메뉴 건너뛰기




Volumn 40, Issue 6-8, 2002, Pages 577-584

Cadmium and H2O2-induced oxidative stress in Populus x canescens roots

Author keywords

Antioxidative enzymes; Heavy metal stress; Hydrogen peroxide; Oxidative stress; Populus; Root physiology

Indexed keywords

POPULUS; POPULUS ALBA; POPULUS ALBA X POPULUS TREMULA; POPULUS BEROLINENSIS; POPULUS TREMULA;

EID: 0036618906     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0981-9428(02)01411-0     Document Type: Conference Paper
Times cited : (204)

References (41)
  • 1
    • 0000024076 scopus 로고
    • Catalase
    • H. Bergmeyer (Ed.), Verlag Chemie, Weinheim
    • H. Aebi, Catalase, in: H. Bergmeyer (Ed.), Methods of Enzymatic Analysis, 3, Verlag Chemie, Weinheim, 1983, pp. 273-277.
    • (1983) Methods of Enzymatic Analysis , vol.3 , pp. 273-277
    • Aebi, H.1
  • 2
    • 0000459986 scopus 로고
    • Seasonal variation in the antioxidant system of eastern white pine
    • R.G. Anderson, B.I. Chevone, J.L. Hess, Seasonal variation in the antioxidant system of eastern white pine, Plant Physiol. 98 (1992) 501-508.
    • (1992) Plant Physiol , vol.98 , pp. 501-508
    • Anderson, R.G.1    Chevone, B.I.2    Hess, J.L.3
  • 3
    • 0034085465 scopus 로고    scopus 로고
    • Responses to cadmium in leaves of transformed poplars overexpressing gamma-glutamylcysteine synthetase
    • A.C.M. Arisi, B. Mocquot, A. Lagriffoul, M. Mench, C.H. Foyer, L. Jouanin, Responses to cadmium in leaves of transformed poplars overexpressing gamma-glutamylcysteine synthetase, Physiol. Plant 109 (2000) 143-149.
    • (2000) Physiol. Plant , vol.109 , pp. 143-149
    • Arisi, A.C.M.1    Mocquot, B.2    Lagriffoul, A.3    Mench, M.4    Foyer, C.H.5    Jouanin, L.6
  • 4
    • 0034714319 scopus 로고    scopus 로고
    • Acute cadmium exposure inactivates thioltransferase (glutaredoxin), inhibits intracellular reduction of protein-glutathionyl-mixed disulfides, and initiates apoptosis
    • C.A. Chrestensen, D.W. Starke, J.J. Mieyal, Acute cadmium exposure inactivates thioltransferase (glutaredoxin), inhibits intracellular reduction of protein-glutathionyl-mixed disulfides, and initiates apoptosis, J. Biol. Chem. 275 (2000) 26556-26565.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26556-26565
    • Chrestensen, C.A.1    Starke, D.W.2    Mieyal, J.J.3
  • 5
    • 0000746853 scopus 로고
    • Enzymatic reactions of ascorbate and glutathione that prevent peroxide damage in soybean root nodules
    • D. Dalton, S. Russell, F. Hanus, G. Pascoe, H. Evans, Enzymatic reactions of ascorbate and glutathione that prevent peroxide damage in soybean root nodules, Proc. Natl. Acad. Sci. USA 83 (1986) 3811-3815.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3811-3815
    • Dalton, D.1    Russell, S.2    Hanus, F.3    Pascoe, G.4    Evans, H.5
  • 6
    • 0030586360 scopus 로고    scopus 로고
    • Analysis of ascorbate in plant tissues by high-performance capillary zone electrophoresis
    • M.W. Davey, G. Bauw, M. van Montagu, Analysis of ascorbate in plant tissues by high-performance capillary zone electrophoresis, Anal. Chem. 239 (1996) 8-19.
