메뉴 건너뛰기




Volumn 164, Issue 2, 2007, Pages 185-194

The possible involvement of peroxidase in defense of yellow lupine embryo axes against Fusarium oxysporum

Author keywords

Fusarium oxysporum; Lignin; Lupinus luteus; Peroxidase; Sucrose

Indexed keywords

PLANT CELL CULTURE; PLANTS (BOTANY); TISSUE;

EID: 33846493020     PISSN: 01761617     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jplph.2005.11.005     Document Type: Article
Times cited : (65)

References (37)
  • 1
    • 0003823070 scopus 로고
    • H2O2-Bestimmung. Verfahren mit 2.2-Azino-di-(3-äthylbenzthiazolin)-6-sulfonat (ABTS)
    • Bergmeyer H.U. (Ed), Verlag Chemie, Weinheim
    • Bergmeyer H.U., and Bernt E. H2O2-Bestimmung. Verfahren mit 2.2-Azino-di-(3-äthylbenzthiazolin)-6-sulfonat (ABTS). In: Bergmeyer H.U. (Ed). Methoden der enzymatischen Analyse (1974), Verlag Chemie, Weinheim 1257-1258
    • (1974) Methoden der enzymatischen Analyse , pp. 1257-1258
    • Bergmeyer, H.U.1    Bernt, E.2
  • 2
    • 0034028789 scopus 로고    scopus 로고
    • Lignins and lignification: selected issues
    • Boudet A.M. Lignins and lignification: selected issues. Plant Physiol Biochem 38 (2000) 1-16
    • (2000) Plant Physiol Biochem , vol.38 , pp. 1-16
    • Boudet, A.M.1
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for quantitation 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.1
  • 4
    • 0032516025 scopus 로고
    • Sucrose is a signal molecule in assimilate partitioning
    • Chiou T.J., and Bush D.R. Sucrose is a signal molecule in assimilate partitioning. Proc Natl Acad Sci USA 95 (1988) 4784-4788
    • (1988) Proc Natl Acad Sci USA , vol.95 , pp. 4784-4788
    • Chiou, T.J.1    Bush, D.R.2
  • 5
    • 0000157995 scopus 로고
    • Quantification of lignin formation in almond bark in response to wounding and infection by Phytophthora species
    • Doster M.A., and Bostock R.M. Quantification of lignin formation in almond bark in response to wounding and infection by Phytophthora species. Phytopathology 78 (1988) 473-477
    • (1988) Phytopathology , vol.78 , pp. 473-477
    • Doster, M.A.1    Bostock, R.M.2
  • 6
    • 0031420435 scopus 로고    scopus 로고
    • Glucose and stress independently regulate source and sink metabolism and defense mechanisms via signal transduction pathways involving protein phosphorylation
    • Ehness R., Ecker M., Godt D.E., and Roitsch T. Glucose and stress independently regulate source and sink metabolism and defense mechanisms via signal transduction pathways involving protein phosphorylation. Plant Cell 9 (1997) 1825-1841
    • (1997) Plant Cell , vol.9 , pp. 1825-1841
    • Ehness, R.1    Ecker, M.2    Godt, D.E.3    Roitsch, T.4
  • 7
    • 1842535485 scopus 로고    scopus 로고
    • Enhancement of defence responses against bayoud disease by treatment of date palm seedlings with an hypoaggressive Fusarium oxysporum isolate
    • El Hassni M., J'Aiti F., Dihazi A., Ait Barka E., Daayf F., and El Hadrami I. Enhancement of defence responses against bayoud disease by treatment of date palm seedlings with an hypoaggressive Fusarium oxysporum isolate. J Phytopathol 152 (2004) 182-189
    • (2004) J Phytopathol , vol.152 , pp. 182-189
    • El Hassni, M.1    J'Aiti, F.2    Dihazi, A.3    Ait Barka, E.4    Daayf, F.5    El Hadrami, I.6
  • 8
    • 2842539282 scopus 로고    scopus 로고
    • Changes in sugar content during induction of systemic acquired resistance to late blight caused by Phytophthora infestans (Mont.) de Bary in potato
    • Engström K., and Strömberg A. Changes in sugar content during induction of systemic acquired resistance to late blight caused by Phytophthora infestans (Mont.) de Bary in potato. J Phytopathol 144 (1996) 33-36
    • (1996) J Phytopathol , vol.144 , pp. 33-36
    • Engström, K.1    Strömberg, A.2
  • 10
    • 0002423269 scopus 로고    scopus 로고
    • Is ascorbate peroxidase only a scavenger of hydrogen peroxide?
