메뉴 건너뛰기




Volumn 97, Issue 2, 1996, Pages 388-396

Alterations in the antioxidative system of suspension-cultured soybean cells (Glycine max) induced by oxidative stress

Author keywords

Antioxidants; antioxidative enzymes; ascorbic acid; diphenyl ether; glutathione; Glycine max; Halliwell Asada pathway; herbicide; homoglutathione; oxidative stress; oxyfluorfen; plant cell culture; soybean

Indexed keywords

GLYCINE MAX;

EID: 0030478735     PISSN: 00319317     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3054.1996.970225.x     Document Type: Article
Times cited : (285)

References (52)
  • 1
    • 0000024076 scopus 로고
    • Catalase
    • (H. U. Bergmeyer, ed.), Verlag Chemie. Weinheim. ISBN 3-527-26043-9
    • Aebi, H. E. 1983. Catalase. - In Methods of Enzymatic Analyses (H. U. Bergmeyer, ed.), Vol. 3, pp. 273-282. Verlag Chemie. Weinheim. ISBN 3-527-26043-9.
    • (1983) Methods of Enzymatic Analyses , vol.3 , pp. 273-282
    • Aebi, H.E.1
  • 2
    • 0027130081 scopus 로고
    • Developmental variability of photooxidative stress tolerance in paraquat-resistant Conyza
    • Amsellem, Z., Jansen, M. A. K., Driesenaar, A. R. J. & Gressel, J. 1993. Developmental variability of photooxidative stress tolerance in paraquat-resistant Conyza. - Plant Physiol. 103: 1097-1106.
    • (1993) Plant Physiol. , vol.103 , pp. 1097-1106
    • Amsellem, Z.1    Jansen, M.A.K.2    Driesenaar, A.R.J.3    Gressel, J.4
  • 3
    • 0002844238 scopus 로고
    • Production and action of active oxygen species in photosynthetic tissues
    • (C. H. Foyer and P. M. Mullineaux, eds), CRC Press, Boca Raton, FL. ISBN 0-8493-5443-9
    • Asada, K, 1994. Production and action of active oxygen species in photosynthetic tissues. - In Causes of Photooxidative Stress and Amelioration of Defence Systems in Plants (C. H. Foyer and P. M. Mullineaux, eds), pp. 77-104. CRC Press, Boca Raton, FL. ISBN 0-8493-5443-9.
    • (1994) Causes of Photooxidative Stress and Amelioration of Defence Systems in Plants , pp. 77-104
    • Asada, K.1
  • 5
    • 0029137110 scopus 로고
    • Antioxidant enzymes and lipid peroxidation during aging of Chrysanthemum morifolium RAM petals
    • Bartoli, C. G., Simontacchi, M., Guiamet, J. J., Montaldi, E. & Puntarulo, S. 1995. Antioxidant enzymes and lipid peroxidation during aging of Chrysanthemum morifolium RAM petals. - Plant Sci. 104: 161-168.
    • (1995) Plant Sci. , vol.104 , pp. 161-168
    • Bartoli, C.G.1    Simontacchi, M.2    Guiamet, J.J.3    Montaldi, E.4    Puntarulo, S.5
  • 6
    • 0028036292 scopus 로고
    • Detoxification of base propenals and other alpha, beta-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases
    • Berhane, K., Widersten, M., Engstrom, A., Kozarich, J. W. & Mannervick, B. 1994. Detoxification of base propenals and other alpha, beta-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases. - Proc. Natl. Acad. Sci. USA 91: 1480-1484.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1480-1484
    • Berhane, K.1    Widersten, M.2    Engstrom, A.3    Kozarich, J.W.4    Mannervick, B.5
  • 7
    • 0001144835 scopus 로고
    • Das Strukturprotein aus Chloroplasten einzelliger Grünalgen und seine Beziehung zum Chlorophyll
    • Böger, P. 1964. Das Strukturprotein aus Chloroplasten einzelliger Grünalgen und seine Beziehung zum Chlorophyll. -Flora 154: 174-211.
