메뉴 건너뛰기




Volumn 55, Issue 399, 2004, Pages 1105-1113

Salinity up-regulates the antioxidative system in root mitochondria and peroxisomes of the wild salt-tolerant tomato species Lycopersicon pennellii

Author keywords

Ascorbate; Ascorbate glutathione cycle enzymes; Glutathione; Mitochondria; Oxidative stress; Peroxisomes; Roots; Salinity; Tomato

Indexed keywords

ANTIOXIDANTS; CATALYST ACTIVITY; ENZYME KINETICS; LIPIDS; OXIDATION; SALTS;

EID: 2442444152     PISSN: 00220957     EISSN: None     Source Type: Journal    
DOI: 10.1093/jxb/erh113     Document Type: Article
Times cited : (401)

References (52)
  • 1
    • 0000459986 scopus 로고
    • Seasonal variation in the antioxidant system of eastern white pine needles
    • Anderson JV, Chevone BI, Hess JL. 1992. Seasonal variation in the antioxidant system of eastern white pine needles. Plant Physiology 98, 501-508.
    • (1992) Plant Physiology , vol.98 , pp. 501-508
    • Anderson, J.V.1    Chevone, B.I.2    Hess, J.L.3
  • 2
    • 0034126442 scopus 로고    scopus 로고
    • Ascorbate biosynthesis in mitochondria is linked to the electron transport chain between complexes III and IV
    • Bartoli CG, Pastori GM, Foyer CH. 2000. Ascorbate biosynthesis in mitochondria is linked to the electron transport chain between complexes III and IV. Plant Physiology 123, 335-343.
    • (2000) Plant Physiology , vol.123 , pp. 335-343
    • Bartoli, C.G.1    Pastori, G.M.2    Foyer, C.H.3
  • 3
    • 0034055539 scopus 로고    scopus 로고
    • Expression and activity of isoenzymes of superoxide dismutase in wheat roots in response to hypoxia and anoxia
    • Biemelt S, Keetman U, Mock HP, Grimm B. 2000. Expression and activity of isoenzymes of superoxide dismutase in wheat roots in response to hypoxia and anoxia. Plant, Cell and Environment 23, 135-144.
    • (2000) Plant, Cell and Environment , vol.23 , pp. 135-144
    • Biemelt, S.1    Keetman, U.2    Mock, H.P.3    Grimm, B.4
  • 4
    • 0021288856 scopus 로고
    • Determination of the production of superoxide radicals and hydrogen peroxide in mitochondria
    • Boveris A. 1984. Determination of the production of superoxide radicals and hydrogen peroxide in mitochondria. Methods in Enzymology 105, 429-435.
    • (1984) Methods in Enzymology , vol.105 , pp. 429-435
    • Boveris, A.1
  • 5
    • 0020458787 scopus 로고
    • Plant productiviy and the environment
    • Boyer JS. 1982. Plant productiviy and the environment. Science 218, 443-448.
    • (1982) Science , vol.218 , pp. 443-448
    • Boyer, J.S.1
  • 6
    • 0035212728 scopus 로고    scopus 로고
    • Peroxisomes as a source of reactive oxygen species and nitric oxide signal molecules in plant cells
    • Corpas FJ, Barroso JB, del Rio LA. 2001. Peroxisomes as a source of reactive oxygen species and nitric oxide signal molecules in plant cells. Trends in Plant Science 6, 145-150.
    • (2001) Trends in Plant Science , vol.6 , pp. 145-150
    • Corpas, F.J.1    Barroso, J.B.2    Del Rio, L.A.3
  • 8
    • 0034527512 scopus 로고    scopus 로고
    • Biphasic effect of copper on the ascorbate-glutathione pathway in primary leaves of Phaseolus vulgaris seedlings during the early stages of metal assimilation
    • Cuypers A, Vangronsveld J, Clijsters H. 2000. Biphasic effect of copper on the ascorbate-glutathione pathway in primary leaves of Phaseolus vulgaris seedlings during the early stages of metal assimilation. Physiologia Plantarum 110, 512-517.