    • Obinger C., Burner U., Ebermann R., Penel C., and Greppin H. (Eds), University of Geneva
    • de Gara L., de Pinto M.C., Paciolla C., Cappetti V., and Arrigoni O. Is ascorbate peroxidase only a scavenger of hydrogen peroxide?. In: Obinger C., Burner U., Ebermann R., Penel C., and Greppin H. (Eds). Plant peroxidases: biochemistry and physiology (1996), University of Geneva 157-162
    • (1996) Plant peroxidases: biochemistry and physiology , pp. 157-162
    • de Gara, L.1    de Pinto, M.C.2    Paciolla, C.3    Cappetti, V.4    Arrigoni, O.5
  • 11
    • 0034522569 scopus 로고    scopus 로고
    • Temporal and spatial assessment of defense responses in resistant and susceptible cabbage varieties during infection with Xanthomonas campestris pv. Campestris
    • Gay P.A., and Tuzun S. Temporal and spatial assessment of defense responses in resistant and susceptible cabbage varieties during infection with Xanthomonas campestris pv. Campestris. Physiol Mol Plant Pathol 57 (2000) 201-210
    • (2000) Physiol Mol Plant Pathol , vol.57 , pp. 201-210
    • Gay, P.A.1    Tuzun, S.2
  • 12
    • 4444272833 scopus 로고    scopus 로고
    • Oxidative metabolism and phenolic compounds in Capsicum annuum L. var. annuum infected by Phytophthora capasici Leon
    • Gayoso C., Pomar F., Merino F., and Bernal M.A. Oxidative metabolism and phenolic compounds in Capsicum annuum L. var. annuum infected by Phytophthora capasici Leon. Sci Horticult 102 (2004) 1-13
    • (2004) Sci Horticult , vol.102 , pp. 1-13
    • Gayoso, C.1    Pomar, F.2    Merino, F.3    Bernal, M.A.4
  • 13
    • 4544284815 scopus 로고    scopus 로고
    • Phenylpropanoids, phenylalanine ammonia lyase and peroxidases in elicitor-challenged cassava (Manihot esculenta) suspension cells and leaves
    • Gomez-Vasquez R., Day R., Buschmann H., Randles S., Beeching J.R., and Cooper R.M. Phenylpropanoids, phenylalanine ammonia lyase and peroxidases in elicitor-challenged cassava (Manihot esculenta) suspension cells and leaves. Ann Bot 94 (2004) 87-97
    • (2004) Ann Bot , vol.94 , pp. 87-97
    • Gomez-Vasquez, R.1    Day, R.2    Buschmann, H.3    Randles, S.4    Beeching, J.R.5    Cooper, R.M.6
  • 15
    • 1842763804 scopus 로고
    • Rapid deposition of lignin in potato tuber tissue as a response to fungi non-pathogenic on potato
    • Hammerschmidt R. Rapid deposition of lignin in potato tuber tissue as a response to fungi non-pathogenic on potato. Physiol Plant Pathol 24 (1984) 33-42
    • (1984) Physiol Plant Pathol , vol.24 , pp. 33-42
    • Hammerschmidt, R.1
  • 16
    • 0002280106 scopus 로고
    • Recherches sur la nutrition minerale des tissues vegetaux cultives in vitro
    • Heller R. Recherches sur la nutrition minerale des tissues vegetaux cultives in vitro. Ann Sci Nat Bot Biol Veg 14 (1954) 1-223
    • (1954) Ann Sci Nat Bot Biol Veg , vol.14 , pp. 1-223
    • Heller, R.1
  • 17
    • 0000020414 scopus 로고    scopus 로고
    • Systemic acquired resistance mediated by the ectopic expression of invertase: possible hexose sensing in the secretory pathway
    • Herbers K., Meuwly P., Frommer W.B., Metraux J.P., and Sonnewald U. Systemic acquired resistance mediated by the ectopic expression of invertase: possible hexose sensing in the secretory pathway. Plant Cell 8 (1996) 793-803
    • (1996) Plant Cell , vol.8 , pp. 793-803
    • Herbers, K.1    Meuwly, P.2    Frommer, W.B.3    Metraux, J.P.4    Sonnewald, U.5
  • 18
    • 0000977882 scopus 로고
    • Isolation and characterization of Populus isoperoxidases involved in the last step of lignin formation
    • Imberty A., Goldberg R., and Catessoen A.M. Isolation and characterization of Populus isoperoxidases involved in the last step of lignin formation. Planta 164 (1985) 221-226
    • (1985) Planta , vol.164 , pp. 221-226
    • Imberty, A.1    Goldberg, R.2    Catessoen, A.M.3
  • 19
    • 0030974632 scopus 로고    scopus 로고