    • (1996) Anal. Chem. , vol.239 , pp. 8-19
    • Davey, M.W.1    Bauw, G.2    Van Montagu, M.3
  • 7
    • 0035132066 scopus 로고    scopus 로고
    • Dimethylthiourea, a hydrogen peroxide trap, partially prevents stress effects and ascorbate peroxidase increase in spermidine-treated maize roots
    • M. De Agazio, M. Zacchini, Dimethylthiourea, a hydrogen peroxide trap, partially prevents stress effects and ascorbate peroxidase increase in spermidine-treated maize roots, Plant Cell Environ. 24 (2001) 237-244.
    • (2001) Plant Cell Environ. , vol.24 , pp. 237-244
    • De Agazio, M.1    Zacchini, M.2
  • 8
    • 0000029028 scopus 로고
    • Perchloric acid procedure for wet-ashing organics for the determination of mercury (and other metals)
    • C. Feldmann, Perchloric acid procedure for wet-ashing organics for the determination of mercury (and other metals), Anal. Chem. 46 (1974) 1606-1609.
    • (1974) Anal. Chem. , vol.46 , pp. 1606-1609
    • Feldmann, C.1
  • 9
    • 0003121376 scopus 로고
    • The presence of glutathione and glutathione reductase in chloroplasts. A proposed role in ascorbic acid metabolism
    • C.H. Foyer, B. Halliwell, The presence of glutathione and glutathione reductase in chloroplasts. A proposed role in ascorbic acid metabolism, Planta 133 (1976) 21-25.
    • (1976) Planta , vol.133 , pp. 21-25
    • Foyer, C.H.1    Halliwell, B.2
  • 10
    • 0014009764 scopus 로고
    • Kinetics of the reaction of N-ethylmaleimide with cysteine and some congeners
    • G. Gorin, P.A. Martic, G. Doughty, Kinetics of the reaction of N-ethylmaleimide with cysteine and some congeners, Anal. Biochem. Biophys. 115 (1966) 593-597.
    • (1966) Anal. Biochem. Biophys. , vol.115 , pp. 593-597
    • Gorin, G.1    Martic, P.A.2    Doughty, G.3
  • 12
    • 0016816804 scopus 로고
    • The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: Inactivation of the enzyme
    • E.K. Hodgson, I. Fridovich, The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme, Biochemistry 14 (1975) 5294-5303.
    • (1975) Biochemistry , vol.14 , pp. 5294-5303
    • Hodgson, E.K.1    Fridovich, I.2
  • 13
    • 0000918942 scopus 로고
    • Monodehydroascorbate reductase in spinach chloroplasts and its participation in the regeneration of ascorbate for scavenging hydrogen peroxide
    • M.A. Hossain, Y. Nakano, K. Asada, Monodehydroascorbate reductase in spinach chloroplasts and its participation in the regeneration of ascorbate for scavenging hydrogen peroxide, Plant Cell Physiol. 25 (1984) 385-395.
    • (1984) Plant Cell Physiol. , vol.25 , pp. 385-395
    • Hossain, M.A.1    Nakano, Y.2    Asada, K.3
  • 14
    • 0029278723 scopus 로고
    • A cadmium-sensitive glutathione deficient mutant of Arabidopsis thaliana
    • R. Howden, C. Andersen, P.B. Goldsbrough, C.S. Cobett, A cadmium-sensitive, glutathione deficient mutant of Arabidopsis thaliana, Plant Physiol. 107 (1995) 1067-1073.
    • (1995) Plant Physiol. , vol.107 , pp. 1067-1073
    • Howden, R.1    Andersen, C.2    Goldsbrough, P.B.3    Cobett, C.S.4
  • 15
    • 0027455935 scopus 로고
    • Response of roots of trees to heavy metals
    • H. Kahle, Response of roots of trees to heavy metals, Environ. Exp. Bot. 33 (1993) 99-119.
    • (1993) Environ. Exp. Bot. , vol.33 , pp. 99-119
    • Kahle, H.1
  • 16
    • 0027143463 scopus 로고
    • Oxidative stimulation of glutathione synthesis in Arabidopsis suspension cultures
    • M.J. May, C.J. Leaver, Oxidative stimulation of glutathione synthesis in Arabidopsis suspension cultures, Plant Physiol. 103 (1993) 621-627.