    • (2000) Physiologia Plantarum , vol.110 , pp. 512-517
    • Cuypers, A.1    Vangronsveld, J.2    Clijsters, H.3
  • 11
    • 0242585515 scopus 로고    scopus 로고
    • Mitochondrial and peroxisomal manganese superoxide dismutase: Differential expression during leaf senescence
    • del Rio LA, Sandalio LM, Altomare DA, Zilinskas BA. 2003. Mitochondrial and peroxisomal manganese superoxide dismutase: differential expression during leaf senescence. Journal of Experimental Botany 54, 923-933.
    • (2003) Journal of Experimental Botany , vol.54 , pp. 923-933
    • Del Rio, L.A.1    Sandalio, L.M.2    Altomare, D.A.3    Zilinskas, B.A.4
  • 12
    • 0036225043 scopus 로고    scopus 로고
    • Chromium ions inactivate electron transport and enhance superoxide generation in vivo in pea (Pisum sativum L. cv. Azad) root mitochondria
    • Dixit V, Pandey V, Shyam R. 2002. Chromium ions inactivate electron transport and enhance superoxide generation in vivo in pea (Pisum sativum L. cv. Azad) root mitochondria. Plant, Cell and Environment 25, 687-693.
    • (2002) Plant, Cell and Environment , vol.25 , pp. 687-693
    • Dixit, V.1    Pandey, V.2    Shyam, R.3
  • 13
    • 0025142672 scopus 로고
    • Malondialdehyde determination as index of lipid peroxidation
    • Draper HH, Hadley M. 1990. Malondialdehyde determination as index of lipid peroxidation. Methods in Enzymology 186, 421-431.
    • (1990) Methods in Enzymology , vol.186 , pp. 421-431
    • Draper, H.H.1    Hadley, M.2
  • 14
    • 0001896020 scopus 로고
    • Evidence for glutathione peroxidase activities in cultured plant cells
    • Drotar A, Phelps P, Fall R. 1985. Evidence for glutathione peroxidase activities in cultured plant cells. Plant Physiology 42, 35-40.
    • (1985) Plant Physiology , vol.42 , pp. 35-40
    • Drotar, A.1    Phelps, P.2    Fall, R.3
  • 15
    • 0032570623 scopus 로고    scopus 로고
    • Flax guaiacol peroxidases can be used to illustrate the possibility of misinterpreting the effects of stress on the activity of developmentally regulated enzymes
    • Fleldes MA, Gerhardt KE. 1998. Flax guaiacol peroxidases can be used to illustrate the possibility of misinterpreting the effects of stress on the activity of developmentally regulated enzymes. Plant Science 132, 89-99.
    • (1998) Plant Science , vol.132 , pp. 89-99
    • Fleldes, M.A.1    Gerhardt, K.E.2
  • 16
    • 0003121376 scopus 로고
    • Presence of glutathione and glutathione reductase in chloroplasts: A proposed role in ascorbic acid metabolism
    • Foyer CH, Halliwell B. 1976. Presence of glutathione and glutathione reductase in chloroplasts: a proposed role in ascorbic acid metabolism. Planta 133, 21-25.
    • (1976) Planta , vol.133 , pp. 21-25
    • Foyer, C.H.1    Halliwell, B.2
  • 17
    • 0033932601 scopus 로고    scopus 로고
    • Oxygen processing in photosynthesis: Regulation and signalling
    • Foyer CH, Noctor G. 2000. Oxygen processing in photosynthesis: regulation and signalling. New Phytologist 146, 359-388.
    • (2000) New Phytologist , vol.146 , pp. 359-388
    • Foyer, C.H.1    Noctor, G.2
  • 18
    • 0142256789 scopus 로고    scopus 로고
    • Differential response of antioxidative system of chloroplasts and mitochondria to long-term NaCl stress of pea plants
    • Gómez JM, Hernández JA, Jiménez A, del Rio LA, Sevilla F. 1999. Differential response of antioxidative system of chloroplasts and mitochondria to long-term NaCl stress of pea plants. Free Radicals Research 31, 11-18.
