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Mechanism of paraquat tolerance in cucumber leaves of various ages

Published online by Cambridge University Press:  20 January 2017

Yong In Kuk ,
Ji-San Shin ,
Ha Il Jung ,
Ja Ock Guh ,
Sunyo Jung  and
Nilda R. Burgos
Ji-San Shin
Affiliation:
Faculty of Applied Plant Science, Chonnam National University, Gwangju 500-757, South Korea
Ha Il Jung
Affiliation:
Faculty of Applied Plant Science, Chonnam National University, Gwangju 500-757, South Korea
Ja Ock Guh
Affiliation:
Faculty of Applied Plant Science, Chonnam National University, Gwangju 500-757, South Korea
Sunyo Jung
Affiliation:
Faculty of Applied Plant Science, Chonnam National University, Gwangju 500-757, South Korea
Nilda R. Burgos
Affiliation:
Department of Crop, Soil, and Environmental Sciences, University of Arkansas, Fayetteville, AR 72704
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Abstract

Differential sensitivity to paraquat was observed between cucumber cultivars and leaf age. Physiological responses to paraquat, including antioxidative enzyme activity, were investigated in leaf age classes of cucumber to identify mechanisms of paraquat tolerance. Leaf injury for ‘Naeseosamcheok’, ‘Daehandadagi’, ‘Baekgwangdadagi’, ‘Sangrokheukjinju’, and ‘Eunseongbaekdadagi’ cultivars was less than that of six other cultivars tested, averaged over leaf age and herbicide rate. The level of foliar injury caused by paraquat was Leaf 1 > 2 > 3 > 4 in seven of 11 cultivars used, where 4 was the youngest leaf. There was a positive correlation between leaf age and its relative susceptibility to paraquat, regardless of growth stage. Lipid peroxidation was less in the youngest leaf (Leaf 4) than in the older leaves at all herbicide concentrations. The youngest leaf had higher values for apparent photosynthesis than the oldest leaf. Differential leaf response to paraquat was partially correlated with the change in superoxide dismutase, ascorbate peroxidant, and glutathione reductase activities in treated leaves. Enzyme activity of ascorbate peroxidase (APX) was higher in Leaf 4 than in Leaves 1, 2, or 3 in untreated plants and after exposure to paraquat. APX isozymes were more abundant in treated than in untreated leaves and produced in higher amounts in younger than in older leaves. Application of ascorbate and glutathione before paraquat treatment protected cucumber leaves from paraquat injury.

Keywords

Paraquatcucumber, Cucumis sativus L.Antioxidative enzymelipid peroxidationphotosynthesis
Type
Physiology, Chemistry, and Biochemistry
Information
Weed Science , Volume 54 , Issue 1 , February 2006 , pp. 6 - 15
Copyright
Copyright © Weed Science Society of America 

