메뉴 건너뛰기




Volumn 36, Issue 6, 1998, Pages 433-440

Dehydroascorbate-reducing proteins in maize are induced by the ascorbate biosynthesis inhibitor lycorine

Author keywords

Ascorbate regeneration; Dehydroascorbate; Lycorine; Zea mays

Indexed keywords

ZEA MAYS;

EID: 0032103181     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0981-9428(98)80207-6     Document Type: Article
Times cited : (44)

References (44)
  • 1
    • 0026664431 scopus 로고
    • Glutaredoxin homologue encoded by vaccinia virus is a virion-associated enzyme with thioltransferase and dehydroascorbate reductase activities
    • [1] Ahn B.Y., Moss B., Glutaredoxin homologue encoded by vaccinia virus is a virion-associated enzyme with thioltransferase and dehydroascorbate reductase activities, Proc. Natl. Acad. Sci. USA 89 (1992) 7060-7065.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7060-7065
    • Ahn, B.Y.1    Moss, B.2
  • 2
    • 0028139387 scopus 로고
    • Ascorbate system and plant development
    • [2] Arrigoni O., Ascorbate system and plant development, J. Bioenerg. Biomemb. 26 (1994) 407-419.
    • (1994) J. Bioenerg. Biomemb. , vol.26 , pp. 407-419
    • Arrigoni, O.1
  • 3
    • 0016806862 scopus 로고
    • Lycorine as an inhibitor of ascorbic acid biosynthesis
    • [3] Arrigoni O., Arrigoni-Liso R., Calabrese G., Lycorine as an inhibitor of ascorbic acid biosynthesis, Nature 256 (1975) 513-514.
    • (1975) Nature , vol.256 , pp. 513-514
    • Arrigoni, O.1    Arrigoni-Liso, R.2    Calabrese, G.3
  • 4
    • 0017107134 scopus 로고
    • Ascorbic acid as a factor controlling the development of cyanide insensitive respiration
    • [4] Arrigoni O., Arrigoni-Liso R., Calabrese G., Ascorbic acid as a factor controlling the development of cyanide insensitive respiration, Science 194 (1976) 332-333.
    • (1976) Science , vol.194 , pp. 332-333
    • Arrigoni, O.1    Arrigoni-Liso, R.2    Calabrese, G.3
  • 5
    • 0017760762 scopus 로고
    • Ascorbic acid requirement for biosynthesis of hydroxyproline-containing proteins in plants
    • [5] Arrigoni O., Arrigoni-Liso R., Calabrese G., Ascorbic acid requirement for biosynthesis of hydroxyproline-containing proteins in plants, FEBS Lett. 82 (1977) 135-137.
    • (1977) FEBS Lett. , vol.82 , pp. 135-137
    • Arrigoni, O.1    Arrigoni-Liso, R.2    Calabrese, G.3
  • 6
    • 0001662170 scopus 로고
    • Ascorbate free radical reductase, a key enzyme of the ascorbic acid system
    • [6] Arrigoni O., Dipierro S., Borraccino G., Ascorbate free radical reductase, a key enzyme of the ascorbic acid system, FEBS Lett. 125 (1981) 242-244.
    • (1981) FEBS Lett. , vol.125 , pp. 242-244
    • Arrigoni, O.1    Dipierro, S.2    Borraccino, G.3
  • 7
    • 0000608572 scopus 로고
    • Changes in the ascorbate system during seed development of Vicia faba L
    • [7] Arrigoni O., De Gara L., Tommasi F., Liso R., Changes in the ascorbate system during seed development of Vicia faba L., Plant Physiol. 99 (1992) 235-238.
    • (1992) Plant Physiol. , vol.99 , pp. 235-238
    • Arrigoni, O.1    De Gara, L.2    Tommasi, F.3    Liso, R.4
  • 9
    • 0022537877 scopus 로고
    • Dehydroascorbic acid and cell membranes: Possible disruptive effects
    • [9] Bianchi J., Rose R.C., Dehydroascorbic acid and cell membranes: possible disruptive effects, Toxicology 40 (1987) 75-82.