    • (1993) Plant Physiol. , vol.103 , pp. 621-627
    • May, M.J.1    Leaver, C.J.2
  • 17
    • 0014691242 scopus 로고
    • Superoxide dismutase: An enzyme function for erythrocuprein (hemocuprein)
    • J.M. McCord, I. Fridovich, Superoxide dismutase: an enzyme function for erythrocuprein (hemocuprein), J. Biol. Chem. 244 (1969) 6049-6055.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 18
    • 85148261600 scopus 로고    scopus 로고
    • Phytochelatins and metal tolerance
    • S.B. Agrawal, M. Agrawal (Eds.), CRC Press, Boca Raton, CA
    • R.K. Mehra, R.D. Tripathi, Phytochelatins and metal tolerance, in: S.B. Agrawal, M. Agrawal (Eds.), Environmental Pollution and Plant Responses, CRC Press, Boca Raton, CA, 2000, pp. 367-382.
    • (2000) Environmental Pollution and Plant Responses , pp. 367-382
    • Mehra, R.K.1    Tripathi, R.D.2
  • 19
    • 0029822638 scopus 로고    scopus 로고
    • Inactivation mechanism of ascorbate peroxidase at low concentrations of ascorbate: Hydrogen peroxide decomposes compound I of ascorbate peroxidase
    • C. Miyake, K. Asada, Inactivation mechanism of ascorbate peroxidase at low concentrations of ascorbate: hydrogen peroxide decomposes compound I of ascorbate peroxidase, Plant Cell Physiol. 37 (1996) 423-430.
    • (1996) Plant Cell Physiol. , vol.37 , pp. 423-430
    • Miyake, C.1    Asada, K.2
  • 20
    • 0010282460 scopus 로고
    • Hydrogen peroxide is scavenged by ascorbate-specific peroxidase in spinach chloroplast
    • Y. Nakano, K. Asada, Hydrogen peroxide is scavenged by ascorbate-specific peroxidase in spinach chloroplast, Plant Cell Physiol. 22 (1981) 860-867.
    • (1981) Plant Cell Physiol. , vol.22 , pp. 860-867
    • Nakano, Y.1    Asada, K.2
  • 21
    • 0029749087 scopus 로고    scopus 로고
    • Synthesis of glutathione in leaves of transgenic poplar overexpressing γ-glutamylcysteine synthetase
    • G. Noctor, M. Strohm, L. Jouanin, K.J. Kunert, C.H. Foyer, H. Rennenberg, Synthesis of glutathione in leaves of transgenic poplar overexpressing γ-glutamylcysteine synthetase, Plant Physiol. 112 (1996) 1071-1078.
    • (1996) Plant Physiol. , vol.112 , pp. 1071-1078
    • Noctor, G.1    Strohm, M.2    Jouanin, L.3    Kunert, K.J.4    Foyer, C.H.5    Rennenberg, H.6
  • 22
    • 0024164573 scopus 로고
    • Quantitative assessment of worldwide contamination of air, water and soils with trace metals
    • J.O. Nriagu, J.M. Pacyna, Quantitative assessment of worldwide contamination of air, water and soils with trace metals, Nature 333 (1988) 134-139.
    • (1988) Nature , vol.333 , pp. 134-139
    • Nriagu, J.O.1    Pacyna, J.M.2
  • 23
    • 0027135026 scopus 로고
    • Hydrogen peroxide and lignification
    • P.D. Olson, J.E. Varner, Hydrogen peroxide and lignification, Plant J. 4 (1993) 887-892.
    • (1993) Plant J. , vol.4 , pp. 887-892
    • Olson, P.D.1    Varner, J.E.2
  • 24
    • 0033369141 scopus 로고    scopus 로고
    • Cd-induced oxidative burst in tobacco BY2 cells: Time course, subcellular location and antioxidant response
    • A. Piqueras, E. Olmos, J.R. Martinez-Solano, E. Hellin, Cd-induced oxidative burst in tobacco BY2 cells: time course, subcellular location and antioxidant response, Free Radic. Res. 31 (1999) 33-38.
