메뉴 건너뛰기




Volumn 148, Issue 1, 1999, Pages 69-76

The effect of Botrytis cinerea infection on ascorbate-glutathione cycle in tomato leaves

Author keywords

Ascorbate glutathione cycle; Botrytis cinerea infection; Lycopersicon esculentum Mill.

Indexed keywords

ASCORBATE OXIDASE; ASCORBIC ACID; DEHYDROASCORBIC ACID REDUCTASE; GLUTATHIONE; GLUTATHIONE REDUCTASE; GLUTATHIONE TRANSFERASE;

EID: 0344563460     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9452(99)00121-1     Document Type: Article
Times cited : (59)

References (28)
  • 1
    • 0029853913 scopus 로고    scopus 로고
    • Alteration in protein accumulation, gene expression and ascorbate-glutathione pathway in tomato (Lycopersicon esculentum) under paraquat and ozone stress
    • Kirtikara K., Talbot D. Alteration in protein accumulation, gene expression and ascorbate-glutathione pathway in tomato (Lycopersicon esculentum) under paraquat and ozone stress. J. Plant Physiol. 148:1996;752-760.
    • (1996) J. Plant Physiol. , vol.148 , pp. 752-760
    • Kirtikara, K.1    Talbot, D.2
  • 3
    • 0030860772 scopus 로고    scopus 로고
    • Evidence for a primary role of active oxygen species in induction of host cell death during infection of bean leaves with Botrytis cinerea
    • v Tiedemann A. Evidence for a primary role of active oxygen species in induction of host cell death during infection of bean leaves with Botrytis cinerea. Physiol. Mol. Plant Pathol. 50:1997;151-166.
    • (1997) Physiol. Mol. Plant Pathol. , vol.50 , pp. 151-166
    • V. Tiedemann, A.1
  • 5
    • 0030484105 scopus 로고    scopus 로고
    • The role of activated oxygen species in plant disease resistance
    • Mehdy M.C., Sharma Y.K., Sathasivan K., Bays N.W. The role of activated oxygen species in plant disease resistance. Plant Physiol. 98:1996;365-374.
    • (1996) Plant Physiol. , vol.98 , pp. 365-374
    • Mehdy, M.C.1    Sharma, Y.K.2    Sathasivan, K.3    Bays, N.W.4
  • 8
    • 0031127932 scopus 로고    scopus 로고
    • Detoxification of xenobiotics by plants: Chemical modification and vacuolar compartmentation
    • Coleman J.O.D., Blake-Kalff M.M.A., Davies T.G.E. Detoxification of xenobiotics by plants: chemical modification and vacuolar compartmentation. Trends Plant Sci. 4:1997;144-151.
    • (1997) Trends Plant Sci. , vol.4 , pp. 144-151
    • Coleman, J.O.D.1    Blake-Kalff, M.M.A.2    Davies, T.G.E.3
  • 9
    • 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. 79:1994;583-593.
    • (1994) Cell , vol.79 , pp. 583-593
    • Levine, A.1    Tenhaken, R.2    Dixon, R.3    Lamb, C.4
  • 10
    • 0030956872 scopus 로고    scopus 로고
    • Hydrogen peroxide- And glutathione-associated mechanisms of acclimatory stress tolerance and signalling
    • Foyer C.H., Lopez-Delgado H., Dat J.F., Scott I.M. Hydrogen peroxide- and glutathione-associated mechanisms of acclimatory stress tolerance and signalling. Physiol. Plant. 100:1997;241-254.
    • (1997) Physiol. Plant. , vol.100 , pp. 241-254
    • Foyer, C.H.1    Lopez-Delgado, H.2    Dat, J.F.3    Scott, I.M.4
  • 11
    • 0001613347 scopus 로고    scopus 로고
    • Pathogen-induced changes in the antioxidant status of the apoplast in barley leaves
    • Vanacker H., Carver T.L.W., Foyer C.H. Pathogen-induced changes in the antioxidant status of the apoplast in barley leaves. Plant Physiol. 117:1998;1103-1114.
    • (1998) Plant Physiol. , vol.117 , pp. 1103-1114
    • Vanacker, H.1    Carver, T.L.W.2    Foyer, C.H.3
  • 12
    • 0029835006 scopus 로고    scopus 로고
