메뉴 건너뛰기




Volumn 8, Issue 2, 2013, Pages 125-133

Cadmium affects the NADP-thioredoxin reductase/thioredoxin system in germinating pea seeds

Author keywords

cadmium; germination; pea; thioredoxin

Indexed keywords


EID: 84877286999     PISSN: 17429145     EISSN: 17429153     Source Type: Journal    
DOI: 10.1080/17429145.2012.689865     Document Type: Article
Times cited : (14)

References (51)
  • 1
    • 0033395864 scopus 로고    scopus 로고
    • Peroxiredoxin antioxidants in seed physiology
    • Aalen, RB. 1999. Peroxiredoxin antioxidants in seed physiology. Seed Sci Res., 9: 285 - 295.
    • (1999) Seed Sci Res. , vol.9 , pp. 285-295
    • Aalen, R.B.1
  • 6
    • 0021103670 scopus 로고
    • Plant seeds contain several thioredoxins of regular size
    • Berstermann, A, Vogt, K and Follmann, H. 1983. Plant seeds contain several thioredoxins of regular size. Eur J Biochem., 131: 139 - 344.
    • (1983) Eur J Biochem. , vol.131 , pp. 139-344
    • Berstermann, A.1    Vogt, K.2    Follmann, H.3
  • 7
    • 0029928068 scopus 로고    scopus 로고
    • Thiocalsin: a thioredoxin- linked, substrate-specific protease dependent on calcium
    • Besse, I, Wong, JH, Kobrehel, K and Buchanan, BB. 1996. Thiocalsin: a thioredoxin- linked, substrate-specific protease dependent on calcium. Proc Natl Acad Sci USA., 93: 3169 - 3175.
    • (1996) Proc Natl Acad Sci USA. , vol.93 , pp. 3169-3175
    • Besse, I.1    Wong, J.H.2    Kobrehel, K.3    Buchanan, B.B.4
  • 8
    • 0031420258 scopus 로고    scopus 로고
    • Seed germination and dormancy
    • Bewley DJ. 1997. Seed germination and dormancy. The Plant Cell. 9: 1055 - 1066.
    • (1997) The Plant Cell , vol.9 , pp. 1055-1066
    • Bewley, D.J.1
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantity of protein utilizing the principle of protein dye binding
    • Bradford, MM. 1976. A rapid and sensitive method for the quantitation of microgram quantity 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
  • 10
    • 0038038526 scopus 로고    scopus 로고
    • Potato plants lacking the CDSP32 plastidic thioredoxin exhibit overoxidation of the BAS1 2-cysteine peroxiredoxin and increased lipid peroxidation in thylakoids under photooxidative stress
    • Broin, M and Rey, P. 2003. Potato plants lacking the CDSP32 plastidic thioredoxin exhibit overoxidation of the BAS1 2-cysteine peroxiredoxin and increased lipid peroxidation in thylakoids under photooxidative stress. Plant Physiol., 132: 1335 - 1343.
    • (2003) Plant Physiol. , vol.132 , pp. 1335-1343
    • Broin, M.1    Rey, P.2
  • 12
    • 12144276615 scopus 로고    scopus 로고
    • Effects of cadmium and copper on antioxidant capacities, lignification and auxin degradation in leaves of pea (Pisum sativum L.) seedling
    • Chaoui, A and El Ferjani, E. 2005. Effects of cadmium and copper on antioxidant capacities, lignification and auxin degradation in leaves of pea (Pisum sativum L.) seedling. Comptes Rendus Biol., 328: 23 - 31.
    • (2005) Comptes Rendus Biol. , vol.328 , pp. 23-31
    • Chaoui, A.1    El Ferjani, E.2
  • 13
    • 9644282867 scopus 로고    scopus 로고
    • Effects of cadmium and copper on peroxidase, NADH oxidase and IAA oxidase activities in cell wall, soluble and microsomal membrane fractions of pea roots
    • Chaoui, A, Jarrar, B and El Ferjani, E. 2004. Effects of cadmium and copper on peroxidase, NADH oxidase and IAA oxidase activities in cell wall, soluble and microsomal membrane fractions of pea roots. J Plant Physiol., 161: 1225 - 1234.