    • (1964) Flora , vol.154 , pp. 174-211
    • Böger, P.1
  • 8
    • 0029167393 scopus 로고
    • Peroxidizing herbicides. I. Mechanism of action
    • _ & Wakabayashi, K. 1995. Peroxidizing herbicides. I. Mechanism of action. - Z. Naturforsch. 50c: 159-166.
    • (1995) Z. Naturforsch. , vol.50 C , pp. 159-166
    • Wakabayashi, K.1
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford. M. M. 1976. 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.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 0000772902 scopus 로고
    • Chloroacetanilide herbicide selectivity: Analysis of glutathione and homoglutathione in tolerant, susceptible, and safened seedlings
    • Breaux, E. J., Patanella, J. E. & Sanders, E. F. 1987. Chloroacetanilide herbicide selectivity: Analysis of glutathione and homoglutathione in tolerant, susceptible, and safened seedlings. - J. Agric. Food Chem. 35: 474-478.
    • (1987) J. Agric. Food Chem. , vol.35 , pp. 474-478
    • Breaux, E.J.1    Patanella, J.E.2    Sanders, E.F.3
  • 11
    • 0002565973 scopus 로고
    • Biological roles of plant peroxidases: Known and potential function
    • (J. Everse, K. E. Everse and M. B. Grisham, eds), CRC Press, Boca Raton, FL. ISBN 0-8493-6964-9
    • Campa, A. 1991. Biological roles of plant peroxidases: known and potential function. - In Peroxidases in Chemistry and Biology (J. Everse, K. E. Everse and M. B. Grisham, eds), Vol. 2, pp. 25-50. CRC Press, Boca Raton, FL. ISBN 0-8493-6964-9.
    • (1991) Peroxidases in Chemistry and Biology , vol.2 , pp. 25-50
    • Campa, A.1
  • 12
    • 0011946403 scopus 로고
    • Isolation of homoglutathione and other acidic peptides from seedlings of Phaseolus aureus
    • Carnegie, P. R. 1963. Isolation of homoglutathione and other acidic peptides from seedlings of Phaseolus aureus. - Bio-chem. J. 89: 459-471.
    • (1963) Bio-chem. J. , vol.89 , pp. 459-471
    • Carnegie, P.R.1
  • 13
    • 0021149578 scopus 로고
    • Peroxidase release induced by ozone in Sedum album leaves
    • Castillo, F. J., Penel, C. & Greppin, H. 1984. Peroxidase release induced by ozone in Sedum album leaves. - Plant Physiol. 74: 846-851.
    • (1984) Plant Physiol. , vol.74 , pp. 846-851
    • Castillo, F.J.1    Penel, C.2    Greppin, H.3
  • 14
    • 77957006400 scopus 로고
    • Assay of catalases and peroxidases
    • (S. P. Colowick and N. O. Kaplan, eds), Academic Press, New York, NY
    • Chance, B. & Maehly, A. C. 1955. Assay of catalases and peroxidases. - In Methods in Enzymology (S. P. Colowick and N. O. Kaplan, eds), Vol. 2, pp. 764-775. Academic Press, New York, NY.
    • (1955) Methods in Enzymology , vol.2 , pp. 764-775
    • Chance, B.1    Maehly, A.C.2
  • 15
    • 0002865296 scopus 로고
    • Herbicide action and effects on detoxification processes
    • (C. H. Foyer and P. M. Mullineaux, eds), CRC Press, Boca Raton, FL. ISBN 0-8493-5443-9
    • Dodge, A. D. 1994. Herbicide action and effects on detoxification processes. - In Causes of Photooxidative Stress and Amelioration of Defence Systems in Plants (C. H. Foyer and P. M. Mullineaux, eds), pp. 219-236. CRC Press, Boca Raton, FL. ISBN 0-8493-5443-9.
