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Volumn 52, Issue 1, 2009, Pages 84-90

Protein degradation and peptidase activity during petal senescence in Dendrobium cv. Khao Sanan

Author keywords

Column; Cysteine peptidase; Flower senescence; Orchid; Peptidase activity; Petal; Protein degradation

Indexed keywords

DENDROBIUM; ORCHIDACEAE;

EID: 58949102051     PISSN: 09255214     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.postharvbio.2008.09.009     Document Type: Article
Times cited : (33)

References (38)
  • 1
    • 34247606060 scopus 로고    scopus 로고
    • Enhanced expression of serine proteases during floral senescence in Gladiolus
    • Azeez A., Sane A.P., Bhatnagar D., and Nath P. Enhanced expression of serine proteases during floral senescence in Gladiolus. Phytochemistry 68 (2007) 1352-1357
    • (2007) Phytochemistry , vol.68 , pp. 1352-1357
    • Azeez, A.1    Sane, A.P.2    Bhatnagar, D.3    Nath, P.4
  • 2
    • 51249169259 scopus 로고
    • A simple and efficient method for isolating RNA from pine trees
    • Chang S., Puryear J., and Cairney J. A simple and efficient method for isolating RNA from pine trees. Plant Mol. Biol. Rep. 11 (1993) 113-116
    • (1993) Plant Mol. Biol. Rep. , vol.11 , pp. 113-116
    • Chang, S.1    Puryear, J.2    Cairney, J.3
  • 3
    • 1842712632 scopus 로고    scopus 로고
    • Purification and characterization of serine proteases that exhibit caspase-like activity and are associated with programmed cell death in Avena sativa
    • Coffeen W.C., and Wolpert T.J. Purification and characterization of serine proteases that exhibit caspase-like activity and are associated with programmed cell death in Avena sativa. Plant Cell 16 (2004) 856-873
    • (2004) Plant Cell , vol.16 , pp. 856-873
    • Coffeen, W.C.1    Wolpert, T.J.2
  • 4
    • 10044231587 scopus 로고    scopus 로고
    • Cytoprotective efficacy and mechanisms of the liposoluble iron chelator 2,2′-dipyridyl in the rat photothrombotic ischemic stroke model
    • Demougeot C., Van Hoecke M., Bertrand N., Prigent-Tessier A., Mossiat C., Beley A., and Marie C. Cytoprotective efficacy and mechanisms of the liposoluble iron chelator 2,2′-dipyridyl in the rat photothrombotic ischemic stroke model. J. Pharmacol. Exp. Therap. 311 (2004) 1080-1087
    • (2004) J. Pharmacol. Exp. Therap. , vol.311 , pp. 1080-1087
    • Demougeot, C.1    Van Hoecke, M.2    Bertrand, N.3    Prigent-Tessier, A.4    Mossiat, C.5    Beley, A.6    Marie, C.7
  • 5
    • 0036367452 scopus 로고    scopus 로고
    • Programmed cell death during flower senescence: isolation and characterization of cysteine proteinases from Sandersonia aurantiaca
    • Eason J.R., Ryan D.J., Pinckney T.T., and O'Donoghue E.M. Programmed cell death during flower senescence: isolation and characterization of cysteine proteinases from Sandersonia aurantiaca. Funct. Plant Biol. 29 (2002) 1055-1064
    • (2002) Funct. Plant Biol. , vol.29 , pp. 1055-1064
    • Eason, J.R.1    Ryan, D.J.2    Pinckney, T.T.3    O'Donoghue, E.M.4
  • 7
    • 4644253630 scopus 로고    scopus 로고
    • Multifunctional role of plant cysteine proteinases
    • Grudkowska M., and Zagdańska B. Multifunctional role of plant cysteine proteinases. Acta Biochim. Pol. 51 (2004) 609-624
    • (2004) Acta Biochim. Pol. , vol.51 , pp. 609-624
    • Grudkowska, M.1    Zagdańska, B.2
  • 8
    • 2642666491 scopus 로고    scopus 로고
    • Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH)
    • Herman C., Thévenet D., Bouloc P., Walker G.C., and D'Ari R. Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH). Genes Dev. 12 (1998) 1348-1355
    • (1998) Genes Dev. , vol.12 , pp. 1348-1355
    • Herman, C.1    Thévenet, D.2    Bouloc, P.3    Walker, G.C.4    D'Ari, R.5
  • 10
    • 0031882508 scopus 로고    scopus 로고
    • Role of ferrous iron chelator 2,2′-dipyridyl in preventing delayed vasospasm in a primate model of subarachnoid hemorrhage
