메뉴 건너뛰기




Volumn 55, Issue , 2012, Pages 23-32

Mercury-induced biochemical and proteomic changes in rice roots

Author keywords

Antioxidative enzymes; Lipid peroxidation; Mercury; Oxidative stress; Proteome

Indexed keywords

ASCORBATE PEROXIDASE; CATALASE; GLUTATHIONE; MALONALDEHYDE; MERCURY; PEROXIDASE; PHYTOHORMONE; PROTEOME; SUPEROXIDE DISMUTASE; VEGETABLE PROTEIN;

EID: 84859803902     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2012.03.008     Document Type: Article
Times cited : (68)

References (43)
  • 1
    • 20444364213 scopus 로고    scopus 로고
    • Uptake of mercury (Hg) by seedlings of rice (Oryza sativa L.) grown in solution culture and interactions with arsenate uptake
    • Du X., Zhu Y., Liu W., Zhao X. Uptake of mercury (Hg) by seedlings of rice (Oryza sativa L.) grown in solution culture and interactions with arsenate uptake. Environ. Exp. Bot. 2005, 54:1-7.
    • (2005) Environ. Exp. Bot. , vol.54 , pp. 1-7
    • Du, X.1    Zhu, Y.2    Liu, W.3    Zhao, X.4
  • 2
    • 33845412045 scopus 로고    scopus 로고
    • Metabolic adaptations to mercury-induced oxidative stress in roots of Medicago sativa L.
    • Zhou Z.S., Huang S.Q., Guo K., Mehta S.K., Zhang P.C., Yang Z.M. Metabolic adaptations to mercury-induced oxidative stress in roots of Medicago sativa L. J. Inorg. Biochem. 2007, 101:1-9.
    • (2007) J. Inorg. Biochem. , vol.101 , pp. 1-9
    • Zhou, Z.S.1    Huang, S.Q.2    Guo, K.3    Mehta, S.K.4    Zhang, P.C.5    Yang, Z.M.6
  • 3
    • 0033912163 scopus 로고    scopus 로고
    • Phytochelatins and their roles in heavy metal detoxification
    • Cobbett C.S. Phytochelatins and their roles in heavy metal detoxification. Plant Physiol. 2000, 123:825-832.
    • (2000) Plant Physiol. , vol.123 , pp. 825-832
    • Cobbett, C.S.1
  • 5
    • 41749120981 scopus 로고    scopus 로고
    • Effects of copper on growth, antioxidant enzymes and phenylalanine ammonia-lyase activities in Jatropha curcas L. seedling
    • Gao S., Yan R., Cao M., Yang W., Wang S., Chen F. Effects of copper on growth, antioxidant enzymes and phenylalanine ammonia-lyase activities in Jatropha curcas L. seedling. Plant Soil Environ. 2008, 54:117-122.
    • (2008) Plant Soil Environ. , vol.54 , pp. 117-122
    • Gao, S.1    Yan, R.2    Cao, M.3    Yang, W.4    Wang, S.5    Chen, F.6
  • 6
    • 0002844238 scopus 로고
    • Production and action of active oxygen species in photosynthetic tissues
    • CRC Press, Boca Raton, C.H. Foyer, P.M. Mullineaux (Eds.)
    • Asada K. Production and action of active oxygen species in photosynthetic tissues. Causes of Photooxidative Stress and Amelioration of Defence Systems in Plants 1994, 77-104. CRC Press, Boca Raton. C.H. Foyer, P.M. Mullineaux (Eds.).
    • (1994) Causes of Photooxidative Stress and Amelioration of Defence Systems in Plants , pp. 77-104
    • Asada, K.1
  • 7
    • 70449562807 scopus 로고    scopus 로고
    • Mercury-induced changes in growth variables and antioxidative enzyme activities in Indian mustard
    • Ansari M.K.A., Ahmad A., Umar S., Iqbal M. Mercury-induced changes in growth variables and antioxidative enzyme activities in Indian mustard. J. Plant Int. 2009, 4:131-136.
    • (2009) J. Plant Int. , vol.4 , pp. 131-136
    • Ansari, M.K.A.1    Ahmad, A.2    Umar, S.3    Iqbal, M.4
  • 8
    • 79960971804 scopus 로고    scopus 로고
    • Plant proteome changes under abiotic stress-contribution of proteomics studies to understanding plant stress response
    • Kosova K., Vitamvas P., Prasil I.T., Renaut J. Plant proteome changes under abiotic stress-contribution of proteomics studies to understanding plant stress response. J. Proteomics 2011, 74:1301-1322.
    • (2011) J. Proteomics , vol.74 , pp. 1301-1322