    • (2004) J Plant Physiol. , vol.161 , pp. 1225-1234
    • Chaoui, A.1    Jarrar, B.2    El Ferjani, E.3
  • 14
    • 33751509841 scopus 로고    scopus 로고
    • Mitochondrial thioredoxin in regulation of oxidant-induced cell death
    • Chen, Y, Cai, J and Jones, DP. 2006. Mitochondrial thioredoxin in regulation of oxidant-induced cell death. FEBS Lett., 580: 6596 - 6602.
    • (2006) FEBS Lett. , vol.580 , pp. 6596-6602
    • Chen, Y.1    Cai, J.2    Jones, D.P.3
  • 15
    • 0034025143 scopus 로고    scopus 로고
    • Phytochelatin biosynthesis and function in heavy-metal detoxification
    • Cobbett, CS. 2000. Phytochelatin biosynthesis and function in heavy-metal detoxification. Curr Opin Plant Biol., 3: 211 - 216.
    • (2000) Curr Opin Plant Biol. , vol.3 , pp. 211-216
    • Cobbett, C.S.1
  • 17
    • 35948992852 scopus 로고    scopus 로고
    • Cadmium response and redoxin targets in Chlamydomonas reinhardtii: a proteomic approach
    • Gillet, S, Decottignies, P, Chardonnet, S and Le Maréchal, P. 2006. Cadmium response and redoxin targets in Chlamydomonas reinhardtii: a proteomic approach. Photosyn Res., 89: 201 - 211.
    • (2006) Photosyn Res. , vol.89 , pp. 201-211
    • Gillet, S.1    Decottignies, P.2    Chardonnet, S.3    Le Maréchal, P.4
  • 18
    • 28744434298 scopus 로고    scopus 로고
    • Differential oxidation of thioredoxin-1, thioredoxin-2, and glutathione by metal ions
    • Hansen, JM, Zhang, H and Jones, DP. 2006. Differential oxidation of thioredoxin-1, thioredoxin-2, and glutathione by metal ions. Free Rad Biol Med., 40: 138 - 145.
    • (2006) Free Rad Biol Med. , vol.40 , pp. 138-145
    • Hansen, J.M.1    Zhang, H.2    Jones, D.P.3
  • 19
    • 66649085738 scopus 로고    scopus 로고
    • Structural and evolutionary aspects of thioredoxin reductases in photosynthetic organisms
    • Jacquot, JP, Eklund, H, Rouhier, N and Schürmann, P. 2009. Structural and evolutionary aspects of thioredoxin reductases in photosynthetic organisms. Trends Plant Sci., 14: 336 - 343.
    • (2009) Trends Plant Sci. , vol.14 , pp. 336-343
    • Jacquot, J.P.1    Eklund, H.2    Rouhier, N.3    Schürmann, P.4
  • 21
    • 0018072333 scopus 로고
    • Evidence for the existence of several enzyme specific thioredoxins in plants
    • Jacquot, JP, Vidal, J, Gadal, P and Schürmann, P. 1978. Evidence for the existence of several enzyme specific thioredoxins in plants. FEBS Lett., 96: 243 - 246.
    • (1978) FEBS Lett. , vol.96 , pp. 243-246
    • Jacquot, J.P.1    Vidal, J.2    Gadal, P.3    Schürmann, P.4
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature., 227: 680 - 685.
    • (1970) Nature. , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 1642547085 scopus 로고    scopus 로고
    • The Arabidopsis cytosolic thioredoxin h5 gene induction by oxidative stress and its W-box-mediated response to pathogen elicitor
    • Laloi, C, Mestres-Ortega, D, Marco, Y, Meyer, Y and Reichheld, JP. 2004. The Arabidopsis cytosolic thioredoxin h5 gene induction by oxidative stress and its W-box-mediated response to pathogen elicitor. Plant Physiol., 134: 1006 - 1016.
    • (2004) Plant Physiol. , vol.134 , pp. 1006-1016
    • Laloi, C.1    Mestres-Ortega, D.2    Marco, Y.3    Meyer, Y.4    Reichheld, J.P.5
  • 28
    • 0029839611 scopus 로고    scopus 로고
    • New evidence for a role of thioredoxin h in germination and seedling development
    • Lozano, RM, Wong, JH, Yee, BC, Peters, A, Kobrehel, K and Buchanan, BB. 1996. New evidence for a role of thioredoxin h in germination and seedling development. Planta., 200: 100 - 106.