    • (1987) Toxicology , vol.40 , pp. 75-82
    • Bianchi, J.1    Rose, R.C.2
  • 11
    • 0025066396 scopus 로고
    • Spontaneous decay of oxidized ascorbic acid (dehydro-L-ascorbic acid) evaluated by high-pressure liquid chromatography
    • [11] Bode A.M., Cunningham L., Rose R.C., Spontaneous decay of oxidized ascorbic acid (dehydro-L-ascorbic acid) evaluated by high-pressure liquid chromatography, Clin. Chem. 36 (1990) 1807-1809.
    • (1990) Clin. Chem. , vol.36 , pp. 1807-1809
    • Bode, A.M.1    Cunningham, L.2    Rose, R.C.3
  • 12
    • 0001445593 scopus 로고
    • The oxidation of ascorbic acid and its reduction in vitro and in vivo
    • [12] Borsook H., Davenport H.W., Jeffreys C.E.P., Warner C., The oxidation of ascorbic acid and its reduction in vitro and in vivo, J. Biol. Chem. 117 (1937) 237-279.
    • (1937) J. Biol. Chem. , vol.117 , pp. 237-279
    • Borsook, H.1    Davenport, H.W.2    Jeffreys, C.E.P.3    Warner, C.4
  • 13
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • [13] Bradford M.M., A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 14
    • 0023951147 scopus 로고
    • Extracellular ascorbic acid and enzyme activities related to ascorbic acid metabolism in Sedum album L. leaves after ozone exposure
    • [14] Castillo F.J., Greppin H., Extracellular ascorbic acid and enzyme activities related to ascorbic acid metabolism in Sedum album L. leaves after ozone exposure, Environ. Exp. Bot. 28 (1988) 231-238.
    • (1988) Environ. Exp. Bot. , vol.28 , pp. 231-238
    • Castillo, F.J.1    Greppin, H.2
  • 15
    • 0026093885 scopus 로고
    • Enzymatic recycling of oxidized ascorbate in pig heart: One-electron vs. two-electron pathway
    • [15] Coassin M., Tomasi A., Vannini V., Ursini F., Enzymatic recycling of oxidized ascorbate in pig heart: one-electron vs. two-electron pathway, Arch. Biochem. Biophys. 290 (1991) 456-462.
    • (1991) Arch. Biochem. Biophys. , vol.290 , pp. 456-462
    • Coassin, M.1    Tomasi, A.2    Vannini, V.3    Ursini, F.4
  • 17
    • 0001106842 scopus 로고
    • Ascorbic acid utilization by prolyl hydroxylase in vivo
    • [17] De Gara L., Tommasi F., Liso R., Arrigoni O., Ascorbic acid utilization by prolyl hydroxylase in vivo. Phytochemistry 30 (1991) 1397-1399.
    • (1991) Phytochemistry , vol.30 , pp. 1397-1399
    • De Gara, L.1    Tommasi, F.2    Liso, R.3    Arrigoni, O.4
  • 18
    • 0001839944 scopus 로고
    • Cytosolic ascorbate peroxidase in Angiosperms and the different expression of its isoforms in maize embryos during germination
    • Welinder K.G., Rasmussen S.K., Penel C., Greppin H. (eds.), University of Geneva Press, Geneva
    • [18] De Gara L., De Tullio M., Paciolla C., Liso R., Arrigoni O., Cytosolic ascorbate peroxidase in Angiosperms and the different expression of its isoforms in maize embryos during germination, in: Welinder K.G., Rasmussen S.K., Penel C., Greppin H. (eds.), Plant peroxidases, biochemistry and physiology, University of Geneva Press, Geneva, 1993, pp. 251-255.
    • (1993) Plant Peroxidases, Biochemistry and Physiology , pp. 251-255
    • De Gara, L.1    De Tullio, M.2    Paciolla, C.3    Liso, R.4    Arrigoni, O.5
  • 19
    • 0028253992 scopus 로고
    • In vivo inhibition of galactono-γ-lactone conversion to ascorbate by lycorine
    • [19] De Gara L., Paciolla C., Tommasi F., Liso R., Arrigoni O., In vivo inhibition of galactono-γ-lactone conversion to ascorbate by lycorine, J. Plant Physiol. 144 (1994) 649-653.