    • (1999) Free Radic. Res. , vol.31 , pp. 33-38
    • Piqueras, A.1    Olmos, E.2    Martinez-Solano, J.R.3    Hellin, E.4
  • 25
    • 0034973677 scopus 로고    scopus 로고
    • Dissecting the superoxide dismutase-ascorbate-glutathione pathway by metabolic modeling: Computer analysis as a step towards flux analysis
    • A. Polle, Dissecting the superoxide dismutase-ascorbate-glutathione pathway by metabolic modeling: computer analysis as a step towards flux analysis, Plant Physiol. 126 (2001) 445-462.
    • (2001) Plant Physiol. , vol.126 , pp. 445-462
    • Polle, A.1
  • 26
    • 0002074841 scopus 로고
    • Compartmental efflux analysis and removal of extracellular cadmium from roots
    • W.E. Rauser, Compartmental efflux analysis and removal of extracellular cadmium from roots, Plant Physiol. 85 (1987) 62-65.
    • (1987) Plant Physiol. , vol.85 , pp. 62-65
    • Rauser, W.E.1
  • 27
    • 0029608733 scopus 로고
    • Phytochelatins and related peptides. Structure, biosynthesis, and function
    • W.E. Rauser, Phytochelatins and related peptides. Structure, biosynthesis, and function, Plant Physiol. 109 (1995) 1141-1149.
    • (1995) Plant Physiol. , vol.109 , pp. 1141-1149
    • Rauser, W.E.1
  • 28
    • 0030763441 scopus 로고    scopus 로고
    • Lignification in plant cell walls
    • A. Ros-Barcelo, Lignification in plant cell walls, Int. Rev. Cytol. 176 (1997) 87-132.
    • (1997) Int. Rev. Cytol. , vol.176 , pp. 87-132
    • Ros-Barcelo, A.1
  • 30
    • 0001002420 scopus 로고
    • Diurnal changes in the glutathione content of spruce needles (Picea abies L.)
    • R. Schupp, H. Rennenberg, Diurnal changes in the glutathione content of spruce needles (Picea abies L.), Plant Sci. 57 (1988) 113-117.
    • (1988) Plant Sci. , vol.57 , pp. 113-117
    • Schupp, R.1    Rennenberg, H.2
  • 31
    • 0036001088 scopus 로고    scopus 로고
    • Plant responses to abiotic stresses: Heavy metal-induced oxidative stress and protection by mycorrhization
    • in press
    • A. Schützendübel, A. Polle, Plant responses to abiotic stresses: heavy metal-induced oxidative stress and protection by mycorrhization, J. Exp. Bot. in press (2002).
    • (2002) J. Exp. Bot.
    • Schützendübel, A.1    Polle, A.2
  • 33
    • 0029137960 scopus 로고
    • Regulation of glutathione synthesis in leaves of transgenic poplar (Populus tremula × P. alba) overexpressing glutathione synthetase
    • M. Strohm, L. Jouanin, K.J. Kunert, C. Pruvost, A. Polle, C.H. Foyer, et al., Regulation of glutathione synthesis in leaves of transgenic poplar (Populus tremula × P. alba) overexpressing glutathione synthetase, Plant J. 7 (1995) 141-145.
    • (1995) Plant J. , vol.7 , pp. 141-145
    • Strohm, M.1    Jouanin, L.2    Kunert, K.J.3    Pruvost, C.4    Polle, A.5    Foyer, C.H.6
  • 34
    • 17444451863 scopus 로고    scopus 로고
    • Cadmium effect on hydrogen peroxide, glutathione and phytochelatin levels in potato tuber
    • A. Stroinski, M. Zielezinska, Cadmium effect on hydrogen peroxide, glutathione and phytochelatin levels in potato tuber, Acta Physiol. Plant 19 (1997) 127-135.