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References

Literature Cited

Amsellem, Z., Jansen, M. A. K., Dreisenaar, A. R. J., and Gressel, J. 1993. Developmental variability of photooxidative stress tolerance in paraquat-resistant Conyza. Plant Physiol 103:1097–1106.CrossRefGoogle ScholarPubMed
Anderson, M. D., Prasad, T. K., and Stewart, C. R. 1995. Changes in isozyme profiles of catalase, peroxidase, and glutathione reductase during acclimation to chilling in mesocotyls of maize seedlings. Plant Physiol 109:1247–1257.CrossRefGoogle ScholarPubMed
Asada, K. 1994. Mechanisms for scavenging reactive molecules generated in chloroplasts under light stress. Pages 129–140 in Baker, N. R. ed. Photoinhibition of Photosynthesis. Washington, DC: Bios Scientific Publishers.Google Scholar
Bhargava, S. 1993. Paraquat tolerance in a photomixotrophic culture of Chenopodium rubrum . Plant Cell Rep 12:230–232.Google Scholar
Bishop, T., Powles, S. B., and Cornic, G. 1987. Mechanism of paraquat resistance in Hordeum glaucum, II: paraquat uptake and translocation. Aust. J. Plant Physiol 14:539–547.Google Scholar
Bowler, C., Slooten, L., Vandenbranden, S., De Rycke, R., Botterman, J., Sybesma, C., Van Montagu, M., and Inzé, D. 1991. Manganese superoxide dismutase can reduce cellular damage mediated by oxygen radicals in transgenic plants. EMBO (Eur. Mol. Biol. Organ.) J 10:1723–1732.CrossRefGoogle ScholarPubMed
Bowler, C. M., Van Montagu, M., and Inzé, D. 1992. Superoxide dismutase and stress tolerance. Annu. Rev. Plant Physiol 43:83–116.CrossRefGoogle Scholar
Bradford, M. M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein-dye binding. Anal. Biochem 72:248–254.CrossRefGoogle Scholar
Buege, J. A. and Aust, S. D. 1978. Microsomal lipid peroxidation. Methods Enzymol 52:302–310.CrossRefGoogle ScholarPubMed
Casano, L. M., Martín, M., and Sabater, B. 1994. Sensitivity of superoxide dismutase transcript levels and activities to oxidative stress is lower in mature-senescent than in young barley leaves. Plant Physiol 106:1033–1039.CrossRefGoogle ScholarPubMed
Chen, G. X. and Asada, K. 1989. Ascorbate peroxidase in tea leaves: occurrence of two isozymes and the differences in their enzymatic and molecular properties. Plant Cell Physiol 30:987–998.Google Scholar
Devine, M. D., Duke, S. O., and Fedtke, C. 1993. Physiology of Herbicide Action. Indianapolis, IN: Prentice Hall PTR. Pp. 163–179.Google Scholar
Dodge, A. D. 1971. The mode of action of the bipyridylium herbicides, paraquat and diquat. Endeavour (Kidlington) 30:130–135.CrossRefGoogle ScholarPubMed
Donahue, J. L., Okpodu, C. M., Cramer, C. L., Grabau, E. A., and Alscher, R. G. 1997. Responses of antioxidants to paraquat in pea leaves: relationships to resistance. Plant Physiol 113:249–257.CrossRefGoogle ScholarPubMed
Edwards, E. A., Rawsthorne, S., and Mullineaux, P. M. 1990. Subcellular distribution of multiple forms of glutathione reductase in leaves of pea (Pisum sativum L). Planta (Berl.) 180:278–284.CrossRefGoogle ScholarPubMed
Farrington, J. A., Ebert, M., Land, E. J., and Fletcher, K. 1973. Bipyridylium quaternary salts and related compounds, V—pulse radiolysis studies of the reaction of paraquat radical with oxygen: implications for the mode of action of bipyridylium herbicides. Biochem. Biophys. Acta 314:372–381.Google Scholar
Foyer, C. H. and Mullineaux, P. 1994. Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants. Boca Raton, FL: CRC.Google Scholar
Fuerst, E. P. and Vaughn, K. C. 1990. Mechanisms of paraquat resistance. Weed Technol 4:150–156.CrossRefGoogle Scholar
Furusawa, I., Tanaka, K., Thanutong, P., Mizuguchi, A., Yazaki, M., and Asada, K. 1984. Paraquat resistant tobacco calluses with enhanced superoxide dismutase activity. Plant Cell Physiol 25:1247–1254.Google Scholar
Harper, D. B. and Harvey, B. M. R. 1978. Mechanism of paraquat tolerance in perennial ryegrass, II: role of superoxide dismutase, catalase, and peroxidase. Plant Cell Environ 1:211–215.CrossRefGoogle Scholar
Hart, J. H. and DiTomaso, J. M. 1994. Sequestration and oxygen radical detoxification as mechanism of paraquat resistance. Weed Sci 42:277–289.Google Scholar
Iturbe-Ormaetxe, I., Escuredo, P. R., Arrese-igor, C., and Becanna, M. 1998. Oxidative damage in pea plants exposed to water deficit or paraquat. Plant Physiol 116:173–181.CrossRefGoogle Scholar
Kenyon, W. H. and Duke, S. O. 1985. Effects of acifluorfen on endogenous antioxidants and protective enzymes in cucumber (Cucumis sativus L.) cotyledons. Plant Physiol 79:862–866.CrossRefGoogle ScholarPubMed