    • (1994) Causes of Photooxidative Stress and Amelioration of Defence Systems in Plants , pp. 219-236
    • Dodge, A.D.1
  • 16
    • 0001896020 scopus 로고
    • Evidence for glutathione peroxidase activities in cultured plant cells
    • Drotar, A., Phelbs, P. & Fall, R. 1985. Evidence for glutathione peroxidase activities in cultured plant cells. - Plant Sci. 42: 35-10.
    • (1985) Plant Sci. , vol.42 , pp. 35-110
    • Drotar, A.1    Phelbs, P.2    Fall, R.3
  • 17
    • 0021014716 scopus 로고
    • Acifluorfen metabolism in soybean: Diphenylether bond cleavage and the formation of homoglutathione, cysteine, and glucose conjugates
    • Frear, D. S., Swanson, H. R. & Mansager, E. R. 1983. Acifluorfen metabolism in soybean: Diphenylether bond cleavage and the formation of homoglutathione, cysteine, and glucose conjugates. - Pestic. Biochem. Physiol. 20: 299-310.
    • (1983) Pestic. Biochem. Physiol. , vol.20 , pp. 299-310
    • Frear, D.S.1    Swanson, H.R.2    Mansager, E.R.3
  • 18
  • 19
    • 0014276538 scopus 로고
    • Nutrient requirements of cell suspension cultures of soybean root cells
    • Gamborg, O. L., Miller, R. A. & Ojima. K. 1968. Nutrient requirements of cell suspension cultures of soybean root cells. - Exp. Cell Res. 50: 151-158.
    • (1968) Exp. Cell Res. , vol.50 , pp. 151-158
    • Gamborg, O.L.1    Miller, R.A.2    Ojima, K.3
  • 20
    • 0029294106 scopus 로고
    • Ascorbate free radical reductase mRNA levels are induced by wounding
    • Grantz, A. A., Brummell, D. A. & Bennett, A. B. 1995. Ascorbate free radical reductase mRNA levels are induced by wounding. - Plant Physiol. 108: 411-418.
    • (1995) Plant Physiol. , vol.108 , pp. 411-418
    • Grantz, A.A.1    Brummell, D.A.2    Bennett, A.B.3
  • 21
    • 84951493786 scopus 로고
    • Enhanced inducibility of antioxidant systems in a Nicotiana tabacum L. biotype results in acifluorfen resistance
    • Gullner, G., Kömives, T. & Király, L. 1991. Enhanced inducibility of antioxidant systems in a Nicotiana tabacum L. biotype results in acifluorfen resistance. - Z. Naturforsch. 46c: 875-881.
    • (1991) Z. Naturforsch. , vol.46 C , pp. 875-881
    • Gullner, G.1    Kömives, T.2    Király, L.3
  • 22
    • 0002214519 scopus 로고
    • Properties and physiological function of a glutathione reductase purified from spinach leaves by affinity chromatography
    • Halliwell, B. & Foyer, C. H. 1978. Properties and physiological function of a glutathione reductase purified from spinach leaves by affinity chromatography. - Planta 139: 9-17.
    • (1978) Planta , vol.139 , pp. 9-17
    • Halliwell, B.1    Foyer, C.H.2
  • 24
    • 0002458223 scopus 로고
    • Purification of dehydroascorbate reductase from spinach and its characterization as a thiol enzyme
    • Hossain. M. A. & Asada, K. 1984. Purification of dehydroascorbate reductase from spinach and its characterization as a thiol enzyme. - Plant Cell Physiol. 25: 85-92.
    • (1984) Plant Cell Physiol. , vol.25 , pp. 85-92
    • Hossain, M.A.1    Asada, K.2
  • 25
    • 0000918942 scopus 로고
    • Monodehydroascorbate reductase in spinach chloroplasts and its participation in regeneration of ascorbate for scavenging hydrogen peroxide
    • _ , Nakano, Y. & Asada, K. 1984. Monodehydroascorbate reductase in spinach chloroplasts and its participation in regeneration of ascorbate for scavenging hydrogen peroxide. -Plant Cell Physiol. 25: 385-395.