    • (1997) Acta Physiol. Plant , vol.19 , pp. 127-135
    • Stroinski, A.1    Zielezinska, M.2
  • 35
    • 17644432094 scopus 로고    scopus 로고
    • The ROOT MERISTEMLESSI/CADMIUM SENSITIVE2 gene defines a glutathione dependent pathway involved in initiation and maintenance of cell division and during postembryonic root development
    • T. Vernoux, R. Wilson, K.A. Seeley, J.P. Reichheld, S. Muroy, S. Brown, et al., The ROOT MERISTEMLESSI/CADMIUM SENSITIVE2 gene defines a glutathione dependent pathway involved in initiation and maintenance of cell division and during postembryonic root development, Plant Cell 12 (2000) 97-109.
    • (2000) Plant Cell , vol.12 , pp. 97-109
    • Vernoux, T.1    Wilson, R.2    Seeley, K.A.3    Reichheld, J.P.4    Muroy, S.5    Brown, S.6
  • 36
    • 84989725632 scopus 로고
    • Purification and characterization of glutathione reductase from Scots pine needles
    • G. Wingsle, Purification and characterization of glutathione reductase from Scots pine needles, Physiol. Plant 76 (1989) 24-30.
    • (1989) Physiol. Plant , vol.76 , pp. 24-30
    • Wingsle, G.1
  • 37
    • 0032170826 scopus 로고    scopus 로고
    • Glutathione metabolic genes coordinately respond to heavy metals and jasmonic acid in Arabidopsis
    • C. Xiang, D.J. Oliver, Glutathione metabolic genes coordinately respond to heavy metals and jasmonic acid in Arabidopsis, Plant Cell 10 (1998) 1539-1550.
    • (1998) Plant Cell , vol.10 , pp. 1539-1550
    • Xiang, C.1    Oliver, D.J.2
  • 38
    • 0034979751 scopus 로고    scopus 로고
    • The biological functions of glutathione revisited in Arabidopsis transgenic plants with altered glutathione levels
    • C. Xiang, B. Werner, E.M. Christensen, D.J. Oliver, The biological functions of glutathione revisited in Arabidopsis transgenic plants with altered glutathione levels, Plant Physiol. 126 (2001) 564-574.
    • (2001) Plant Physiol. , vol.126 , pp. 564-574
    • Xiang, C.1    Werner, B.2    Christensen, E.M.3    Oliver, D.J.4
  • 39
    • 0030574278 scopus 로고    scopus 로고
    • Heavy metal detoxification in higher plants - A review
    • M.H. Zenk, Heavy metal detoxification in higher plants - a review, Gene 179 (1996) 21-30.
    • (1996) Gene , vol.179 , pp. 21-30
    • Zenk, M.H.1
  • 40
    • 0032838738 scopus 로고    scopus 로고
    • Overexpression of glutathione synthetase in Indian mustard enhances cadmium accumulation and tolerance
    • Y.L. Zhu, E. Pilon-Smits, L. Jouanin, N. Terry, Overexpression of glutathione synthetase in Indian mustard enhances cadmium accumulation and tolerance, Plant Physiol. 119 (1999) 73-79.
    • (1999) Plant Physiol. , vol.119 , pp. 73-79
    • Zhu, Y.L.1    Pilon-Smits, E.2    Jouanin, L.3    Terry, N.4
  • 41
    • 0001076785 scopus 로고    scopus 로고
    • Cadmium tolerance and accumulation in Indian mustard is enhanced by overexpressing gamma-glutamylcysteine synthetase
    • Y.L. Zhu, E. Pilon-Smits, A.S. Tarun, S. Weber, L. Jouanin, N. Terry, Cadmium tolerance and accumulation in Indian mustard is enhanced by overexpressing gamma-glutamylcysteine synthetase, Plant Physiol. 121 (1999) 1169-1177.
    • (1999) Plant Physiol. , vol.121 , pp. 1169-1177
    • Zhu, Y.L.1    Pilon-Smits, E.2    Tarun, A.S.3    Weber, S.4    Jouanin, L.5    Terry, N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.