Kuk, Y. I., Shin, J. S., Chung, J. S., Kwon, O. D., Kim, D. K., Han, O., and Guh, J. O. 2003. Differential tolerances and their mechanism on the response of tobacco (Nicotiana tabacum L.) leaves of varying ages to protoporphyrinogen oxidase-inhibiting herbicides and paraquat. Kor. J. Weed Sci 23:100–111.Google Scholar
Kunert, K. J. 1984. Herbicide-induced lipid peroxidation in higher plants: the role of vitamin C. Pages 383–386 in Bors, W. ed. Oxygen Radicals in Chemistry and Biology. Berlin: Walter de Gruyter.CrossRefGoogle Scholar
Kurepa, J., Hérouart, D., Van Montagu, M., and Inzé, D. 1997. Differential expression of CuZn- and Fe-superoxide dismutase genes of tobacco during development, oxidative stress, and hormonal treatment. Plant Cell Physiol 38:463–470.CrossRefGoogle Scholar
Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4 . Nature 227:680–685.CrossRefGoogle ScholarPubMed
Lee, E. H. and Bennett, J. H. 1982. Superoxide dismutase: a possible protective enzyme against ozone injury in snap beans (Phaseolus vulgaris L). Plant Physiol 69:1444–1469.Google Scholar
Madamanchi, N. R., Anderson, J. V., Alscher, R. G., Cramer, C. L., and Hess, J. L. 1992. Purification of multiple forms of glutathione reductase from pea (Pisum sativum L.) seedlings and enzyme levels in ozone fumigated pea leaves. Plant Physiol 100:138–145.Google Scholar
Matters, G. L. and Scandalios, J. G. 1986. Effect of the free radical-generating herbicide paraquat on the expression of the superoxide dismutase (SOD) genes in maize. Biochem. Biophys. Acta 882:29–38.CrossRefGoogle ScholarPubMed
Mishra, N. P., Mishra, R. K., and Singhal, G. S. 1993. Changes in the activities of antioxidant enzymes during exposure of intact wheat leaves of strong visible light at different temperature in the presence of protein synthesis inhibitors. Plant Physiol 102:903–910.Google Scholar
Mittler, R. and Zilinskas, B. 1993. Detection of ascorbate peroxidase activity in native gels by inhibition of the ascorbate-dependent reduction of nitroblue tetrazolium. Anal. Biochem 212:540–546.CrossRefGoogle ScholarPubMed
Moran, J. F., Becana, M., Iturbe-Ormaetxe, I., Frechilla, S., Klucas, R. V., and Aparicio-Tejo, P. 1994. Drought induces oxidative stress in pea plants. Planta (Berl.) 194:346–352.CrossRefGoogle Scholar
Pastori, G. M. and Trippi, V. S. 1993. Antioxidative protection in a drought-resistant maize strain during leaf senescence. Physiol. Plant 87:227–231.CrossRefGoogle Scholar
Perl-Treves, R. and Galun, E. 1991. The tomato Cu/Zn superoxide dismutase genes are developmentally regulated and respond to light and stress. Plant Mol. Biol. Int. J 17:745–760.CrossRefGoogle ScholarPubMed
Rabinowitch, H. D. and Fridovich, I. 1983. Superoxide radicals, superoxide dismutases, and oxygen toxicity in plants. Photochem. Photobiol 37:679–690.CrossRefGoogle Scholar
Rao, M. V., Paliyath, G., and Ormrod, D. P. 1996. Ultraviolet B– and ozone-induced biochemical changes in antioxidant enzymes of Arabidopsis thaliana . Plant Physiol 110:125–136.Google Scholar
[SAS] Statistical Analysis System. 2000. SA/STAT User's Guide, Version 7, Cary, NC:. Statistical Analysis System Institute, Electronic Version.Google Scholar
Scandalios, J. 1994. Molecular biology of superoxide dismutase. Pages 147–164 in Alscher, R. G. ed. Plant Responses to the Gaseous Environment: Molecular, Metabolic and Physiological Aspects. London: Butterworth.CrossRefGoogle Scholar
Schmitz-Eiberger, M. and Noga, G. 2001. Reduction of paraquat-induced oxidative stress in Phaseolus vulgaris and Malus domestica . Scientia Horticulturae 91:153–167.CrossRefGoogle Scholar
Shaaltiel, Y. and Gressel, J. 1986. Multienzyme oxygen radical detoxifying system correlated with paraquat resistance in Conyza bonariensis . Pestic. Biochem. Physiol 26:22–28.Google Scholar
Sherman, T. D., Becerril, J. M., Matsumoto, H., Duke, M. V., Jacobs, J. M., Jacobs, N. J., and Duke, S. O. 1991. Physiological basis for differential sensitivities of plant species to protoporphyrinogen oxidase-inhibiting herbicides. Plant Physiol 97:280–287.Google Scholar
Spychalla, J. P. and Desborough, S. L. 1990. Superoxide dismutase, catalase, and -tocopherol content of stored potato tubers. Plant Physiol 94:1214–1218.CrossRefGoogle ScholarPubMed
Szigeti, Z., Racz, I., Darko, E., Lasztity, D., and Lehoczki, E. 1996. Are either SOD and catalase or the polyamines involved in the paraquat resistance of Conyza Canadensis? J. Environ Sci. Health Part B Pestic. Food Contam. Agric. Wastes 31:599–604.Google Scholar
Tanaka, Y., Chisaka, H., and Saka, H. 1986. Movement of paraquat in resistant and susceptible biotypes of Erigeron philadelphicus and E. Canadensis . Physiol. Plant 66:605–608.CrossRefGoogle Scholar