    • Sugar sensing in higher plants
    • Jang J.C., and Sheen J. Sugar sensing in higher plants. Trends Plant Sci 2 (1997) 208-214
    • (1997) Trends Plant Sci , vol.2 , pp. 208-214
    • Jang, J.C.1    Sheen, J.2
  • 20
    • 0000920872 scopus 로고    scopus 로고
    • Carbohydrate-modulated gene expression in plants
    • Koch K.E. Carbohydrate-modulated gene expression in plants. Annu Rev Plant Physiol Plant Mol Biol 47 (1996) 509-540
    • (1996) Annu Rev Plant Physiol Plant Mol Biol , vol.47 , pp. 509-540
    • Koch, K.E.1
  • 21
    • 0000435925 scopus 로고
    • Tissue specificity of tobacco peroxidase isozymes and their induction by wounding and tobacco mosaic virus infection
    • Lagrimini L.M., and Rothstein S. Tissue specificity of tobacco peroxidase isozymes and their induction by wounding and tobacco mosaic virus infection. Plant Physiol 84 (1987) 438-442
    • (1987) Plant Physiol , vol.84 , pp. 438-442
    • Lagrimini, L.M.1    Rothstein, S.2
  • 23
    • 0030861162 scopus 로고    scopus 로고
    • The possible involvement of peroxidase in resistance to Botrytis cinerea in heat treated tomato fruit
    • Lurie S., Fallik E., Handros A., and Shapira R. The possible involvement of peroxidase in resistance to Botrytis cinerea in heat treated tomato fruit. Physiol Mol Plant Pathol 50 (1997) 141-149
    • (1997) Physiol Mol Plant Pathol , vol.50 , pp. 141-149
    • Lurie, S.1    Fallik, E.2    Handros, A.3    Shapira, R.4
  • 24
    • 33845992761 scopus 로고
    • The assay of catalase and peroxidase
    • Glick D. (Ed), Interscience Publishers Inc., New York
    • Maehly A.C., and Chance B. The assay of catalase and peroxidase. In: Glick D. (Ed). Methods of biochemical analysis (1954), Interscience Publishers Inc., New York 357-425
    • (1954) Methods of biochemical analysis , pp. 357-425
    • Maehly, A.C.1    Chance, B.2
  • 25
    • 0028247896 scopus 로고
    • Plant peroxidases: interaction between their prosthetic groups
    • Maranon M.J.R., and van Huystee R.B. Plant peroxidases: interaction between their prosthetic groups. Phytochemistry 37 (1994) 1217-1225
    • (1994) Phytochemistry , vol.37 , pp. 1217-1225
    • Maranon, M.J.R.1    van Huystee, R.B.2
  • 26
    • 0035839041 scopus 로고    scopus 로고
    • Mechanisms of survival of necrotrophic fungal plant pathogens in hosts expressing the hypersensitive response
    • Mayer A.M., Staples R.C., and Gil-ad N.L. Mechanisms of survival of necrotrophic fungal plant pathogens in hosts expressing the hypersensitive response. Phytochemistry 58 (2001) 33-41
    • (2001) Phytochemistry , vol.58 , pp. 33-41
    • Mayer, A.M.1    Staples, R.C.2    Gil-ad, N.L.3
  • 27
    • 0028255693 scopus 로고
    • Cell suspension cultures of spruce (Picea abies): inactivation of extracellular enzymes by fungal elicitor-induced transient release of hydrogen peroxide (oxidative burst)
    • Messner B., and Boll M. Cell suspension cultures of spruce (Picea abies): inactivation of extracellular enzymes by fungal elicitor-induced transient release of hydrogen peroxide (oxidative burst). Plant Cell Tissue Organ Culture 39 (1994) 69-78
    • (1994) Plant Cell Tissue Organ Culture , vol.39 , pp. 69-78
    • Messner, B.1    Boll, M.2
  • 28
    • 19544380964 scopus 로고    scopus 로고
    • The role of carbohydrates in early metabolic responses of germinating lupine seeds to Fusarium oxysporum f. sp. lupine
    • Morkunas I., Kozłowska M., and Ratajczak W. The role of carbohydrates in early metabolic responses of germinating lupine seeds to Fusarium oxysporum f. sp. lupine. Acta Agrobot 55 (2002) 247-254
    • (2002) Acta Agrobot , vol.55 , pp. 247-254
    • Morkunas, I.1    Kozłowska, M.2    Ratajczak, W.3
  • 29
    • 3142649185 scopus 로고    scopus 로고
    • Response of embryo axes of germinating seeds of yellow lupine to Fusarium oxysporum