    • (1999) Free Radicals Research , vol.31 , pp. 11-18
    • Gómez, J.M.1    Hernández, J.A.2    Jiménez, A.3    Del Rio, L.A.4    Sevilla, F.5
  • 19
    • 0025369970 scopus 로고
    • The measurement and mechanism of lipid peroxidation in biological systems
    • Gutteridge JMC, Halliwell B. 1990. The measurement and mechanism of lipid peroxidation in biological systems. Trends in Biochemical Science 15, 129-135.
    • (1990) Trends in Biochemical Science , vol.15 , pp. 129-135
    • Gutteridge, J.M.C.1    Halliwell, B.2
  • 21
  • 23
    • 0040557481 scopus 로고    scopus 로고
    • Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves
    • Jiménez A, Hernández JA, del Río LA, Sevilla F. 1997. Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves. Plant Physiology 114, 275-284.
    • (1997) Plant Physiology , vol.114 , pp. 275-284
    • Jiménez, A.1    Hernández, J.A.2    Del Río, L.A.3    Sevilla, F.4
  • 24
    • 84954309674 scopus 로고
    • Superoxide dismutase
    • Fukui T, Soda K, ed. Tokyo: Kondansha Ltd.
    • Kanematsu S, Asada K. 1994. Superoxide dismutase. In: Fukui T, Soda K, ed. Molecular aspects of enzyme catalysis. Tokyo: Kondansha Ltd., 191-210.
    • (1994) Molecular Aspects of Enzyme Catalysis , pp. 191-210
    • Kanematsu, S.1    Asada, K.2
  • 26
    • 0036066838 scopus 로고    scopus 로고
    • Changes in antioxidant levels in Oryza sativa L. roots subjected to NaCl-salinity stress
    • Khan MH, Singha KLB, Panda SK. 2002. Changes in antioxidant levels in Oryza sativa L. roots subjected to NaCl-salinity stress. Acta Physiologiae Plantarum 24, 145-148.
    • (2002) Acta Physiologiae Plantarum , vol.24 , pp. 145-148
    • Khan, M.H.1    Singha, K.L.B.2    Panda, S.K.3
  • 28
    • 0020585306 scopus 로고
    • Glutathione and ascorbic acid in spinach (Spinacia oleracea) chloroplasts
    • Law MY, Charles SA, Halliwell B. 1983. Glutathione and ascorbic acid in spinach (Spinacia oleracea) chloroplasts. Biochemical Journal 210, 899-903.
    • (1983) Biochemical Journal , vol.210 , pp. 899-903
    • Law, M.Y.1    Charles, S.A.2    Halliwell, B.3
  • 29
    • 0034951302 scopus 로고    scopus 로고
    • The inductive responses of the antioxidant enzymes by salt stress in the rice (Oryza sativa L.)
    • Lee DH, Kim YS, Lee CB. 2001. The inductive responses of the antioxidant enzymes by salt stress in the rice (Oryza sativa L.). Journal of Plant Physiology 158, 737-745.
    • (2001) Journal of Plant Physiology , vol.158 , pp. 737-745
    • Lee, D.H.1    Kim, Y.S.2    Lee, C.B.3
  • 30
    • 0142229566 scopus 로고    scopus 로고
    • Exogenous silicon (Si) increases antioxidant enzyme activity and reduces lipid peroxidation in roots of salt-stressed barley (Hordeum vulgare L.)
    • Liang YC, Chen Q, Liu Q, Zhang WH, Ding RX. 2003. Exogenous silicon (Si) increases antioxidant enzyme activity and reduces lipid peroxidation in roots of salt-stressed barley (Hordeum vulgare L.). Journal of Plant Physiology 160, 1157-1164.
