메뉴 건너뛰기




Volumn 1794, Issue 3, 2009, Pages 459-467

Differential proteomic analysis of soluble extracellular proteins reveals the cysteine protease and cystatin involved in suspension-cultured cell proliferation in rice

Author keywords

Cell proliferation; Cystatin; Cysteine protease; Soluble extracellular protein; Suspension cultured rice cell

Indexed keywords

CYSTATIN; CYSTEINE PROTEINASE; PROTEIN;

EID: 59349098502     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.11.023     Document Type: Article
Times cited : (26)

References (45)
  • 1
    • 0027356728 scopus 로고
    • Structure and function of plant cell wall proteins
    • Showalter A.M. Structure and function of plant cell wall proteins. Plant Cell 5 (1993) 9-23
    • (1993) Plant Cell , vol.5 , pp. 9-23
    • Showalter, A.M.1
  • 4
    • 0036779358 scopus 로고    scopus 로고
    • Role of the extracellular matrix in cell-cell signalling: paracrine paradigms
    • Brownlee C. Role of the extracellular matrix in cell-cell signalling: paracrine paradigms. Curr. Opin. Plant Biol. 5 (2002) 396-401
    • (2002) Curr. Opin. Plant Biol. , vol.5 , pp. 396-401
    • Brownlee, C.1
  • 7
    • 0038047058 scopus 로고    scopus 로고
    • Proteomic analysis of changes in the extracellular matrix of Arabidopsis cell suspension cultures induced by fungal elicitors
    • Ndimba B.K., Chivasa S., Hamilton J.M., Simon W.J., and Slabas A.R. Proteomic analysis of changes in the extracellular matrix of Arabidopsis cell suspension cultures induced by fungal elicitors. Proteomics 3 (2003) 1047-1059
    • (2003) Proteomics , vol.3 , pp. 1047-1059
    • Ndimba, B.K.1    Chivasa, S.2    Hamilton, J.M.3    Simon, W.J.4    Slabas, A.R.5
  • 9
    • 24644494802 scopus 로고    scopus 로고
    • A proteomic approach to apoplastic proteins involved in cell wall regeneration in protoplasts of Arabidopsis suspension-cultured cells
    • Kwon H.K., Yokoyama R., and Nishitani K. A proteomic approach to apoplastic proteins involved in cell wall regeneration in protoplasts of Arabidopsis suspension-cultured cells. Plant Cell Physiol. 46 (2005) 843-857
    • (2005) Plant Cell Physiol. , vol.46 , pp. 843-857
    • Kwon, H.K.1    Yokoyama, R.2    Nishitani, K.3
  • 10
    • 29544449701 scopus 로고    scopus 로고
    • Pathogen elicitor-induced changes in the maize extracellular matrix proteome
    • Chivasa S., Simon W.J., Yu X.L., Yalpani N., and Slabas A.R. Pathogen elicitor-induced changes in the maize extracellular matrix proteome. Proteomics 5 (2005) 4894-4904
    • (2005) Proteomics , vol.5 , pp. 4894-4904
    • Chivasa, S.1    Simon, W.J.2    Yu, X.L.3    Yalpani, N.4    Slabas, A.R.5
  • 11
    • 33645799967 scopus 로고    scopus 로고
    • Cell wall proteome in the maize primary root elongation zone. I. Extraction and identification of water-soluble and lightly ionically bound proteins
    • Zhu J., Chen S., Alvarez S., Asirvatham V.S., Schachtman D.P., Wu Y., and Sharp R.E. Cell wall proteome in the maize primary root elongation zone. I. Extraction and identification of water-soluble and lightly ionically bound proteins. Plant Physiol. 140 (2006) 311-325
    • (2006) Plant Physiol. , vol.140 , pp. 311-325
    • Zhu, J.1    Chen, S.2    Alvarez, S.3    Asirvatham, V.S.4    Schachtman, D.P.5    Wu, Y.6    Sharp, R.E.7
  • 13
    • 0034051713 scopus 로고    scopus 로고
    • Secreted proteins of tobacco cultured BY2 cells: identification of a new member of pathogenesis-related proteins
    • Okushima Y., Koizumi N., Kusano T., and Sano H. Secreted proteins of tobacco cultured BY2 cells: identification of a new member of pathogenesis-related proteins. Plant Mol. Bio. 42 (2000) 479-488
    • (2000) Plant Mol. Bio. , vol.42 , pp. 479-488
    • Okushima, Y.1    Koizumi, N.2    Kusano, T.3    Sano, H.4
  • 14
    • 14644433039 scopus 로고    scopus 로고
    • Changes in the tobacco leaf apoplast proteome in response to salt stress
    • Dani V., Simon W.J., Duranti M., and Croy R.R.D. Changes in the tobacco leaf apoplast proteome in response to salt stress. Proteomics 5 (2005) 737-745