    • Morkunas I., Bednarski W., and Kozłowska M. Response of embryo axes of germinating seeds of yellow lupine to Fusarium oxysporum. Plant Physiol Biochem 42 (2004) 493-499
    • (2004) Plant Physiol Biochem , vol.42 , pp. 493-499
    • Morkunas, I.1    Bednarski, W.2    Kozłowska, M.3
  • 30
    • 19544380741 scopus 로고    scopus 로고
    • Sucrose-stimulated accumulation of isoflavonoids as a defense response of lupine to Fusarium oxysporum
    • Morkunas I., Marczak Ł., Stachowiak J., and Stobiecki M. Sucrose-stimulated accumulation of isoflavonoids as a defense response of lupine to Fusarium oxysporum. Plant Physiol Biochem 43 (2005) 363-373
    • (2005) Plant Physiol Biochem , vol.43 , pp. 363-373
    • Morkunas, I.1    Marczak, Ł.2    Stachowiak, J.3    Stobiecki, M.4
  • 31
    • 0036007886 scopus 로고    scopus 로고
    • Infection of leaves of Arabidopsis thaliana by Botrytis cinerea: changes in ascorbic acid, free radicals and lipid peroxidation products
    • Muckenschnabel I., Goodman B.A., Williamson B., Lyon G.D., and Deighton N. Infection of leaves of Arabidopsis thaliana by Botrytis cinerea: changes in ascorbic acid, free radicals and lipid peroxidation products. J Exp Bot 53 (2002) 207-214
    • (2002) J Exp Bot , vol.53 , pp. 207-214
    • Muckenschnabel, I.1    Goodman, B.A.2    Williamson, B.3    Lyon, G.D.4    Deighton, N.5
  • 32
    • 0010282460 scopus 로고
    • Hydrogen peroxide is scavenged by ascorbate-specific peroxidase in spinach chloroplasts
    • Nakano Y., and 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
  • 33
    • 0033545534 scopus 로고    scopus 로고
    • Fungal peroxidase: its structure, function, and applications
    • Nakayama T., and Amachi T. Fungal peroxidase: its structure, function, and applications. J Mol Catal B: Enzymatic 6 (1999) 185-198
    • (1999) J Mol Catal B: Enzymatic , vol.6 , pp. 185-198
    • Nakayama, T.1    Amachi, T.2
  • 34
    • 0033153127 scopus 로고    scopus 로고
    • Source-sink regulation by sugar and stress
    • Roitsch T. Source-sink regulation by sugar and stress. Curr Opin Plant Biol 2 (1999) 198-206
    • (1999) Curr Opin Plant Biol , vol.2 , pp. 198-206
    • Roitsch, T.1
  • 35
    • 0035030687 scopus 로고    scopus 로고
    • Release of reactive oxygen intermediates (superoxide radicals, hydrogen peroxide, and hydroxyl radicals) and peroxidase in germinating radish seeds controlled by light, gibberellin, and abscisic acid
    • Schopfer P., Plachy C., and Frahry G. Release of reactive oxygen intermediates (superoxide radicals, hydrogen peroxide, and hydroxyl radicals) and peroxidase in germinating radish seeds controlled by light, gibberellin, and abscisic acid. Plant Physiol 125 (2001) 1591-1602
    • (2001) Plant Physiol , vol.125 , pp. 1591-1602
    • Schopfer, P.1    Plachy, C.2    Frahry, G.3
  • 36
    • 0033776330 scopus 로고    scopus 로고
    • Deglucosidation of quercetin glucosides to the aglycone and formation of antifungal agents by peroxidase-dependent oxidation of quercetin on browning of onion scales
    • Takahama U., and Hirota S. Deglucosidation of quercetin glucosides to the aglycone and formation of antifungal agents by peroxidase-dependent oxidation of quercetin on browning of onion scales. Plant Cell Physiol 41 (2000) 1021-1029
    • (2000) Plant Cell Physiol , vol.41 , pp. 1021-1029
    • Takahama, U.1    Hirota, S.2
  • 37
    • 0000488624 scopus 로고
    • Activity, isozyme pattern, and cellular localization of peroxidase as related to systemic resistance of tobacco to blue mold (Peronospora tabacina) and to tobacco mosaic virus
    • Ye X.S., Pan S.Q., and Kuć J. Activity, isozyme pattern, and cellular localization of peroxidase as related to systemic resistance of tobacco to blue mold (Peronospora tabacina) and to tobacco mosaic virus. Phytopathology 80 (1990) 1295-1299
    • (1990) Phytopathology , vol.80 , pp. 1295-1299
    • Ye, X.S.1    Pan, S.Q.2    Kuć, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.