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Volumn 221, Issue 3-4, 2003, Pages 269-275

Iron deficiency enhances the levels of ascorbate, glutathione, and related enzymes in sugar beet roots

Author keywords

Ascorbate; Ascorbate free radical reductase; Beta vulgaris; Glutathione; Glutathione reductase; Iron deficiency

Indexed keywords

BETA VULGARIS; BETA VULGARIS SUBSP. VULGARIS;

EID: 0038461907     PISSN: 0033183X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00709-002-0051-6     Document Type: Article
Times cited : (93)

References (40)
  • 1
    • 0001662170 scopus 로고
    • Ascorbate free radical reductase a key enzyme of the ascorbic acid system
    • Arrigoni O, Dipierro S, Borraccino G (1981) Ascorbate free radical reductase a key enzyme of the ascorbic acid system. FEBS Lett 125: 242-245
    • (1981) FEBS Lett , vol.125 , pp. 242-245
    • Arrigoni, O.1    Dipierro, S.2    Borraccino, G.3
  • 2
    • 0002907902 scopus 로고    scopus 로고
    • 2 scavenging in plants
    • Scandalios JG (ed). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • 2 scavenging in plants. In: Scandalios JG (ed) Oxidative stress and the molecular biology of antioxidant defenses. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp 715-735
    • (1997) Oxidative Stress and the Molecular Biology of Antioxidant Defenses , pp. 715-735
    • Asada, K.1
  • 3
    • 0344507330 scopus 로고    scopus 로고
    • Comparison of redox activities in plasma membranes from roots and shoots of etiolated bean seedlings
    • Asard H, Bérczi A (1998) Comparison of redox activities in plasma membranes from roots and shoots of etiolated bean seedlings. Protoplasma 205: 37-42
    • (1998) Protoplasma , vol.205 , pp. 37-42
    • Asard, H.1    Bérczi, A.2
  • 4
    • 0542444213 scopus 로고    scopus 로고
    • NADH-Monodehydroascorbate oxidoreductase is one of the redox enzymes in spinach leaf plasma membranes
    • Bérczi A, Møller IM (1998) NADH-Monodehydroascorbate oxidoreductase is one of the redox enzymes in spinach leaf plasma membranes. Plant Physiol 116: 1029-1036
    • (1998) Plant Physiol , vol.116 , pp. 1029-1036
    • Bérczi, A.1    Møller, I.M.2
  • 5
    • 0000703397 scopus 로고
    • Properties of glutathione reductase from chloroplasts and roots of pea
    • Bielawski W, Joy KW (1986a) Properties of glutathione reductase from chloroplasts and roots of pea. Phytochemistry 25: 2261-2265
    • (1986) Phytochemistry , vol.25 , pp. 2261-2265
    • Bielawski, W.1    Joy, K.W.2
  • 6
    • 0001206778 scopus 로고
    • Reduced and oxidised glutathione and glutathione-reductase activity in tissues of Pisum sativum
    • _ (1986b) Reduced and oxidised glutathione and glutathione-reductase activity in tissues of Pisum sativum. Planta 169: 267-272
    • (1986) Planta , vol.169 , pp. 267-272
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (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
  • 8
    • 0004957464 scopus 로고
    • Magnesium deficiency and high light intensity enhance activities of superoxide dismutase, ascorbate peroxidase and glutathione reductase in bean leaves
    • Cakmak I, Marschner H (1992) Magnesium deficiency and high light intensity enhance activities of superoxide dismutase, ascorbate peroxidase and glutathione reductase in bean leaves. Plant Physiol 98: 1222-1227
    • (1992) Plant Physiol , vol.98 , pp. 1222-1227
    • Cakmak, I.1    Marschner, H.2
  • 9
    • 0001210431 scopus 로고
    • Effects of elevated cytosolic glutathione reductase activity on the cellular glutathione pool and photosynthesis in leaves under normal and stress conditions
    • Foyer CH, Lelandais M, Galap C, Kunert KJ (1991) Effects of elevated cytosolic glutathione reductase activity on the cellular glutathione pool and photosynthesis in leaves under normal and stress conditions. Plant Physiol 97: 863-872