    • (2005) Proteomics , vol.5 , pp. 737-745
    • Dani, V.1    Simon, W.J.2    Duranti, M.3    Croy, R.R.D.4
  • 16
    • 7944228440 scopus 로고    scopus 로고
    • Genomic basis for cell-wall diversity in plants. A comparative approach to gene families in rice and Arabidopsis
    • Yokoyama R., and Nishitani K. Genomic basis for cell-wall diversity in plants. A comparative approach to gene families in rice and Arabidopsis. Plant Cell Physiol. 45 (2004) 1111-1121
    • (2004) Plant Cell Physiol. , vol.45 , pp. 1111-1121
    • Yokoyama, R.1    Nishitani, K.2
  • 17
    • 16344375435 scopus 로고    scopus 로고
    • Rice proteome analysis: a step toward functional analysis of the rice genome
    • Komatsu S., and Tanaka N. Rice proteome analysis: a step toward functional analysis of the rice genome. Proteomics 5 (2005) 938-949
    • (2005) Proteomics , vol.5 , pp. 938-949
    • Komatsu, S.1    Tanaka, N.2
  • 20
    • 0029821720 scopus 로고    scopus 로고
    • Phytosulfokine, sulfated peptides that induce the proliferation of single mesophyll cells of Asparagus officinalis L
    • Matsubayashi Y., and Sakagami Y. Phytosulfokine, sulfated peptides that induce the proliferation of single mesophyll cells of Asparagus officinalis L. Proc. Natl Acad. Sci. USA 93 (1996) 7623-7627
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 7623-7627
    • Matsubayashi, Y.1    Sakagami, Y.2
  • 21
    • 0037394093 scopus 로고    scopus 로고
    • Expression and function of cell wall-bound cationic peroxidase in asparagus somatic embryogenesis
    • Takeda H., Kotake T., Nakagawa N., Sakurai N., and Nevins D.J. Expression and function of cell wall-bound cationic peroxidase in asparagus somatic embryogenesis. Plant Physiol. 131 (2003) 1765-1774
    • (2003) Plant Physiol. , vol.131 , pp. 1765-1774
    • Takeda, H.1    Kotake, T.2    Nakagawa, N.3    Sakurai, N.4    Nevins, D.J.5
  • 22
    • 0030660281 scopus 로고    scopus 로고
    • Phytosulfokine-α, a sulfated pentapeptide, stimulates the proliferation of rice cells by means of specific high- and low-affinity binding sites
    • Matsubayashi Y., Takagi L., and Sakagami Y. Phytosulfokine-α, a sulfated pentapeptide, stimulates the proliferation of rice cells by means of specific high- and low-affinity binding sites. Proc. Natl Acad. Sci. USA 94 (1997) 13357-13362
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 13357-13362
    • Matsubayashi, Y.1    Takagi, L.2    Sakagami, Y.3
  • 23
    • 0035940404 scopus 로고    scopus 로고
    • RALF, a 5-kDa ubiquitous polypeptide in plants, arrests root growth and development
    • Pearce G., Moura D.S., Stratmann J., and Ryan C.A. RALF, a 5-kDa ubiquitous polypeptide in plants, arrests root growth and development. Proc. Natl Acad. Sci. USA 98 (2001) 12843-12847
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 12843-12847
    • Pearce, G.1    Moura, D.S.2    Stratmann, J.3    Ryan, C.A.4
  • 24
    • 0034685783 scopus 로고    scopus 로고
    • 120- and 160-kDa receptors for endogenous mitogenic peptide, phytosulfokine-a, in rice plasma membranes
    • Matsubayashi Y., and Sakagami Y. 120- and 160-kDa receptors for endogenous mitogenic peptide, phytosulfokine-a, in rice plasma membranes. J. Biol. Chem. 275 (2000) 15520-15525
    • (2000) J. Biol. Chem. , vol.275 , pp. 15520-15525
    • Matsubayashi, Y.1    Sakagami, Y.2
  • 25
    • 0029202021 scopus 로고
    • Apoplastic pH and ammonium concentration in leaves of Brassica napus
    • Husted S., and Schjoerring J.K. Apoplastic pH and ammonium concentration in leaves of Brassica napus. Plant Physiol. 109 (1995) 1453-1460
    • (1995) Plant Physiol. , vol.109 , pp. 1453-1460
    • Husted, S.1    Schjoerring, J.K.2
  • 26
    • 0042831314 scopus 로고    scopus 로고
    • Oryzacystatin I expressed in transgenic potato induces digestive compensation in an insect natural predator via its herbivorous prey feeding on the plant
    • Bouchard É., Cloutier C., and Michaud D. Oryzacystatin I expressed in transgenic potato induces digestive compensation in an insect natural predator via its herbivorous prey feeding on the plant. Molecular Ecology 12 (2003) 2439-2446