    • Horky L.L., Pluta R.M., Boock R.J., and Oldfield E.H. Role of ferrous iron chelator 2,2′-dipyridyl in preventing delayed vasospasm in a primate model of subarachnoid hemorrhage. J. Neurosurg. 88 (1998) 298-303
    • (1998) J. Neurosurg. , vol.88 , pp. 298-303
    • Horky, L.L.1    Pluta, R.M.2    Boock, R.J.3    Oldfield, E.H.4
  • 11
    • 33845693003 scopus 로고    scopus 로고
    • AtATG genes, homologs of yeast autophagy genes, are involved in constitutive autophagy in Arabidopsis root tip cells
    • Inoue Y., Suzuki T., Hattori M., Yoshimoto K., Ohsumi Y., and Moriyasu Y. AtATG genes, homologs of yeast autophagy genes, are involved in constitutive autophagy in Arabidopsis root tip cells. Plant Cell Physiol. 47 (2006) 1641-1652
    • (2006) Plant Cell Physiol. , vol.47 , pp. 1641-1652
    • Inoue, Y.1    Suzuki, T.2    Hattori, M.3    Yoshimoto, K.4    Ohsumi, Y.5    Moriyasu, Y.6
  • 12
    • 24944590697 scopus 로고    scopus 로고
    • Ethylene-sensitivity regulates proteolytic activity and cysteine protease gene expression in petunia corollas
    • Jones M.L., Chaffin G.S., Eason J.R., and Clark D.G. Ethylene-sensitivity regulates proteolytic activity and cysteine protease gene expression in petunia corollas. J. Exp. Bot. 56 (2005) 2733-2744
    • (2005) J. Exp. Bot. , vol.56 , pp. 2733-2744
    • Jones, M.L.1    Chaffin, G.S.2    Eason, J.R.3    Clark, D.G.4
  • 13
    • 0034966638 scopus 로고    scopus 로고
    • Ethylene production and post-pollination development in Dendrobium flowers treated with foreign pollen
    • Ketsa S., Bunya-atichart K., and van Doorn W.G. Ethylene production and post-pollination development in Dendrobium flowers treated with foreign pollen. Aust. J. Plant Physiol. 28 (2001) 409-415
    • (2001) Aust. J. Plant Physiol. , vol.28 , pp. 409-415
    • Ketsa, S.1    Bunya-atichart, K.2    van Doorn, W.G.3
  • 14
    • 0030454532 scopus 로고    scopus 로고
    • Inhibition of petunia flower senescence by 2,2′-dipyridyl
    • Knee M. Inhibition of petunia flower senescence by 2,2′-dipyridyl. Postharvest Biol. Technol. 9 (1996) 351-360
    • (1996) Postharvest Biol. Technol. , vol.9 , pp. 351-360
    • Knee, M.1
  • 17
    • 0000624192 scopus 로고
    • Function of lysosomes and lysosomal enzymes in the senescing corolla of morning glory (Ipomoea purpurea)
    • Matile P., and Winkenbach F. Function of lysosomes and lysosomal enzymes in the senescing corolla of morning glory (Ipomoea purpurea). J. Exp. Bot. 22 (1971) 759-771
    • (1971) J. Exp. Bot. , vol.22 , pp. 759-771
    • Matile, P.1    Winkenbach, F.2
  • 19
    • 0032189170 scopus 로고    scopus 로고
    • Purification and characterization of an endoprotease from alfalfa senescent leaves
    • Nieri B., Canino S., Versace R., and Alpi A. Purification and characterization of an endoprotease from alfalfa senescent leaves. Phytochemistry 49 (1998) 643-649
    • (1998) Phytochemistry , vol.49 , pp. 643-649
    • Nieri, B.1    Canino, S.2    Versace, R.3    Alpi, A.4
  • 20
    • 0029903809 scopus 로고    scopus 로고
    • Changes in sugar, protein, respiration, and ethylene in developing and harvested Geraldton waxflower (Chamelaucium uncinatum) flowers. New Zeal
    • Olley C.M., Joyce D.C., and Irving D.E. Changes in sugar, protein, respiration, and ethylene in developing and harvested Geraldton waxflower (Chamelaucium uncinatum) flowers. New Zeal. J. Crop Hort. Sci. 24 (1996) 143-150
    • (1996) J. Crop Hort. Sci. , vol.24 , pp. 143-150
    • Olley, C.M.1    Joyce, D.C.2    Irving, D.E.3
  • 21
    • 0343433408 scopus 로고    scopus 로고
    • Cysteine proteases and their inhibitors
    • Otto H.H., and Schirmeister T. Cysteine proteases and their inhibitors. Chem. Rev. 97 (1997) 133-171
    • (1997) Chem. Rev. , vol.97 , pp. 133-171
    • Otto, H.H.1    Schirmeister, T.2
  • 22
    • 13144275310 scopus 로고    scopus 로고
    • Delay of Iris flower senescence by protease inhibitors
    • Pak C., and van Doorn W.G. Delay of Iris flower senescence by protease inhibitors. New Phytol. 165 (2005) 473-480