    • (1996) Planta. , vol.200 , pp. 100-106
    • Lozano, R.M.1    Wong, J.H.2    Yee, B.C.3    Peters, A.4    Kobrehel, K.5    Buchanan, B.B.6
  • 30
    • 77956989433 scopus 로고
    • Cycling assay for nicotinamide adenine dinucleotides
    • Matsumura, H and Miyachi, S. 1980. Cycling assay for nicotinamide adenine dinucleotides. Methods Enzymol., 69: 465 - 470.
    • (1980) Methods Enzymol. , vol.69 , pp. 465-470
    • Matsumura, H.1    Miyachi, S.2
  • 31
    • 0030990260 scopus 로고    scopus 로고
    • Nickel and cadmium toxicity and enzymatic activity in Ni-tolerant and non-tolerant populations of Silene italica Pers
    • Mattioni, C, Gabbrielli, R, Vangronsveld, J and Clijsters, H. 1997. Nickel and cadmium toxicity and enzymatic activity in Ni-tolerant and non-tolerant populations of Silene italica Pers. J Plant Physiol., 150: 173 - 177.
    • (1997) J Plant Physiol. , vol.150 , pp. 173-177
    • Mattioni, C.1    Gabbrielli, R.2    Vangronsveld, J.3    Clijsters, H.4
  • 32
    • 0036119804 scopus 로고    scopus 로고
    • Classification of plant thioredoxins by sequence similarity and intron position
    • Meyer, Y, Vignols, F and Reichheld, JP. 2002. Classification of plant thioredoxins by sequence similarity and intron position. Methods Enzymol., 347: 394 - 402.
    • (2002) Methods Enzymol. , vol.347 , pp. 394-402
    • Meyer, Y.1    Vignols, F.2    Reichheld, J.P.3
  • 33
    • 12144254081 scopus 로고    scopus 로고
    • Biochemical changes associated with cadmium and copper stress in germinating pea seeds (Pisum sativum L.)
    • Mihoub, A, Chaoui, A and El Ferjani, E. 2005. Biochemical changes associated with cadmium and copper stress in germinating pea seeds (Pisum sativum L.). Comptes Rendus Biol., 328: 33 - 41.
    • (2005) Comptes Rendus Biol. , vol.328 , pp. 33-41
    • Mihoub, A.1    Chaoui, A.2    El Ferjani, E.3
  • 34
    • 0038038334 scopus 로고    scopus 로고
    • Identification and differential expression of two thioredoxin h isoforms in germinating seeds from pea
    • Montrichard, F, Renard, M, Alkhalfioui, F, Duval, FD and Macherel, D. 2003. Identification and differential expression of two thioredoxin h isoforms in germinating seeds from pea. Plant Physiol., 132: 1707 - 1715.
    • (2003) Plant Physiol. , vol.132 , pp. 1707-1715
    • Montrichard, F.1    Renard, M.2    Alkhalfioui, F.3    Duval, F.D.4    Macherel, D.5
  • 35
    • 0033914955 scopus 로고    scopus 로고
    • Expression of thioredoxins f and m, and of their targets fructose-1,6-bisphosphatase and NADP-malate dehydrogenase, in pea plants grown under normal and light/temperature stress conditions
    • Pagano, EA, Chueca, A and López-Gorge, J. 2000. Expression of thioredoxins f and m, and of their targets fructose-1,6-bisphosphatase and NADP-malate dehydrogenase, in pea plants grown under normal and light/temperature stress conditions. J Exp Bot., 51: 1299 - 1307.
    • (2000) J Exp Bot. , vol.51 , pp. 1299-1307
    • Pagano, E.A.1    Chueca, A.2    López-Gorge, J.3
  • 36
    • 77951498659 scopus 로고    scopus 로고
    • Membrane damage and solute leakage from germinating pea seed under cadmium stress
    • Rahoui, S, Chaoui, A and El Ferjani, E. 2010. Membrane damage and solute leakage from germinating pea seed under cadmium stress. J Hazard Mater., 178: 1128 - 1131.
    • (2010) J Hazard Mater. , vol.178 , pp. 1128-1131
    • Rahoui, S.1    Chaoui, A.2    El Ferjani, E.3
  • 38
    • 58349083055 scopus 로고    scopus 로고