    • (2003) Molecular Ecology , vol.12 , pp. 2439-2446
    • Bouchard, É.1    Cloutier, C.2    Michaud, D.3
  • 27
    • 18944390005 scopus 로고    scopus 로고
    • A practical vector for efficient knockdown of gene expression in rice (Oryza sativa L.)
    • Wang Z., Chen C., Xu Y., Jiang R., Han Y., Xu Z., and Chong K. A practical vector for efficient knockdown of gene expression in rice (Oryza sativa L.). Plant Mol. Biol. Rep. 22 (2004) 409-417
    • (2004) Plant Mol. Biol. Rep. , vol.22 , pp. 409-417
    • Wang, Z.1    Chen, C.2    Xu, Y.3    Jiang, R.4    Han, Y.5    Xu, Z.6    Chong, K.7
  • 28
    • 2642563793 scopus 로고    scopus 로고
    • Large-scale production of enhancer trapping lines for rice functional genomics
    • Yang Y., Peng H., Huang H., Wu J., Jia S., Huang D., and Lu T. Large-scale production of enhancer trapping lines for rice functional genomics. Plant Science 167 (2004) 281-288
    • (2004) Plant Science , vol.167 , pp. 281-288
    • Yang, Y.1    Peng, H.2    Huang, H.3    Wu, J.4    Jia, S.5    Huang, D.6    Lu, T.7
  • 29
    • 0033757969 scopus 로고    scopus 로고
    • Multiple mode regulation of a cysteine proteinase gene expression in rice
    • Ho S.L., Tong W.F., and Yu S.M. Multiple mode regulation of a cysteine proteinase gene expression in rice. Plant Physiol. 122 (2000) 57-66
    • (2000) Plant Physiol. , vol.122 , pp. 57-66
    • Ho, S.L.1    Tong, W.F.2    Yu, S.M.3
  • 30
    • 50249165829 scopus 로고    scopus 로고
    • Improvement of recombinant hGM-CSF production by suppression of cysteine proteinase gene expression using RNA interference in a transgenic rice culture
    • Kim N., Kim T., Kim O., Ko E., Jang Y., Jung E., Kwon T., and Yang M. Improvement of recombinant hGM-CSF production by suppression of cysteine proteinase gene expression using RNA interference in a transgenic rice culture. Plant Mol Biol. 68 (2008) 263-275
    • (2008) Plant Mol Biol. , vol.68 , pp. 263-275
    • Kim, N.1    Kim, T.2    Kim, O.3    Ko, E.4    Jang, Y.5    Jung, E.6    Kwon, T.7    Yang, M.8
  • 31
    • 0001312872 scopus 로고
    • An examination of centrifugation as a method of extracting an extracellular solution from peas, and its use for the study of indoleacetic acid-induced growth
    • Terry M., and Bonner B.A. An examination of centrifugation as a method of extracting an extracellular solution from peas, and its use for the study of indoleacetic acid-induced growth. Plant Physiol. 66 (1980) 321-325
    • (1980) Plant Physiol. , vol.66 , pp. 321-325
    • Terry, M.1    Bonner, B.A.2
  • 32
    • 0001024577 scopus 로고
    • Studies on the growth in culture of plant cells. The initiation of division in suspensions of stationary phase cells of Acer pseudoplatanus
    • Stuart R., and Street H.E. Studies on the growth in culture of plant cells. The initiation of division in suspensions of stationary phase cells of Acer pseudoplatanus. J. Exp. Bot. 20 (1969) 556-571
    • (1969) J. Exp. Bot. , vol.20 , pp. 556-571
    • Stuart, R.1    Street, H.E.2
  • 33
    • 0032853146 scopus 로고    scopus 로고
    • The endogenous sulfated pentapeptide phytosulfokine-alpha stimulates tracheary element differentiation of isolated mesophyll cells of zinnia
    • Matsubayashi Y., Takagi L., Omura N., Morita A., and Sakagami Y. The endogenous sulfated pentapeptide phytosulfokine-alpha stimulates tracheary element differentiation of isolated mesophyll cells of zinnia. Plant Physiol. 120 (1999) 1043-1048
    • (1999) Plant Physiol. , vol.120 , pp. 1043-1048
    • Matsubayashi, Y.1    Takagi, L.2    Omura, N.3    Morita, A.4    Sakagami, Y.5
  • 34
    • 0033955472 scopus 로고    scopus 로고
    • A secreted peptide growth factor, phytosulfokine, acting as a stimulatory factor of carrot somatic embryo formation
    • Hanai H., Matsuno T., Yamamoto M., Matsubayashi Y., Kobayashi T., Kamada H., and Sakagami Y. A secreted peptide growth factor, phytosulfokine, acting as a stimulatory factor of carrot somatic embryo formation. Plant Cell Physiol. 41 (2000) 27-32