    • (2003) Journal of Plant Physiology , vol.160 , pp. 1157-1164
    • Liang, Y.C.1    Chen, Q.2    Liu, Q.3    Zhang, W.H.4    Ding, R.X.5
  • 31
    • 5844283971 scopus 로고    scopus 로고
    • Ascorbate peroxidase activity, not the mRNA level, is enhanced in salt-stressed Raphanus sativus plants
    • Lopez F, Vansuyt G, Casse-Delbart F, Fourcroy P. 1996. Ascorbate peroxidase activity, not the mRNA level, is enhanced in salt-stressed Raphanus sativus plants. Physiologia Plantarum 97, 13-20.
    • (1996) Physiologia Plantarum , vol.97 , pp. 13-20
    • Lopez, F.1    Vansuyt, G.2    Casse-Delbart, F.3    Fourcroy, P.4
  • 32
    • 0039552192 scopus 로고    scopus 로고
    • Characterization of membrane polypeptides from pea leaf peroxisomes involved in superoxide radical generation
    • Lopez-Huertas E, Corpas FJ, Sandalio LM, Del Rio LA. 1999. Characterization of membrane polypeptides from pea leaf peroxisomes involved in superoxide radical generation. Biochemical Journal 337, 531-536.
    • (1999) Biochemical Journal , vol.337 , pp. 531-536
    • Lopez-Huertas, E.1    Corpas, F.J.2    Sandalio, L.M.3    Del Rio, L.A.4
  • 33
    • 0035748929 scopus 로고    scopus 로고
    • Antioxidative defense to lead stress in subcellular compartments of pea root cells
    • Malecka A, Jarmuszklewicz W, Tomaszewska B. 2001. Antioxidative defense to lead stress in subcellular compartments of pea root cells. Acta Biochimia Polonica 48, 687-698.
    • (2001) Acta Biochimia Polonica , vol.48 , pp. 687-698
    • Malecka, A.1    Jarmuszklewicz, W.2    Tomaszewska, B.3
  • 34
    • 0032816975 scopus 로고    scopus 로고
    • Antioxidative responses of shoots and roots of wheat to increasing NaCl concentrations
    • Meneguzzo S, Navari-Izzo F, Izzo R. 1999. Antioxidative responses of shoots and roots of wheat to increasing NaCl concentrations. Journal of Plant Physiology 155, 274-280.
    • (1999) Journal of Plant Physiology , vol.155 , pp. 274-280
    • Meneguzzo, S.1    Navari-Izzo, F.2    Izzo, R.3
  • 35
    • 0027177774 scopus 로고
    • Detection of ascorbate peroxidase activity in native gels by inhibition of the ascorbate-dependent reduction of nitroblue tetrazolium
    • Mittler R, Zilinskas BA. 1993. Detection of ascorbate peroxidase activity in native gels by inhibition of the ascorbate-dependent reduction of nitroblue tetrazolium. Analytical Biochemistry 212, 540-546.
    • (1993) Analytical Biochemistry , vol.212 , pp. 540-546
    • Mittler, R.1    Zilinskas, B.A.2
  • 36
    • 0036486856 scopus 로고    scopus 로고
    • Response of the cultivated tomato and its wild salt-tolerant relative Lycopersicon pennellii to salt-dependent oxidative stress: Increased activities of antioxidant enzymes in root plastids
    • Mittova V, Guy M, Tal M, Volokita M. 2002a. Response of the cultivated tomato and its wild salt-tolerant relative Lycopersicon pennellii to salt-dependent oxidative stress: increased activities of antioxidant enzymes in root plastids. Free Radicals Research 36, 195-202.
    • (2002) Free Radicals Research , vol.36 , pp. 195-202
    • Mittova, V.1    Guy, M.2    Tal, M.3    Volokita, M.4
  • 37
    • 0036068551 scopus 로고    scopus 로고
    • Salt stress induces up-regulation of an efficient chloroplast antioxidant system in the salt-tolerant wild tomato species Lycopersicon pennellii but not in the cultivated species
    • Mittova V, Tal M, Volokita M, Guy M. 2002b. Salt stress induces up-regulation of an efficient chloroplast antioxidant system in the salt-tolerant wild tomato species Lycopersicon pennellii but not in the cultivated species. Physiologia Plantarum 115, 393-400.