    • Respiratory metabolism in the embryonic axis of germinating pea seed exposed to cadmium
    • Smiri, M, Chaoui, A and El Ferjani, E. 2009. Respiratory metabolism in the embryonic axis of germinating pea seed exposed to cadmium. J Plant Physiol., 166: 259 - 269.
    • (2009) J Plant Physiol. , vol.166 , pp. 259-269
    • Smiri, M.1    Chaoui, A.2    El Ferjani, E.3
  • 39
    • 77957567375 scopus 로고    scopus 로고
    • Interaction between heavy metals and thiol-linked redox reactions in germination
    • Smiri, M, Chaoui, A and El Ferjani, E. 2010a. Interaction between heavy metals and thiol-linked redox reactions in germination. Pakistan J Biol Sci., 13: 877 - 883.
    • (2010) Pakistan J Biol Sci. , vol.13 , pp. 877-883
    • Smiri, M.1    Chaoui, A.2    El Ferjani, E.3
  • 43
    • 77956721382 scopus 로고    scopus 로고
    • Redox regulation of the glutathione reductase/iso-glutaredoxin system in germinating pea seed exposed to cadmium
    • Smiri, M, Chaoui, A, Rouhier, N, Gelhaye, E, Jacquot, JP and El Ferjani, E. 2010e. Redox regulation of the glutathione reductase/iso-glutaredoxin system in germinating pea seed exposed to cadmium. Plant Sci., 179: 423 - 436.
    • (2010) Plant Sci. , vol.179 , pp. 423-436
    • Smiri, M.1    Chaoui, A.2    Rouhier, N.3    Gelhaye, E.4    Jacquot, J.P.5    El Ferjani, E.6
  • 44
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin, H, Staehelin, T and Gordon, J. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA., 76: 4350 - 4354.
    • (1979) Proc Natl Acad Sci USA. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 47
    • 0015462313 scopus 로고
    • Biochemical effects of mercury, cadmium, and lead
    • Vallee, BL and Ulmer, DD. 1972. Biochemical effects of mercury, cadmium, and lead. Annu Rev Biochem., 41: 91 - 128.
    • (1972) Annu Rev Biochem. , vol.41 , pp. 91-128
    • Vallee, B.L.1    Ulmer, D.D.2
  • 48
    • 85032069192 scopus 로고
    • Effects of metals on enzyme activity in plants
    • Van Assche, F and Clijsters, H. 1990. Effects of metals on enzyme activity in plants. Plant Cell Environ., 13: 195 - 206.
    • (1990) Plant Cell Environ. , vol.13 , pp. 195-206
    • Van Assche, F.1    Clijsters, H.2
  • 49
    • 0035896609 scopus 로고    scopus 로고
    • A proteome analysis of the cadmium response in Saccharomyces cerevisiae
    • Vido, K, Spector, D, Lagniel, G, Lopez, S, Toledano, MB and Labarre, J. 2001. A proteome analysis of the cadmium response in Saccharomyces cerevisiae. J Biol Chem., 276: 8469 - 8474.
    • (2001) J Biol Chem. , vol.276 , pp. 8469-8474
    • Vido, K.1    Spector, D.2    Lagniel, G.3    Lopez, S.4    Toledano, M.B.5    Labarre, J.6
  • 50
    • 0031841449 scopus 로고    scopus 로고
    • Biophysical, physiological and biochemical processes regulating seed germination
    • Welbaum, GE, Bradford, KJ, Kyu-Ock, Y and Oluoch, MO. 1998. Biophysical, physiological and biochemical processes regulating seed germination. Seed Sci Res., 8: 161 - 172.
    • (1998) Seed Sci Res. , vol.8 , pp. 161-172
    • Welbaum, G.E.1    Bradford, K.J.2    Kyu-Ock, Y.3    Oluoch, M.O.4
  • 51
    • 0000283759 scopus 로고
    • Comparison of tissue preparation methods for assay of nicotinamide coenzymes
    • Zhao, Z, Hu, X and Ross, CW. 1987. Comparison of tissue preparation methods for assay of nicotinamide coenzymes. Plant Physiol., 84: 987 - 988.
    • (1987) Plant Physiol. , vol.84 , pp. 987-988
    • Zhao, Z.1    Hu, X.2    Ross, C.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.