    • (1984) Plant Cell Physiol. , vol.25 , pp. 385-395
    • Nakano, Y.1    Asada, K.2
  • 26
    • 0001139394 scopus 로고
    • Effects of acifluorfen on endogenous antioxidants and protective enzymes in cucumber (Cucumis sativus L.) cotyledons
    • Kenyon, W. H. & Duke, S. O. 1985. Effects of acifluorfen on endogenous antioxidants and protective enzymes in cucumber (Cucumis sativus L.) cotyledons. - Plant Physiol. 79: 862-866.
    • (1985) Plant Physiol. , vol.79 , pp. 862-866
    • Kenyon, W.H.1    Duke, S.O.2
  • 27
    • 84989758245 scopus 로고
    • Homoglutathione: Isolation, quantification and occurrence in legumes
    • Klapheck, S. 1988. Homoglutathione: isolation, quantification and occurrence in legumes. - Physiol. Plant. 74: 727-732.
    • (1988) Physiol. Plant. , vol.74 , pp. 727-732
    • Klapheck, S.1
  • 28
    • 0001174752 scopus 로고
    • Diphenylether herbicide metabolism in a spruce cell suspension culture: The identification of two novel metabolites derived from a glutathione conjugate
    • Lamoureux, G. L., Rusness, D. G., Schröder, P. & Rennenberg, H. 1991. Diphenylether herbicide metabolism in a spruce cell suspension culture: The identification of two novel metabolites derived from a glutathione conjugate. - Pestic. Biochem. Physiol. 39: 291-301
    • (1991) Pestic. Biochem. Physiol. , vol.39 , pp. 291-301
    • Lamoureux, G.L.1    Rusness, D.G.2    Schröder, P.3    Rennenberg, H.4
  • 29
    • 0020585306 scopus 로고
    • Glutathione and ascorbic acid in spinach (Spinacia oleracea) chloroplasts. The effect of hydrogen peroxide and of paraquat
    • Law, M. Y, Charles, S. A. & Halliwell, B. 1983. Glutathione and ascorbic acid in spinach (Spinacia oleracea) chloroplasts. The effect of hydrogen peroxide and of paraquat. -Biochem. J. 210:899-903.
    • (1983) Biochem. J. , vol.210 , pp. 899-903
    • Law, M.Y.1    Charles, S.A.2    Halliwell, B.3
  • 30
    • 0028171293 scopus 로고
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response. - Cell 79: 583-593.
    • (1994) Cell , vol.79 , pp. 583-593
    • Levine, A.1    Tenhaken, R.2    Dixon, R.3    Lamb, C.4
  • 31
    • 0023101764 scopus 로고
    • Photoreceptors and respiratory electron flow involvement in the activity of acifluorfen-methyl and LS 82-556 on nonchlorophyllous soybean cells
    • Matringe, M. & Scalla, R. 1987. Photoreceptors and respiratory electron flow involvement in the activity of acifluorfen-methyl and LS 82-556 on nonchlorophyllous soybean cells. -Pestic. Biochem. Physiol. 27: 267-274.
    • (1987) Pestic. Biochem. Physiol. , vol.27 , pp. 267-274
    • Matringe, M.1    Scalla, R.2
  • 32
    • 0000375138 scopus 로고
    • Studies on the mode of action of acifluorfen-methyl in nonchlorophyllous soybean cells
    • _ & Scalla, R. 1988, Studies on the mode of action of acifluorfen-methyl in nonchlorophyllous soybean cells. - Plant Physiol. 86: 619-622.
    • (1988) Plant Physiol. , vol.86 , pp. 619-622
    • Scalla, R.1
  • 33
    • 0024970331 scopus 로고
    • Protoporphyrinogen oxidase as a molecular target for diphenyl ether herbicides
    • _ , Camadro, J.-M., Labbe, P. & Scalla, R. 1989. Protoporphyrinogen oxidase as a molecular target for diphenyl ether herbicides. - Biochem. J. 260: 231-235.