    • Kosova, K.1    Vitamvas, P.2    Prasil, I.T.3    Renaut, J.4
  • 9
    • 33644848361 scopus 로고    scopus 로고
    • Rice proteomics: a cornerstone for cereal food crop proteomes
    • Agrawal G.K., Rakwal R. Rice proteomics: a cornerstone for cereal food crop proteomes. Mass Spectrom. Rev. 2006, 25:1-53.
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 1-53
    • Agrawal, G.K.1    Rakwal, R.2
  • 10
    • 79954997524 scopus 로고    scopus 로고
    • Rice proteomics: a move toward expanded proteome coverage to comparative and functional proteomics uncovers the mysteries of rice and plant biology
    • Agrawal G.K., Rakwal R. Rice proteomics: a move toward expanded proteome coverage to comparative and functional proteomics uncovers the mysteries of rice and plant biology. Proteomics 2011, 11:1630-1649.
    • (2011) Proteomics , vol.11 , pp. 1630-1649
    • Agrawal, G.K.1    Rakwal, R.2
  • 11
    • 33846901307 scopus 로고    scopus 로고
    • Burning characteristics and emission products related to metallic content in incense
    • Lin T.C., Yang C.R., Chang F.H. Burning characteristics and emission products related to metallic content in incense. J. Hazard. Mater. 2007, 140:165-172.
    • (2007) J. Hazard. Mater. , vol.140 , pp. 165-172
    • Lin, T.C.1    Yang, C.R.2    Chang, F.H.3
  • 12
    • 74249090986 scopus 로고    scopus 로고
    • A different role for hydrogen peroxide and the antioxidative system under short and long salt stress in Brassica oleracea roots
    • Hernandez M., Fernandez-Garcia N., Diaz-Vivancos P., Olmos E. A different role for hydrogen peroxide and the antioxidative system under short and long salt stress in Brassica oleracea roots. J. Exp. Bot. 2010, 61:521-535.
    • (2010) J. Exp. Bot. , vol.61 , pp. 521-535
    • Hernandez, M.1    Fernandez-Garcia, N.2    Diaz-Vivancos, P.3    Olmos, E.4
  • 13
    • 0023501904 scopus 로고
    • Histochemical detection of lipid peroxidation in the liver of bromobenzene-poisoned mice
    • Pompella A., Maellaro E., Casini A.F., Comporti M. Histochemical detection of lipid peroxidation in the liver of bromobenzene-poisoned mice. Am. J. Pathol. 1987, 129:295-301.
    • (1987) Am. J. Pathol. , vol.129 , pp. 295-301
    • Pompella, A.1    Maellaro, E.2    Casini, A.F.3    Comporti, M.4
  • 14
    • 30344451367 scopus 로고    scopus 로고
    • Nitric oxide reduces aluminum toxicity by preventing oxidative stress in the roots of Cassia tora L.
    • Wang Y.S., Yang Z.M. Nitric oxide reduces aluminum toxicity by preventing oxidative stress in the roots of Cassia tora L. Plant Cell Physiol. 2005, 46:1915-1923.
    • (2005) Plant Cell Physiol. , vol.46 , pp. 1915-1923
    • Wang, Y.S.1    Yang, Z.M.2
  • 15
    • 0027177774 scopus 로고
    • Detection of ascorbate peroxidase activity in native gels by inhibition of the ascorbate-dependent reduction of nitroblue tetrazolium
    • Mittler R., Zilinskas B.A. Detection of ascorbate peroxidase activity in native gels by inhibition of the ascorbate-dependent reduction of nitroblue tetrazolium. Anal. Biochem. 1993, 212:540-546.
    • (1993) Anal. Biochem. , vol.212 , pp. 540-546
    • Mittler, R.1    Zilinskas, B.A.2
  • 16
    • 0037694117 scopus 로고    scopus 로고
    • Effect of light on peroxidase and lignin synthesis in mungbean hypocotyls
    • Chen Y.A., Shin J.W., Liu Z.H. Effect of light on peroxidase and lignin synthesis in mungbean hypocotyls. Plant Physiol. Biochem. 2002, 40:33-39.
    • (2002) Plant Physiol. Biochem. , vol.40 , pp. 33-39
    • Chen, Y.A.1    Shin, J.W.2    Liu, Z.H.3
  • 17
    • 0000459986 scopus 로고
    • Seasonal variation in the antioxidant system of eastern white pine needles: evidence for thermal dependence