    • (1994) J. Plant Physiol. , vol.144 , pp. 649-653
    • De Gara, L.1    Paciolla, C.2    Tommasi, F.3    Liso, R.4    Arrigoni, O.5
  • 20
    • 0030773307 scopus 로고    scopus 로고
    • Ascorbate synthesis and ascorbate peroxidase activity during the early stage of wheat germination
    • [20] De Gara L., de Pinto M.C., Arrigoni O., Ascorbate synthesis and ascorbate peroxidase activity during the early stage of wheat germination, Physiol. Plant. 100 (1997) 894-900.
    • (1997) Physiol. Plant. , vol.100 , pp. 894-900
    • De Gara, L.1    De Pinto, M.C.2    Arrigoni, O.3
  • 21
    • 0029295940 scopus 로고
    • The multiplicity of enzymatic DHA reduction: A new purification procedure for a DHA reducing protein from potato tubers
    • [21] De Tullio M.C., Paciolla C., de Pinto M.C., De Gara L., The multiplicity of enzymatic DHA reduction: a new purification procedure for a DHA reducing protein from potato tubers, J. Biol. Res. - Boll. Soc. It. Biol. Sper. 71 (1995) 163-170.
    • (1995) J. Biol. Res. - Boll. Soc. It. Biol. Sper. , vol.71 , pp. 163-170
    • De Tullio, M.C.1    Paciolla, C.2    De Pinto, M.C.3    De Gara, L.4
  • 23
    • 0030589186 scopus 로고    scopus 로고
    • Enzymatic method to determine dehydroascorbic acid in biological samples and in bread dough at various stages of mixing
    • [23] Every D., Enzymatic method to determine dehydroascorbic acid in biological samples and in bread dough at various stages of mixing, Anal. Biochem. 242 (1996) 234-239.
    • (1996) Anal. Biochem. , vol.242 , pp. 234-239
    • Every, D.1
  • 24
    • 0031570782 scopus 로고    scopus 로고
    • Hexokinase inactivation induced by ascorbic acid/ Fe(II) in rabbit erythrocyte is independent of glutathione-reductive processes and appears to be mediated by dehydroascorbic acid
    • [24] Fiorani M., De Sanctis R., Saltarelli R., Stocchi V., Hexokinase inactivation induced by ascorbic acid/ Fe(II) in rabbit erythrocyte is independent of glutathione-reductive processes and appears to be mediated by dehydroascorbic acid, Arch. Biochem. Biophys. 342 (1997) 191-196.
    • (1997) Arch. Biochem. Biophys. , vol.342 , pp. 191-196
    • Fiorani, M.1    De Sanctis, R.2    Saltarelli, R.3    Stocchi, V.4
  • 25
    • 0010508344 scopus 로고
    • Studi sulla fisiologia dell'acido ascorbico XXIII: Azione inibente dell'acido deidroascorbico sulla fosforilazione ossidativa di mitocondri vegetali
    • [25] Forti G., Studi sulla fisiologia dell'acido ascorbico XXIII: Azione inibente dell'acido deidroascorbico sulla fosforilazione ossidativa di mitocondri vegetali, Rend. Acc. Naz. Lincei 24 (1958) 70-77.
    • (1958) Rend. Acc. Naz. Lincei , vol.24 , pp. 70-77
    • Forti, G.1
  • 27
    • 0040557481 scopus 로고    scopus 로고
    • Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves
    • [27] Jiménez A., Hernández J.A., del Río L.A., Sevilla F., Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves, Plant Physiol. 114 (1997) 275-284.
    • (1997) Plant Physiol. , vol.114 , pp. 275-284
    • Jiménez, A.1    Hernández, J.A.2    Del Río, L.A.3    Sevilla, F.4
  • 28
    • 0028804550 scopus 로고
    • Extraction and determination of ascorbate and dehydroascorbate from plant tissue
    • [28] Kampfenkel K., Van Montagu M., Inzé D., Extraction and determination of ascorbate and dehydroascorbate from plant tissue, Anal. Biochem. 225 (1995) 165-167.
    • (1995) Anal. Biochem. , vol.225 , pp. 165-167
    • Kampfenkel, K.1    Van Montagu, M.2    Inzé, D.3
  • 29
    • 0030994762 scopus 로고    scopus 로고
    • Purification and characterization of dehydroascorbate reductase from rice
    • [29] Kato Y., Urano J., Maki Y., Ushimaru T., Purification and characterization of dehydroascorbate reductase from rice, Plant Cell Physiol. 38 (1997) 173-178.