    • (2002) Physiologia Plantarum , vol.115 , pp. 393-400
    • Mittova, V.1    Tal, M.2    Volokita, M.3    Guy, M.4
  • 38
    • 0037708395 scopus 로고    scopus 로고
    • Up-regulation of the leaf mitochondrial and peroxisomal antioxidative systems in response to salt-induced oxidative stress in the wild salt-tolerant tomato species Lycopersicon pennellii
    • Mittova V, Tal M, Volokita M, Guy M. 2003. Up-regulation of the leaf mitochondrial and peroxisomal antioxidative systems in response to salt-induced oxidative stress in the wild salt-tolerant tomato species Lycopersicon pennellii. Plant, Cell and Environment 26, 845-856.
    • (2003) Plant, Cell and Environment , vol.26 , pp. 845-856
    • Mittova, V.1    Tal, M.2    Volokita, M.3    Guy, M.4
  • 39
    • 0033823856 scopus 로고    scopus 로고
    • Activities of SOD and the ascorbate-glutathione cycle enzymes in subcellular compartments in leaves and roots of the cultivated tomato and its wild salt-tolerant relative Lycopersicon pennellii
    • Mittova V, Volokita M, Guy M, Tal M. 2000. Activities of SOD and the ascorbate-glutathione cycle enzymes in subcellular compartments in leaves and roots of the cultivated tomato and its wild salt-tolerant relative Lycopersicon pennellii. Physiologia Plantarum 110, 42-51.
    • (2000) Physiologia Plantarum , vol.110 , pp. 42-51
    • Mittova, V.1    Volokita, M.2    Guy, M.3    Tal, M.4
  • 40
    • 0035781005 scopus 로고    scopus 로고
    • Plant mitochondria and oxidative stress: Electron transport, NADPH turnover, and metabolism of reactive oxygen species
    • Møller IM. 2001. Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species. Annual Review of Plant Physiology and Plant Molecular Biology 52, 561-591.
    • (2001) Annual Review of Plant Physiology and Plant Molecular Biology , vol.52 , pp. 561-591
    • Møller, I.M.1
  • 42
    • 0028254179 scopus 로고
    • The influence of apoplastic ascorbate on the activities of cell wall-associated peroxidase and NADH oxidase in needles of Norway spruce (Picea abies L)
    • Otter T, Polle A. 1994. The influence of apoplastic ascorbate on the activities of cell wall-associated peroxidase and NADH oxidase in needles of Norway spruce (Picea abies L). Plant Cell Physiology 35, 1231-1238.
    • (1994) Plant Cell Physiology , vol.35 , pp. 1231-1238
    • Otter, T.1    Polle, A.2
  • 43
    • 1842825473 scopus 로고    scopus 로고
    • Global impact of salinity and agricultural ecosystyems
    • Läuchli A, Lüttge U, eds. Kluwer Academic Publishers
    • Pitman MG, Läuchli A. 2002. Global impact of salinity and agricultural ecosystyems. In: Läuchli A, Lüttge U, eds. Salinity, environment - plants, molecules, Kluwer Academic Publishers, 3-20.
    • (2002) Salinity, Environment - Plants, Molecules , pp. 3-20
    • Pitman, M.G.1    Läuchli, A.2
  • 44
    • 0032469049 scopus 로고    scopus 로고
    • Chilling-induced changes in membrane fluidity and antioxidant enzyme activities in Coffea arabica L. roots
    • Quelroz CGS, Alonso A, Mares-Guia M, Magalhaes AC 1998. Chilling-induced changes in membrane fluidity and antioxidant enzyme activities in Coffea arabica L. roots. Biologia Plantarum 41, 403-413.