    • Anderson J.V., Chevone B.I., Hess J.L. Seasonal variation in the antioxidant system of eastern white pine needles: evidence for thermal dependence. Plant Physiol. 1992, 98:501-508.
    • (1992) Plant Physiol. , vol.98 , pp. 501-508
    • Anderson, J.V.1    Chevone, B.I.2    Hess, J.L.3
  • 18
    • 0024119482 scopus 로고
    • Two dimensional electrophoresis with immobilized pH gradients of leaf proteins from barley (Hordeum vulgare): method, reproducibility and genetic aspects
    • Gorg A., Postel W., Domscheit A., Gunther S. Two dimensional electrophoresis with immobilized pH gradients of leaf proteins from barley (Hordeum vulgare): method, reproducibility and genetic aspects. Electrophoresis 1988, 9:681-692.
    • (1988) Electrophoresis , vol.9 , pp. 681-692
    • Gorg, A.1    Postel, W.2    Domscheit, A.3    Gunther, S.4
  • 22
    • 35348817940 scopus 로고    scopus 로고
    • ROS and phytohormones in plant-plant allelopathic interaction
    • Bogatek R., Gniazdowska A. ROS and phytohormones in plant-plant allelopathic interaction. Plant Signal. Behav. 2007, 2:317-318.
    • (2007) Plant Signal. Behav. , vol.2 , pp. 317-318
    • Bogatek, R.1    Gniazdowska, A.2
  • 23
    • 33750562340 scopus 로고    scopus 로고
    • Over-expression of OsAGAP, an ARF-GAP, interferes with auxin influx, vesicle trafficking and root development
    • Zhuang X., Jiang J., Li J., Ma Q., Xu Y., Xue Y., Xu Z., Chong K. Over-expression of OsAGAP, an ARF-GAP, interferes with auxin influx, vesicle trafficking and root development. Plant J. 2006, 48:581-591.
    • (2006) Plant J. , vol.48 , pp. 581-591
    • Zhuang, X.1    Jiang, J.2    Li, J.3    Ma, Q.4    Xu, Y.5    Xue, Y.6    Xu, Z.7    Chong, K.8
  • 24
    • 0029058524 scopus 로고
    • Chaperone like activity of protein disulfide isomerase in the refolding of rhodanese
    • Song J.L., Wang C.C. Chaperone like activity of protein disulfide isomerase in the refolding of rhodanese. Eur. J. Biochem. 1995, 231:312-316.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 312-316
    • Song, J.L.1    Wang, C.C.2
  • 26
    • 48249085699 scopus 로고    scopus 로고
    • Quantitative changes in protein expression of cadmium exposed poplar plants
    • Kieffer P., Dommes J., Hoffmann L., Hausman J.F., Renaut J. Quantitative changes in protein expression of cadmium exposed poplar plants. Proteomics 2008, 8:2514-2530.
    • (2008) Proteomics , vol.8 , pp. 2514-2530
    • Kieffer, P.1    Dommes, J.2    Hoffmann, L.3    Hausman, J.F.4    Renaut, J.5
  • 28
    • 33645472456 scopus 로고    scopus 로고
    • Comparative proteomic analysis provides new insights into chilling stress responses in rice
    • Yan S.P., Zhang Q.Y., Tang Z.C., Su W.A., Sun W.N. Comparative proteomic analysis provides new insights into chilling stress responses in rice. Mol. Cell Proteomics 2006, 5:484-496.
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 484-496
    • Yan, S.P.1    Zhang, Q.Y.2    Tang, Z.C.3    Su, W.A.4    Sun, W.N.5
  • 29
    • 34247588074 scopus 로고    scopus 로고
    • Metabolic alterations proposed by proteome in rice roots grown under low P and high Al concentration under low pH
    • Fukuda T., Saito A., Wasaki J., Shinano T., Osaki M. Metabolic alterations proposed by proteome in rice roots grown under low P and high Al concentration under low pH. Plant Sci. 2007, 172:1157-1165.
    • (2007) Plant Sci. , vol.172 , pp. 1157-1165
    • Fukuda, T.1    Saito, A.2    Wasaki, J.3    Shinano, T.4    Osaki, M.5
  • 30
    • 66449136555 scopus 로고    scopus 로고
    • Identification of elicitor responsive proteins in rice leaves by a proteomic approach
    • Liao M., Li Y., Wang Z. Identification of elicitor responsive proteins in rice leaves by a proteomic approach. Proteomics 2009, 9:2809-2819.