    • (2000) Plant Cell Physiol. , vol.41 , pp. 27-32
    • Hanai, H.1    Matsuno, T.2    Yamamoto, M.3    Matsubayashi, Y.4    Kobayashi, T.5    Kamada, H.6    Sakagami, Y.7
  • 36
    • 4644253630 scopus 로고    scopus 로고
    • Multifunctional role of plant cysteine proteinases
    • Grudkowska M., and Zagdańska B. Multifunctional role of plant cysteine proteinases. Acta. Biochimica. Polonica. 51 (2004) 609-624
    • (2004) Acta. Biochimica. Polonica. , vol.51 , pp. 609-624
    • Grudkowska, M.1    Zagdańska, B.2
  • 37
    • 0030039128 scopus 로고    scopus 로고
    • Identification and characterization of a rice cysteine endopeptidase that digests glutelin
    • Kato H., and Mtnamikawa T. Identification and characterization of a rice cysteine endopeptidase that digests glutelin. Eur. J. Biochern. 23 (1996) 310-316
    • (1996) Eur. J. Biochern. , vol.23 , pp. 310-316
    • Kato, H.1    Mtnamikawa, T.2
  • 38
    • 0037164073 scopus 로고    scopus 로고
    • Plant seed cystatins and their target enzymes of endogenous and exogenous origin
    • Arai S., Matcumoto I., Emori Y., and Abe K. Plant seed cystatins and their target enzymes of endogenous and exogenous origin. J. Agric. Food. Chem. 50 (2002) 6612-6617
    • (2002) J. Agric. Food. Chem. , vol.50 , pp. 6612-6617
    • Arai, S.1    Matcumoto, I.2    Emori, Y.3    Abe, K.4
  • 39
    • 0032787406 scopus 로고    scopus 로고
    • The use of cysteine proteinase inhibitors to engineer resistance against potyviruses in transgenic tobacco plants
    • Gutierrez-Campos R., Torres-Acosta J.A., Saucedo-Arias L.J., and Gomez-Lim M.A. The use of cysteine proteinase inhibitors to engineer resistance against potyviruses in transgenic tobacco plants. Nature Biotechnology 17 (1999) 1223-1226
    • (1999) Nature Biotechnology , vol.17 , pp. 1223-1226
    • Gutierrez-Campos, R.1    Torres-Acosta, J.A.2    Saucedo-Arias, L.J.3    Gomez-Lim, M.A.4
  • 40
    • 0033101490 scopus 로고    scopus 로고
    • The involvement of cysteine proteases and protease inhibitor genes in programmed cell death in plants
    • Solomon M., Belenghi B., Delledonne M., and Levine A. The involvement of cysteine proteases and protease inhibitor genes in programmed cell death in plants. Plant Cell 11 (1999) 431-444
    • (1999) Plant Cell , vol.11 , pp. 431-444
    • Solomon, M.1    Belenghi, B.2    Delledonne, M.3    Levine, A.4
  • 42
    • 1542279127 scopus 로고    scopus 로고
    • Oryzacystatin I expression in transformed tobacco produces a conditional growth phenotype and enhances chilling tolerance
    • Vyver C.V.D., Schneidereit J., Driscoll S., Turner J., Kunert K., and Foyer C.H. Oryzacystatin I expression in transformed tobacco produces a conditional growth phenotype and enhances chilling tolerance. Plant Biotechnol. J. 1 (2003) 101-112
    • (2003) Plant Biotechnol. J. , vol.1 , pp. 101-112
    • Vyver, C.V.D.1    Schneidereit, J.2    Driscoll, S.3    Turner, J.4    Kunert, K.5    Foyer, C.H.6
  • 44
    • 0023657047 scopus 로고
    • Molecular cloning of a cysteine proteinase inhibitor of rice (Oryzacystatin). Homology with animal cystatins and transient expression in the ripening process of rice seeds
    • Abe K., Emori Y., Kondo H., Suzukis K., and Arai S. Molecular cloning of a cysteine proteinase inhibitor of rice (Oryzacystatin). Homology with animal cystatins and transient expression in the ripening process of rice seeds. J. Biol. Chem. 262 (1987) 16793-16797
    • (1987) J. Biol. Chem. , vol.262 , pp. 16793-16797
    • Abe, K.1    Emori, Y.2    Kondo, H.3    Suzukis, K.4    Arai, S.5
  • 45
    • 0034056453 scopus 로고    scopus 로고
    • Identification of a signal peptide for oryzacystatin-I
    • Womack J.S., Randall J., and Kemp J.D. Identification of a signal peptide for oryzacystatin-I. Planta 210 (2000) 844-847
    • (2000) Planta , vol.210 , pp. 844-847
    • Womack, J.S.1    Randall, J.2    Kemp, J.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.