    • An Arabidopsis mutant depleted in glutathione shows unaltered responses to fungal and bacterial pathogens
    • May M.J., Parker J.E., Daniels M.J., Leaver C.J., Cobbett C.S. An Arabidopsis mutant depleted in glutathione shows unaltered responses to fungal and bacterial pathogens. Mol. Plant Microbe Interact. 9:1996;349-356.
    • (1996) Mol. Plant Microbe Interact. , vol.9 , pp. 349-356
    • May, M.J.1    Parker, J.E.2    Daniels, M.J.3    Leaver, C.J.4    Cobbett, C.S.5
  • 13
    • 0343668457 scopus 로고    scopus 로고
    • Involvement of reactive oxygen species, glutathione metabolism, and lipid peroxidation in the Cf-gene-dependent defence response of tomato cotyledons induced by race-specific elicitors of Cladosporium fulvum
    • May M.J., Hammond-Kosack K.E., Jones J.D.G. Involvement of reactive oxygen species, glutathione metabolism, and lipid peroxidation in the Cf-gene-dependent defence response of tomato cotyledons induced by race-specific elicitors of Cladosporium fulvum. Plant Physiol. 110:1996;1367-1379.
    • (1996) Plant Physiol. , vol.110 , pp. 1367-1379
    • May, M.J.1    Hammond-Kosack, K.E.2    Jones, J.D.G.3
  • 14
    • 0010282460 scopus 로고
    • Hydrogen peroxide is scavenged by ascorbate-specific peroxidase in spinach chloroplasts
    • Nakano Y., Asada K. Hydrogen peroxide is scavenged by ascorbate-specific peroxidase in spinach chloroplasts. Plant Cell. Physiol. 22:1981;867-880.
    • (1981) Plant Cell. Physiol. , vol.22 , pp. 867-880
    • Nakano, Y.1    Asada, K.2
  • 15
    • 0002458223 scopus 로고
    • Purification of dehydroascorbate reductase from spinach and its characterization as a thiol enzyme
    • Hossain M.A., Asada K. Purification of dehydroascorbate reductase from spinach and its characterization as a thiol enzyme. Plant Cell. Physiol. 25:1984;85-92.
    • (1984) Plant Cell. Physiol. , vol.25 , pp. 85-92
    • Hossain, M.A.1    Asada, K.2
  • 16
    • 0005575145 scopus 로고
    • Glutathione reductase
    • Grune & Stratton, New York
    • E. Beutler, Glutathione reductase, in: Red Cells Metabolism, second ed., Grune & Stratton, New York, 1975, pp. 69-70.
    • (1975) In: Red Cells Metabolism, Second Ed. , pp. 69-70
    • Beutler, E.1
  • 17
    • 0019808342 scopus 로고
    • Glutathione S-transferase of human red blood cells assay, value in normal subjects and in two pathological circumstances - Hyperbilirubinemia and impaired renal function
    • Carmagnol F., Sinet P.M., Rapin J., Jerome H. Glutathione S-transferase of human red blood cells assay, value in normal subjects and in two pathological circumstances - hyperbilirubinemia and impaired renal function. Clin. Chim. Acta. 117:1981;209-217.
    • (1981) Clin. Chim. Acta , vol.117 , pp. 209-217
    • Carmagnol, F.1    Sinet, P.M.2    Rapin, J.3    Jerome, H.4
  • 18
    • 0018887652 scopus 로고
    • An improved method for determination of L-ascorbic acid and L-dehydroascorbic acid in blood plasma
    • Okamura M. An improved method for determination of L-ascorbic acid and L-dehydroascorbic acid in blood plasma. Clin. Chim. Acta. 103:1980;259-268.
    • (1980) Clin. Chim. Acta , vol.103 , pp. 259-268
    • Okamura, M.1
  • 19
    • 0030478735 scopus 로고    scopus 로고
    • Alterations in the antioxidative system of suspension-cultured soybean cells (Glycine max) induced by oxidative stress
    • Knörzer O.C., Durner J., Böger P. Alterations in the antioxidative system of suspension-cultured soybean cells (Glycine max) induced by oxidative stress. Physiol. Plant. 97:1996;388-396.