    • (1991) Plant Physiol , vol.97 , pp. 863-872
    • Foyer, C.H.1    Lelandais, M.2    Galap, C.3    Kunert, K.J.4
  • 10
    • 0029410773 scopus 로고
    • Overexpression of glutathione reductase but not glutathione synthetase leads to increases in antioxidant capacity and resistance to photoinhibition in poplar trees
    • _ Souriau N, Perret S, Lelandais M, Kunert KJ, Pruvost C, Jouanin L (1995) Overexpression of glutathione reductase but not glutathione synthetase leads to increases in antioxidant capacity and resistance to photoinhibition in poplar trees. Plant Physiol 109: 1047-1057
    • (1995) Plant Physiol , vol.109 , pp. 1047-1057
    • Souriau, N.1    Perret, S.2    Lelandais, M.3    Kunert, K.J.4    Pruvost, C.5    Jouanin, L.6
  • 11
    • 0030956872 scopus 로고    scopus 로고
    • Hydrogen peroxide- and glutathione-associated mechanisms of acclimatory stress tolerance and signalling
    • _ López-Delgado H, Dat JF, Scott IM (1997) Hydrogen peroxide- and glutathione-associated mechanisms of acclimatory stress tolerance and signalling. Physiol Plant 100: 241-254
    • (1997) Physiol Plant , vol.100 , pp. 241-254
    • López-Delgado, H.1    Dat, J.F.2    Scott, I.M.3
  • 12
    • 0035205673 scopus 로고    scopus 로고
    • The functions of inter- and intracellular glutathione transport systems in plants
    • _ Theodoulou FL, Delrot S (2001) The functions of inter- and intracellular glutathione transport systems in plants. Trends Plant Sci 6: 486-492
    • (2001) Trends Plant Sci , vol.6 , pp. 486-492
    • Theodoulou, F.L.1    Delrot, S.2
  • 13
    • 0029294106 scopus 로고
    • Ascorbate free radical reductase mRNA levels are induced by wounding
    • Grantz AA, Brummell DA, Bennett AB (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
  • 14
    • 0028080557 scopus 로고
    • The role of ascorbate free radical as an electron acceptor to cytochrome b-mediated trans-plasma membrane electron transport in higher plants
    • Horemans N, Asard H, Caubergs RJ (1994) The role of ascorbate free radical as an electron acceptor to cytochrome b-mediated trans-plasma membrane electron transport in higher plants. Plant Physiol 104: 1455-1458
    • (1994) Plant Physiol , vol.104 , pp. 1455-1458
    • Horemans, N.1    Asard, H.2    Caubergs, R.J.3
  • 15
    • 0033843746 scopus 로고    scopus 로고
    • Ascorbate function and associated transport systems in plants
    • _ Foyer CH, Potters G, Asard H (2000) Ascorbate function and associated transport systems in plants. Plant Physiol Biochem 38: 531-540
    • (2000) Plant Physiol Biochem , vol.38 , pp. 531-540
    • Foyer, C.H.1    Potters, G.2    Asard, H.3
  • 16
    • 0022372087 scopus 로고
    • Monodehydroascorbate reductase from cucumber is a flavin adenine dinucleotide enzyme
    • Hossain MA, Asada K (1985) Monodehydroascorbate reductase from cucumber is a flavin adenine dinucleotide enzyme. J Biol Chem 260: 12920-12926
    • (1985) J Biol Chem , vol.260 , pp. 12920-12926
    • Hossain, M.A.1    Asada, K.2
  • 17
    • 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
  • 18
    • 0000405262 scopus 로고
    • Characterization of a membrane fraction containing a b-type cytochrome
    • Jesaitis AJ, Heners PR, Hertel R, Briggs WR (1977) Characterization of a membrane fraction containing a b-type cytochrome. Plant Physiol 59: 941-947
    • (1977) Plant Physiol , vol.59 , pp. 941-947
    • Jesaitis, A.J.1    Heners, P.R.2    Hertel, R.3    Briggs, W.R.4
  • 19
    • 0027523668 scopus 로고
    • Iron release and uptake by plant ferritin: Effects of pH, reduction and chelation
    • Laulhère JP, Briat JF (1993) Iron release and uptake by plant ferritin: effects of pH, reduction and chelation. Biochem J 290: 693-699
    • (1993) Biochem J , vol.290 , pp. 693-699
    • Laulhère, J.P.1    Briat, J.F.2
  • 21