    • (2009) Proteomics , vol.9 , pp. 2809-2819
    • Liao, M.1    Li, Y.2    Wang, Z.3
  • 31
    • 65049087669 scopus 로고    scopus 로고
    • Expression analysis of nine rice heat shock protein genes under abiotic stresses and ABA treatment
    • Zou J., Liu A., Chen X., Zhou X., Gao G., Wang W., Zhang X. Expression analysis of nine rice heat shock protein genes under abiotic stresses and ABA treatment. J. Plant Physiol. 2009, 166:851-861.
    • (2009) J. Plant Physiol. , vol.166 , pp. 851-861
    • Zou, J.1    Liu, A.2    Chen, X.3    Zhou, X.4    Gao, G.5    Wang, W.6    Zhang, X.7
  • 35
    • 34248541296 scopus 로고    scopus 로고
    • Down-regulation of hydroxycinnamoyl CoA: shikimate hydroxycinnamoyl transferase in transgenic alfalfa affects lignification, development and forage quality
    • Shadle G., Chen F., Srinivasa Reddy M.S., Jackson L., Nakashima J., Dixon R.A. Down-regulation of hydroxycinnamoyl CoA: shikimate hydroxycinnamoyl transferase in transgenic alfalfa affects lignification, development and forage quality. Phytochemistry 2007, 68:1521-1529.
    • (2007) Phytochemistry , vol.68 , pp. 1521-1529
    • Shadle, G.1    Chen, F.2    Srinivasa Reddy, M.S.3    Jackson, L.4    Nakashima, J.5    Dixon, R.A.6
  • 36
    • 30744475972 scopus 로고    scopus 로고
    • Peroxidase activity and lignification in soybean root growth-inhibition by juglone
    • Bohm P.A.F., Zanardo F.M.L., Ferrarese M.L.L., Ferrarese-Filho O. Peroxidase activity and lignification in soybean root growth-inhibition by juglone. Biol. Plant 2006, 50:315-317.
    • (2006) Biol. Plant , vol.50 , pp. 315-317
    • Bohm, P.A.F.1    Zanardo, F.M.L.2    Ferrarese, M.L.L.3    Ferrarese-Filho, O.4
  • 38
    • 0030918183 scopus 로고    scopus 로고
    • Isolation of a cDNA coding for an ubiquitin-conjugating enzyme UBC1 of tomato-the first stress-induced UBC of higher plants
    • Feussner K., Feussner I., Leopold I., Wasternack C. Isolation of a cDNA coding for an ubiquitin-conjugating enzyme UBC1 of tomato-the first stress-induced UBC of higher plants. FEBS Lett. 1997, 409:211-215.
    • (1997) FEBS Lett. , vol.409 , pp. 211-215
    • Feussner, K.1    Feussner, I.2    Leopold, I.3    Wasternack, C.4
  • 40
    • 77952260641 scopus 로고    scopus 로고
    • Genome-wide characterisation of the Gcn5 histone acetyltransferase in budding yeast during stress adaptation reveals evolutionarily conserved and diverged roles
    • Xue-Franzen Y., Johnsson A., Brodin D., Henriksson J., Burglin T.R., Wright A.P. Genome-wide characterisation of the Gcn5 histone acetyltransferase in budding yeast during stress adaptation reveals evolutionarily conserved and diverged roles. BMC Genomics 2010, 11:200-216.
    • (2010) BMC Genomics , vol.11 , pp. 200-216
    • Xue-Franzen, Y.1    Johnsson, A.2    Brodin, D.3    Henriksson, J.4    Burglin, T.R.5    Wright, A.P.6
  • 41
    • 62349111195 scopus 로고    scopus 로고
    • Epigenetic regulation of stress responses in plants
    • Chinnusamy V., Zhu J.K. Epigenetic regulation of stress responses in plants. Curr. Opin. Plant Biol. 2009, 12:133-139.
    • (2009) Curr. Opin. Plant Biol. , vol.12 , pp. 133-139
    • Chinnusamy, V.1    Zhu, J.K.2
  • 43
    • 1242294378 scopus 로고    scopus 로고
    • The defense response of germinating maize embryos against fungal infection: a proteomics approach
    • Campo S., Carrascal M., Coca M., Abian J., San Segundo B. The defense response of germinating maize embryos against fungal infection: a proteomics approach. Proteomics 2004, 4:383-396.
    • (2004) Proteomics , vol.4 , pp. 383-396
    • Campo, S.1    Carrascal, M.2    Coca, M.3    Abian, J.4    San Segundo, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.