    • (1996) Physiol. Plant. , vol.97 , pp. 388-396
    • Knörzer, O.C.1    Durner, J.2    Böger, P.3
  • 20
    • 0017066115 scopus 로고
    • Enzymatic assay for glutathione
    • Brehe J.E., Burch H.B. Enzymatic assay for glutathione. Anal. Biochem. 74:1976;315-319.
    • (1976) Anal. Biochem. , vol.74 , pp. 315-319
    • Brehe, J.E.1    Burch, H.B.2
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • 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
  • 22
    • 0028794687 scopus 로고
    • Physiological aspects of resistance to Botrytis cinerea
    • Elad Y., Evensen K. Physiological aspects of resistance to Botrytis cinerea. Phytopathology. 85:1995;637-643.
    • (1995) Phytopathology , vol.85 , pp. 637-643
    • Elad, Y.1    Evensen, K.2
  • 23
    • 0029175756 scopus 로고
    • Effects of powdery mildew infection of barley on the ascorbate-glutathione cycle and other antioxidants in different host-pathogen interactions
    • El-Zahaby H.M., Gullner G., Király Z. Effects of powdery mildew infection of barley on the ascorbate-glutathione cycle and other antioxidants in different host-pathogen interactions. Phytopathology. 85:1995;1225-1230.
    • (1995) Phytopathology , vol.85 , pp. 1225-1230
    • El-Zahaby, H.M.1    Gullner, G.2    Király, Z.3
  • 24
    • 0031403884 scopus 로고    scopus 로고
    • Local and systemic responses of antioxidants to tobacco mosaic virus infection and to salicylic acid in tobacco
    • Fodor J., Gullner G., Ádám A.L., Barna B., Kömives T., Király Z. Local and systemic responses of antioxidants to tobacco mosaic virus infection and to salicylic acid in tobacco. Plant Physiol. 114:1997;1443-1451.
    • (1997) Plant Physiol. , vol.114 , pp. 1443-1451
    • Fodor, J.1    Gullner, G.2    Ádám, A.L.3    Barna, B.4    Kömives, T.5    Király, Z.6
  • 25
    • 85053492389 scopus 로고
    • Ascorbic acid
    • R.G. Alscher, & J.L. Hess. Boca Raton, FL: CRC Press
    • Foyer C.H. Ascorbic acid. Alscher R.G., Hess J.L. Antioxidants in Higher Plants. 1993;31-58 CRC Press, Boca Raton, FL.
    • (1993) Antioxidants in Higher Plants , pp. 31-58
    • Foyer, C.H.1
  • 26
    • 0032103181 scopus 로고    scopus 로고
    • Dehydroascorbate-reducing proteins in maize are induced by the ascorbate biosynthesis inhibitor lycorine
    • De Tullio M.C., De Gara L., Paciolla C., Arrigoni O. Dehydroascorbate-reducing proteins in maize are induced by the ascorbate biosynthesis inhibitor lycorine. Plant Physiol. Biochem. 36:1998;433-440.
    • (1998) Plant Physiol. Biochem. , vol.36 , pp. 433-440
    • De Tullio, M.C.1    De Gara, L.2    Paciolla, C.3    Arrigoni, O.4
  • 27
    • 38249005950 scopus 로고
    • Oxidative stress in interactions between Avena sativa L. and Drechslera spp
    • Gönner M.V., Schlösser E. Oxidative stress in interactions between Avena sativa L. and Drechslera spp. Physiol. Mol. Plant Pathol. 42:1993;221-234.
    • (1993) Physiol. Mol. Plant Pathol. , vol.42 , pp. 221-234
    • Gönner, M.V.1    Schlösser, E.2
  • 28
    • 7944239352 scopus 로고    scopus 로고
    • Role of the ascorbate-glutathione cycle of mitochondria and peroxisomes in the senescence of pea leaves
    • Jiménez A., Hernández J.A., Pastori G., del Río L.A., Sevilla F. Role of the ascorbate-glutathione cycle of mitochondria and peroxisomes in the senescence of pea leaves. Plant Physiol. 118:1998;1327-1335.
    • (1998) Plant Physiol. , vol.118 , pp. 1327-1335
    • Jiménez, A.1    Hernández, J.A.2    Pastori, G.3    Del Río, L.A.4    Sevilla, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.