    • (1989) Biochem. J. , vol.260 , pp. 231-235
    • Camadro, J.-M.1    Labbe, P.2    Scalla, R.3
  • 34
    • 0027951017 scopus 로고
    • Active oxygen species in plant defence against pathogens
    • Mehdy. M. C. 1994. Active oxygen species in plant defence against pathogens. - Plant Physiol. 106: 467-472.
    • (1994) Plant Physiol. , vol.106 , pp. 467-472
    • Mehdy, M.C.1
  • 36
    • 0028873575 scopus 로고
    • Development of antioxidative defence system of wheat seedlings in response to high light
    • Mishra, N. P., Fatma, T. & Singhal, G. S. 1995. Development of antioxidative defence system of wheat seedlings in response to high light. - Physiol. Plant. 95: 77-82.
    • (1995) Physiol. Plant. , vol.95 , pp. 77-82
    • Mishra, N.P.1    Fatma, T.2    Singhal, G.S.3
  • 37
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bio assays with tobacco tissue cultures
    • Murashige, T. & Skoog, F. 1962. A revised medium for rapid growth and bio assays with tobacco tissue cultures. - Physiol. Plant. 15:473-497.
    • (1962) Physiol. Plant. , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 38
    • 0010282460 scopus 로고
    • Hydrogen peroxide is scavenged by ascorbate-specific peroxidase in spinach chloroplasts
    • Nakano, Y. & Asada, K. 1981. Hydrogen peroxide is scavenged by ascorbate-specific peroxidase in spinach chloroplasts. -Plant Cell Physiol. 22: 867-880.
    • (1981) Plant Cell Physiol. , vol.22 , pp. 867-880
    • Nakano, Y.1    Asada, K.2
  • 40
    • 0029168202 scopus 로고
    • Glutathione regulation of glutathione-S-transferase and peroxidase activity in herbicide-treated Zea mays
    • Nemat Alla, M. M. 1995. Glutathione regulation of glutathione-S-transferase and peroxidase activity in herbicide-treated Zea mays. - Plant Physiol. Biochem. 33: 185-192.
    • (1995) Plant Physiol. Biochem. , vol.33 , pp. 185-192
    • Nemat Alla, M.M.1
  • 41
    • 0018887652 scopus 로고
    • An improved method for determination of L-ascorbic acid and L-dehydroascorbic acid in blood plasma
    • Okamura, M. 1980. An improved method for determination of L-ascorbic acid and L-dehydroascorbic acid in blood plasma. _ Clin. Chim. Acta 103: 259-268.
    • (1980) Clin. Chim. Acta , vol.103 , pp. 259-268
    • Okamura, M.1
  • 42
    • 0027954797 scopus 로고
    • Evidence for chilling-induced oxidative stress in maize seedlings and a regulatory role for hydrogen peroxide
    • Prasad, T. K., Anderson, M. D., Martin, B. A. & Stewart, C. R. 1994. Evidence for chilling-induced oxidative stress in maize seedlings and a regulatory role for hydrogen peroxide. _ Plant Cell 6: 65-74.
    • (1994) Plant Cell , vol.6 , pp. 65-74
    • Prasad, T.K.1    Anderson, M.D.2    Martin, B.A.3    Stewart, C.R.4
  • 43
    • 0000073130 scopus 로고
    • A new thiol in legumes
    • Price, C. A. 1957. A new thiol in legumes. - Nature 180: 148-149.
    • (1957) Nature , vol.180 , pp. 148-149
    • Price, C.A.1
  • 44
    • 0028878088 scopus 로고
    • Amelioration of ozone-induced oxidative damage in wheat plants grown under high carbon dioxide
    • Rao, M. V., Hale, B. A. & Ormrod, D. P. 1995. Amelioration of ozone-induced oxidative damage in wheat plants grown under high carbon dioxide. - Plant Physiol. 109: 421-432.