    • (1998) Biologia Plantarum , vol.41 , pp. 403-413
    • Quelroz, C.G.S.1    Alonso, A.2    Mares-Guia, M.3    Magalhaes, A.C.4
  • 45
    • 0345211443 scopus 로고    scopus 로고
    • Free radical formation and activity of antioxidant enzymes in lupin roots exposed to lead
    • Rucinska R, Waplak S, Gwozdz E. 1999. Free radical formation and activity of antioxidant enzymes in lupin roots exposed to lead. Plant Physiology and Biochemistry 37, 187-194.
    • (1999) Plant Physiology and Biochemistry , vol.37 , pp. 187-194
    • Rucinska, R.1    Waplak, S.2    Gwozdz, E.3
  • 46
    • 0000410406 scopus 로고
    • Intraorganellar distribution of superoxide dismutase in plant peroxisomes (glyoxisomes and lef peroxisomes)
    • Sandalio LM, del Rio LA. 1988. Intraorganellar distribution of superoxide dismutase in plant peroxisomes (glyoxisomes and lef peroxisomes). Plant Physiology 88, 1215-1218.
    • (1988) Plant Physiology , vol.88 , pp. 1215-1218
    • Sandalio, L.M.1    Del Rio, L.A.2
  • 47
    • 0001857316 scopus 로고    scopus 로고
    • Molecular genetics of superoxide dismutase in plants
    • Scandalios JG, ed. New York: Cold Spring Harbor Laboratory Press
    • Scandalios JG. 1997. Molecular genetics of superoxide dismutase in plants. In: Scandalios JG, ed. Oxidative stress and the molecular biology of antioxidant defenses. New York: Cold Spring Harbor Laboratory Press, 527-568.
    • (1997) Oxidative Stress and the Molecular Biology of Antioxidant Defenses , pp. 527-568
    • Scandalios, J.G.1
  • 48
    • 0035212036 scopus 로고    scopus 로고
    • Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli
    • Seaver LC, Imlay JA. 2001. Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli. Journal of Bacteriology 183, 7182-7189.
    • (2001) Journal of Bacteriology , vol.183 , pp. 7182-7189
    • Seaver, L.C.1    Imlay, J.A.2
  • 49
    • 0034918132 scopus 로고    scopus 로고
    • Response of the cultivated tomato and its wild salt-tolerant relative Lycopersicon pennellii to salt-dependent oxidative stress: The root antioxidative system
    • Shalata A, Mittova V, Volokita M, Guy M, Tal M. 2001. Response of the cultivated tomato and its wild salt-tolerant relative Lycopersicon pennellii to salt-dependent oxidative stress: the root antioxidative system. Physiologia Plantarum 112, 487-494.
    • (2001) Physiologia Plantarum , vol.112 , pp. 487-494
    • Shalata, A.1    Mittova, V.2    Volokita, M.3    Guy, M.4    Tal, M.5
  • 50
    • 0037680176 scopus 로고    scopus 로고
    • The characterization of peroxidases in mitochondria of maize roots
    • Sukalovic VHT, Vuletic M. 2003. The characterization of peroxidases in mitochondria of maize roots. Plant Science 164, 999-1007.
    • (2003) Plant Science , vol.164 , pp. 999-1007
    • Sukalovic, V.H.T.1    Vuletic, M.2
  • 51
    • 0028306066 scopus 로고
    • Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides
    • Wolff S. 1994. Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides. Methods in Enzymology 233, 182-189.
    • (1994) Methods in Enzymology , vol.233 , pp. 182-189
    • Wolff, S.1
  • 52
    • 0033514878 scopus 로고    scopus 로고
    • Drought and salinity differentially influence activities of superoxide dismutases in narrow-leafed lupines
    • Yu Q, Rengel Z. 1999. Drought and salinity differentially influence activities of superoxide dismutases in narrow-leafed lupines. Plant Science 142, 1-11.
    • (1999) Plant Science , vol.142 , pp. 1-11
    • Yu, Q.1    Rengel, Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.