    • (1997) Plant Cell Physiol. , vol.38 , pp. 173-178
    • Kato, Y.1    Urano, J.2    Maki, Y.3    Ushimaru, T.4
  • 30
    • 0010471478 scopus 로고    scopus 로고
    • Oxalate biosynthesis from analogs of ascorbic acid in the pathogenic fungus Sclerotinia sclerotiorum
    • [30] Keates S.E., Loewus F.A., Franceschi V.R., Oxalate biosynthesis from analogs of ascorbic acid in the pathogenic fungus Sclerotinia sclerotiorum, Plant Physiol. 114 Suppl. (1997) 48.
    • (1997) Plant Physiol. , vol.114 , Issue.SUPPL. , pp. 48
    • Keates, S.E.1    Loewus, F.A.2    Franceschi, V.R.3
  • 31
    • 0029073615 scopus 로고
    • Determination of ascorbic acid and dehydroascorbic acid in plasma by high-performance liquid chromatography with coulometric detection - Are they reliable biomarkers of oxidative stress?
    • [31] Lykkesfeldt J., Loft S., Poulsen H.E., Determination of ascorbic acid and dehydroascorbic acid in plasma by high-performance liquid chromatography with coulometric detection - are they reliable biomarkers of oxidative stress? Anal. Biochem. 229 (1995) 329-335.
    • (1995) Anal. Biochem. , vol.229 , pp. 329-335
    • Lykkesfeldt, J.1    Loft, S.2    Poulsen, H.E.3
  • 32
    • 0030821482 scopus 로고    scopus 로고
    • Dehydroascorbate and dehydroascorbate reductase are phantom indicators of oxidative stress in plants
    • [32] Morell S., Follmann H., De Tullio M., Häberlein I., Dehydroascorbate and dehydroascorbate reductase are phantom indicators of oxidative stress in plants, FEBS Lett. 414 (1997) 567-570.
    • (1997) FEBS Lett. , vol.414 , pp. 567-570
    • Morell, S.1    Follmann, H.2    De Tullio, M.3    Häberlein, I.4
  • 33
    • 85025528184 scopus 로고
    • Comparison of the enzymatic activities of dehydroascorbic acid reductase, glutathione reductase, catalase, peroxidase and superoxide dismutase of healthy and damaged spruce needles (Picea abies (L.) Karst.)
    • [33] Osswald W.F., Kraus R., Hippeli S., Benz B., Volpert R., Elstner E.F., Comparison of the enzymatic activities of dehydroascorbic acid reductase, glutathione reductase, catalase, peroxidase and superoxide dismutase of healthy and damaged spruce needles (Picea abies (L.) Karst.), J. Plant Physiol. 139 (1992) 742-748.
    • (1992) J. Plant Physiol. , vol.139 , pp. 742-748
    • Osswald, W.F.1    Kraus, R.2    Hippeli, S.3    Benz, B.4    Volpert, R.5    Elstner, E.F.6
  • 35
    • 0029872005 scopus 로고    scopus 로고
    • Purification, cloning and expression of dehydroascorbic acid-reducing activity from human neutrophils: Identification as glutaredoxin
    • [35] Park J.B., Levine M., Purification, cloning and expression of dehydroascorbic acid-reducing activity from human neutrophils: identification as glutaredoxin, Biochem. J. 315 (1996) 931-938.
    • (1996) Biochem. J. , vol.315 , pp. 931-938
    • Park, J.B.1    Levine, M.2
  • 36
    • 0026552796 scopus 로고
    • Short term effects of oxidized ascorbic acid on bovine corneal endothelium and human placenta
    • [36] Rose R.C., Choi J.L., Bode A.M., Short term effects of oxidized ascorbic acid on bovine corneal endothelium and human placenta, Life Sci. 50 (1992) 1543-1549.