    • (1995) Plant Physiol. , vol.109 , pp. 421-432
    • Rao, M.V.1    Hale, B.A.2    Ormrod, D.P.3
  • 45
    • 0002885603 scopus 로고
    • Regulation and properties of plant catalases
    • (C. H. Foyer and P. M, Mullineaux, eds), CRC Press, Boca Raton, FL. ISBN 0-8493-5443-9
    • Scandalios, G. D. 1994. Regulation and properties of plant catalases. - In Causes of Photooxidative Stress and Amelioration of Defence Systems in Plants (C. H. Foyer and P. M, Mullineaux, eds), pp. 275-314. CRC Press, Boca Raton, FL. ISBN 0-8493-5443-9.
    • (1994) Causes of Photooxidative Stress and Amelioration of Defence Systems in Plants , pp. 275-314
    • Scandalios, G.D.1
  • 46
    • 0000714106 scopus 로고
    • Lipid peroxidation in higher plants. The role of glutathione reductase
    • Schmidt, A. & Kunert, K.-J. 1986. Lipid peroxidation in higher plants. The role of glutathione reductase. - Plant Physiol. 82: 700-702.
    • (1986) Plant Physiol. , vol.82 , pp. 700-702
    • Schmidt, A.1    Kunert, K.-J.2
  • 47
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-KB transcription factor and HIV-1
    • Schreck, R., Rieber, P. & Bäuerle, P. A. 1991. Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-KB transcription factor and HIV-1. -EMBO J. 10: 2247-2258.
    • (1991) EMBO J. , vol.10 , pp. 2247-2258
    • Schreck, R.1    Rieber, P.2    Bäuerle, P.A.3
  • 48
    • 0027209389 scopus 로고
    • Strategies of antioxidant defense
    • Sies, H. 1993. Strategies of antioxidant defense. - Eur. J. Biochem. 215: 213-219.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 213-219
    • Sies, H.1
  • 49
    • 0000788403 scopus 로고
    • Drought influences the activity of enzymes of the chloroplast hydrogen peroxide scavenging system
    • Smirnoff, N. & Colombé, S. V. 1988. Drought influences the activity of enzymes of the chloroplast hydrogen peroxide scavenging system. - J. Exp. Bot. 39: 1097-1108.
    • (1988) J. Exp. Bot. , vol.39 , pp. 1097-1108
    • Smirnoff, N.1    Colombé, S.V.2
  • 50
    • 0000751377 scopus 로고
    • Stimulation of glutathione synthesis in photorespiring plants by catalase inhibitors
    • Smith, I. K. 1985. Stimulation of glutathione synthesis in photorespiring plants by catalase inhibitors. - Plant Physiol. 79: 1044-1047.
    • (1985) Plant Physiol. , vol.79 , pp. 1044-1047
    • Smith, I.K.1
  • 51
    • 0027935268 scopus 로고
    • The redox couple between glutathione and ascorbic acid: A chemical and physiological perspective
    • Winkler, B. S., Orselli, S. M. & Rex, T. S. 1994. The redox couple between glutathione and ascorbic acid: A chemical and physiological perspective. - Free Rad. Biol. Med. 17: 333-349.
    • (1994) Free Rad. Biol. Med. , vol.17 , pp. 333-349
    • Winkler, B.S.1    Orselli, S.M.2    Rex, T.S.3
  • 52
    • 0028151722 scopus 로고
    • Constitutive variation of ascorbate peroxidase activity during development parallels that of superoxide dismutase and glutathione reductase in paraquatresistant Conyza
    • Ye, B. & Gressel, J. 1994. Constitutive variation of ascorbate peroxidase activity during development parallels that of superoxide dismutase and glutathione reductase in paraquatresistant Conyza. - Plant Sci. 102: 147-151.
    • (1994) Plant Sci. , vol.102 , pp. 147-151
    • Ye, B.1    Gressel, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.