (1981) Hydrogen peroxide is scavenged by ascorbate-specific peroXidase in spinach chloroplasts. Plant Cell Physiol. 22:867-880
  17. Norman MA, Fuerst EP, Smeda RJ, Vaughn KC (1993) Evaluation of paraquat resistance mechanisms in Conyza. Pestic. Biochem. Physiol. 46:236-249 https://doi.org/10.1006/pest.1993.1055
  18. O' Kane D, Gill V, Boyd P, Burdon R (1996) Chilling, oxidative stress and antioxidant responses in Arabidopsis thaliana callus. Planta 198:371-377 https://doi.org/10.1007/BF00620053
  19. Oberley LW, Spitz DR (1984) Assay of superoxide dismutase activity in tumor tissue. Methods Enzymol. 105:457-464 https://doi.org/10.1016/S0076-6879(84)05064-3
  20. Preston C (l994) Resistance to photosystem I disrupting herbicides, in: S.B. Powles,J.A.M. Holtum, (eds.), Herbicide Resistance in Plants: Biology and Biochemistry, Lewis Publishers, Boca Raton, FL, p. 61-82
  21. Rizhsky L, Hallak-Herr E, Van Breusegem F, Rachmilevitch S, Barr JE, Rodermel S, Inze D, Mittler R (2002) Double antisense plants lacking ascorbate peroxidase and catalase are less sensitive to oxidative stress than single antisense plants lacking ascorbate peroxidase or catalase, Plant J. ??:329-342
  22. Sylvestre I, Droillard MJ, Bureau JM, Paulin A (1989) Effects of the ethylene rise on the peroxidation of membrane lipids during the senescence of cut carnations. Plant Physiol. Biochem. 27:407-413
  23. Van Breusegem F, Slooten L, Stassart]M, Moens T, Botterman J, Van Montagu M, Inze D (1999) Overproduction of Arabidopsis thaliana FeSOD confers oxidative stress tolerance to transgenic maize. Plant Cell Physiol. 40:515-523 https://doi.org/10.1093/oxfordjournals.pcp.a029572
  24. Ye B, Gressel J (2000) Transient, oxidant-induced antioxidant transcript and enzyme levels correlate with greater oxidantresistance in paraquat-resistant Conyza bonariensis. Planta 211:50-61 https://doi.org/10.1007/s004250000257