    • 85013968410 scopus 로고
    • Characterization and partial purification of multiple electron transport activities in plasma membranes from maize (Zea mays) roots
    • Luster DG, Buckhout TJ (1988) Characterization and partial purification of multiple electron transport activities in plasma membranes from maize (Zea mays) roots. Physiol Plant 73: 339-347
    • (1988) Physiol Plant , vol.73 , pp. 339-347
    • Luster, D.G.1    Buckhout, T.J.2
  • 22
    • 12044251152 scopus 로고
    • Role of ascorbate in detoxifying ozone in apoplast of spinach (Spinacia oleracea L.) leaves
    • Luwe MWF, Takahama U, Heber U (1993) Role of ascorbate in detoxifying ozone in apoplast of spinach (Spinacia oleracea L.) leaves. Plant Physiol 101: 969-976
    • (1993) Plant Physiol , vol.101 , pp. 969-976
    • Luwe, M.W.F.1    Takahama, U.2    Heber, U.3
  • 23
    • 0000121196 scopus 로고
    • Purification and characterization of pea cytosolic ascorbate peroxidase
    • Mittler R, Zilinskas BA (1991) Purification and characterization of pea cytosolic ascorbate peroxidase. Plant Physiol 97: 962-968
    • (1991) Plant Physiol , vol.97 , pp. 962-968
    • Mittler, R.1    Zilinskas, B.A.2
  • 24
    • 0000890351 scopus 로고
    • Iron reductase systems on the plant plasma membrane: A review
    • Moog PR, Brüggemann W (1994) Iron reductase systems on the plant plasma membrane: a review. Plant Soil 165: 241-260
    • (1994) Plant Soil , vol.165 , pp. 241-260
    • Moog, P.R.1    Brüggemann, W.2
  • 25
    • 0002752725 scopus 로고    scopus 로고
    • Glutathione reductase: Regulation and role in oxidative stress
    • Scandalios J (ed). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Mullineaux PM, Criessen GP (1997) Glutathione reductase: regulation and role in oxidative stress. In: Scandalios J (ed) Oxidative stress and the molecular biology of antioxidant defenses. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp 667-713
    • (1997) Oxidative Stress and the Molecular Biology of Antioxidant Defenses , pp. 667-713
    • Mullineaux, P.M.1    Criessen, G.P.2
  • 26
    • 0028151023 scopus 로고
    • Molecular cloning and characterization of a cDNA encoding pea monodehydroascorbate reductase
    • Murthy SS, Zilinskas BA (1994) Molecular cloning and characterization of a cDNA encoding pea monodehydroascorbate reductase. J Biol Chem 269: 31129-31133
    • (1994) J Biol Chem , vol.269 , pp. 31129-31133
    • Murthy, S.S.1    Zilinskas, B.A.2
  • 28
    • 0031735647 scopus 로고    scopus 로고
    • Ascorbate and glutathione: Keeping active oxygen under control
    • Noctor G, Foyer CH (1998) Ascorbate and glutathione: keeping active oxygen under control. Annu Rev Plant Physiol Plant Mol Biol 49: 249-279
    • (1998) Annu Rev Plant Physiol Plant Mol Biol , vol.49 , pp. 249-279
    • Noctor, G.1    Foyer, C.H.2
  • 29
    • 0030484276 scopus 로고    scopus 로고
    • +-ATPase in plasma membranes isolated from green alga Chlamydomonas reinhardtii
    • +-ATPase in plasma membranes isolated from green alga Chlamydomonas reinhardtii. Physiol Plant 97: 445-453
    • (1996) Physiol Plant , vol.97 , pp. 445-453
    • Norling, B.1    Nurani, G.2    Franzén, L.G.3
  • 30
    • 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
  • 31
    • 49149141770 scopus 로고
    • Glutathione metabolism and possible biological roles in higher plants
    • Rennenberg H (1982) Glutathione metabolism and possible biological roles in higher plants. Phytochemistry 21: 2771-2781
    • (1982) Phytochemistry , vol.21 , pp. 2771-2781
    • Rennenberg, H.1
  • 32
    • 0000527867 scopus 로고
    • Different strategies for iron acquisition in higher plants
    • Römheld V (1987) Different strategies for iron acquisition in higher plants. Physiol Plant 70: 231-234
    • (1987) Physiol Plant , vol.70 , pp. 231-234
    • Römheld, V.1