    • (1992) Life Sci. , vol.50 , pp. 1543-1549
    • Rose, R.C.1    Choi, J.L.2    Bode, A.M.3
  • 37
    • 0028136613 scopus 로고
    • A novel dehydroascorbate reductase from spinach chloroplasts homologous to plant trypsin inhibitor
    • [37] Trümper S., Follmann H., Häberlein I., A novel dehydroascorbate reductase from spinach chloroplasts homologous to plant trypsin inhibitor, FEBS Lett. 352 (1994) 159-162.
    • (1994) FEBS Lett. , vol.352 , pp. 159-162
    • Trümper, S.1    Follmann, H.2    Häberlein, I.3
  • 38
    • 0030452648 scopus 로고    scopus 로고
    • Enhancement of oxidative stress tolerance in transgenic tobacco plants overproducing Fe-superoxide dismutase in chloroplasts
    • [38] Van Camp W., Capiau K., Van Montagu M., Inzé D., Slooten L., Enhancement of oxidative stress tolerance in transgenic tobacco plants overproducing Fe-superoxide dismutase in chloroplasts, Plant Physiol. 112 (1996) 1703-1714.
    • (1996) Plant Physiol. , vol.112 , pp. 1703-1714
    • Van Camp, W.1    Capiau, K.2    Van Montagu, M.3    Inzé, D.4    Slooten, L.5
  • 39
    • 0025082330 scopus 로고
    • Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity
    • [39] Wells W.W., Xu D.P., Yang Y., Rocque P.A., Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity, J. Biol. Chem. 265 (1990) 15361-15364.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15361-15364
    • Wells, W.W.1    Xu, D.P.2    Yang, Y.3    Rocque, P.A.4
  • 40
    • 0029928826 scopus 로고    scopus 로고
    • Purification and characterization of a glutathione dependent dehydroascorbate reductase from human erythrocytes
    • [40] Xu D.P., Washburn M.P., Sun G.P., Wells W.W., Purification and characterization of a glutathione dependent dehydroascorbate reductase from human erythrocytes, Biochem. Biophys. Res. Commun. 221 (1996) 117-121.
    • (1996) Biochem. Biophys. Res. Commun. , vol.221 , pp. 117-121
    • Xu, D.P.1    Washburn, M.P.2    Sun, G.P.3    Wells, W.W.4
  • 41
    • 0010510463 scopus 로고
    • Investigation of ascorbic acid dehydrogenase of pea (Pisum sativum) and its distribution in the developing plant
    • [41] Yamaguchi M., Joslyn M.A., Investigation of ascorbic acid dehydrogenase of pea (Pisum sativum) and its distribution in the developing plant, Plant Physiol. 26 (1951) 757-772.
    • (1951) Plant Physiol. , vol.26 , pp. 757-772
    • Yamaguchi, M.1    Joslyn, M.A.2
  • 42
    • 0016977112 scopus 로고
    • Formation of free-radical products by the reaction of dehydroascorbic acid with amino acids
    • [42] Yano M., Hayashi T., Namiki M., Formation of free-radical products by the reaction of dehydroascorbic acid with amino acids, J. Agricol. Food Chem. 24 (1976) 815-819.
    • (1976) J. Agricol. Food Chem. , vol.24 , pp. 815-819
    • Yano, M.1    Hayashi, T.2    Namiki, M.3
  • 43
    • 0026515974 scopus 로고
    • Lipofuscin-like fluorophores can result from reactions between oxidized ascorbic acid and glutamine. Carbonyl-protein cross-linking may represent a common reaction in oxygen radical and glycosylation-related ageing processes
    • [43] Yin D., Lipofuscin-like fluorophores can result from reactions between oxidized ascorbic acid and glutamine. Carbonyl-protein cross-linking may represent a common reaction in oxygen radical and glycosylation-related ageing processes, Mech. Ageing Dev. 62 (1992) 35-46.
    • (1992) Mech. Ageing Dev. , vol.62 , pp. 35-46
    • Yin, D.1
  • 44
    • 0030045289 scopus 로고    scopus 로고
    • Enzymatic responses of the ascorbate-glutathione cycle to drought in sorghum and sunflower plants
    • [44] Zhang J., Kirkham M.B., Enzymatic responses of the ascorbate-glutathione cycle to drought in sorghum and sunflower plants, Plant Sci. 113 (1996) 139-147.
    • (1996) Plant Sci. , vol.113 , pp. 139-147
    • Zhang, J.1    Kirkham, M.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.