  • 33
    • 0028407352 scopus 로고
    • cDNA cloning of monodehydroascorbate radical reductase from cucumber: A high degree of homology in terms of amino acid sequence between this enzyme and bacterial flavoenzymes
    • Sano S, Asada K (1994) cDNA cloning of monodehydroascorbate radical reductase from cucumber: a high degree of homology in terms of amino acid sequence between this enzyme and bacterial flavoenzymes. Plant Cell Physiol 35: 425-437
    • (1994) Plant Cell Physiol , vol.35 , pp. 425-437
    • Sano, S.1    Asada, K.2
  • 34
    • 0033039643 scopus 로고    scopus 로고
    • Mechanisms and regulation of reduction-based iron uptake in plants
    • Schmidt W (1999) Mechanisms and regulation of reduction-based iron uptake in plants. New Phytol 141: 1-26
    • (1999) New Phytol , vol.141 , pp. 1-26
    • Schmidt, W.1
  • 35
    • 0017333009 scopus 로고
    • Oxidation of ascorbate anion by electron transfer to phenoxyl radicals
    • Schuler RH (1977) Oxidation of ascorbate anion by electron transfer to phenoxyl radicals. Radiat Res 69: 417-433
    • (1977) Radiat Res , vol.69 , pp. 417-433
    • Schuler, R.H.1
  • 36
    • 0027442863 scopus 로고
    • Riboflavin 3′- and 5′-sulfate, two novel flavins accumulating in the roots of iron-deficient sugar beet (Beta vulgaris)
    • Susín S, Abián J, Sánchez-Baeza F, Peleato ML, Abadía A, Gelpi E, Abadía J (1993) Riboflavin 3′- and 5′-sulfate, two novel flavins accumulating in the roots of iron-deficient sugar beet (Beta vulgaris). J Biol Chem 268: 20958-20965
    • (1993) J Biol Chem , vol.268 , pp. 20958-20965
    • Susín, S.1    Abián, J.2    Sánchez-Baeza, F.3    Peleato, M.L.4    Abadía, A.5    Gelpi, E.6    Abadía, J.7
  • 37
    • 0030062467 scopus 로고    scopus 로고
    • The pH requirement for in vivo activity of the iron-deficiency-induced "Turbo" ferric chelate reductase
    • _ Abadía A, González-Reyes JA, Lucena JJ, Abadía J (1996) The pH requirement for in vivo activity of the iron-deficiency-induced "Turbo" ferric chelate reductase. Plant Physiol 110: 111-123
    • (1996) Plant Physiol , vol.110 , pp. 111-123
    • Abadía, A.1    González-Reyes, J.A.2    Lucena, J.J.3    Abadía, J.4
  • 38
    • 0028313430 scopus 로고
    • +-transport activity in barley roots by salt stress: Possible role of increase in chloride permeability
    • +-transport activity in barley roots by salt stress: possible role of increase in chloride permeability. Soil Sci Plant Nutr 40: 555-563
    • (1994) Soil Sci Plant Nutr , vol.40 , pp. 555-563
    • Yamashita, K.1    Kasai, M.2    Yamamoto, Y.3    Matsumoto, H.4
  • 39
    • 0013490142 scopus 로고    scopus 로고
    • Characterization of ferric chelate reductase in plasma membranes isolated from cucumber roots
    • Ando T, Fujita K, Mae T, Matsumoto H, Mori S, Sekiya J (eds). Kluwer, Dordrecht (Developments in plant and soil sciences, vol 78)
    • Zaharieva T, Yamashita K, Matsumoto H (1997) Characterization of ferric chelate reductase in plasma membranes isolated from cucumber roots. In: Ando T, Fujita K, Mae T, Matsumoto H, Mori S, Sekiya J (eds) Plant nutrition for sustainable food production and environment. Kluwer, Dordrecht, pp 125-126 (Developments in plant and soil sciences, vol 78)
    • (1997) Plant Nutrition for Sustainable Food Production and Environment , pp. 125-126
    • Zaharieva, T.1    Yamashita, K.2    Matsumoto, H.3
  • 40
    • 0032962391 scopus 로고    scopus 로고
    • Iron deficiency induced changes in ascorbate content and enzyme activities related to ascorbate metabolism in cucumber roots
    • _ (1999) Iron deficiency induced changes in ascorbate content and enzyme activities related to ascorbate metabolism in cucumber roots. Plant Cell Physiol 40: 273-280
    • (1999) Plant Cell Physiol , vol.40 , pp. 273-280


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