    • (2005) New Phytol. , vol.165 , pp. 473-480
    • Pak, C.1    van Doorn, W.G.2
  • 24
    • 0030773692 scopus 로고    scopus 로고
    • Secretion of an aminopeptidase during transition of third-to fourth-stage larvae of Ascaris suum
    • Rhoads M.L., Fetterer R.H., and Urban J.F. Secretion of an aminopeptidase during transition of third-to fourth-stage larvae of Ascaris suum. J. Parasitol. 83 (1997) 780-784
    • (1997) J. Parasitol. , vol.83 , pp. 780-784
    • Rhoads, M.L.1    Fetterer, R.H.2    Urban, J.F.3
  • 25
    • 0032189507 scopus 로고    scopus 로고
    • A cysteine endopeptidase with a C-terminal KDEL motif isolated from castor bean endosperm is a marker enzyme for the ricinosome, a putative lytic compartment
    • Schmid M., Simpson D., Kalousek F., and Gietl C. A cysteine endopeptidase with a C-terminal KDEL motif isolated from castor bean endosperm is a marker enzyme for the ricinosome, a putative lytic compartment. Planta 206 (1998) 466-475
    • (1998) Planta , vol.206 , pp. 466-475
    • Schmid, M.1    Simpson, D.2    Kalousek, F.3    Gietl, C.4
  • 26
    • 0037473751 scopus 로고    scopus 로고
    • βB2-crystallin undergoes extensive truncation during aging in human lenses
    • Srivastava O.P., and Srivastava K. βB2-crystallin undergoes extensive truncation during aging in human lenses. Biochem. Biophys. Res. Commun. 301 (2003) 44-49
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 44-49
    • Srivastava, O.P.1    Srivastava, K.2
  • 27
    • 0032422199 scopus 로고    scopus 로고
    • Characterization of proteolytic activity during senescence in daylilies
    • Stephenson P., and Rubinstein B. Characterization of proteolytic activity during senescence in daylilies. Physiol. Plant. 104 (1998) 463-473
    • (1998) Physiol. Plant. , vol.104 , pp. 463-473
    • Stephenson, P.1    Rubinstein, B.2
  • 28
    • 0036008857 scopus 로고    scopus 로고
    • Is a cysteine proteinase inhibitor involved in the regulation of petal wilting in senescing carnation (Dianthus caryophyllus L.) flowers?
    • Sugawara H., Shibuya K., Yoshioka T., Hashiba T., and Satoh S. Is a cysteine proteinase inhibitor involved in the regulation of petal wilting in senescing carnation (Dianthus caryophyllus L.) flowers?. J. Exp. Bot. 53 (2002) 407-413
    • (2002) J. Exp. Bot. , vol.53 , pp. 407-413
    • Sugawara, H.1    Shibuya, K.2    Yoshioka, T.3    Hashiba, T.4    Satoh, S.5
  • 29
    • 33847101743 scopus 로고    scopus 로고
    • 1-MCP pretreatment prevents bud and flower abscission in Dendrobium orchids
    • Uthaichay N., Ketsa S., and van Doorn W.G. 1-MCP pretreatment prevents bud and flower abscission in Dendrobium orchids. Postharvest Biol. Technol. 43 (2007) 374-380
    • (2007) Postharvest Biol. Technol. , vol.43 , pp. 374-380
    • Uthaichay, N.1    Ketsa, S.2    van Doorn, W.G.3
  • 31
    • 43149114674 scopus 로고    scopus 로고
    • Physiology and molecular biology of petal senescence
    • van Doorn W.G., and Woltering E.J. Physiology and molecular biology of petal senescence. J. Exp. Bot. 59 (2008) 453-480
    • (2008) J. Exp. Bot. , vol.59 , pp. 453-480
    • van Doorn, W.G.1    Woltering, E.J.2
  • 34
    • 0021764208 scopus 로고
    • Natural structural variation in enzymes as a tool in the study of mechanism exemplified by a comparison of the catalytic-site structure and characteristics of cathepsin B and papain.
    • Willenbrock F., and Brocklehurst K. Natural structural variation in enzymes as a tool in the study of mechanism exemplified by a comparison of the catalytic-site structure and characteristics of cathepsin B and papain. pH-dependent kinetics of the reactions of cathepsin B from bovine spleen and from rat liver with a thiol-specific two-protonic-state probe (2,2′-dipyridyl disulphide) and with a specific synthetic substrate (N-α-benzyloxycarbonyl-l-arginyl-l-arginine 2-naphthylamide). Biochem. J. 222 (1984) 805-814
    • (1984) Biochem. J. , vol.222 , pp. 805-814
    • Willenbrock, F.1    Brocklehurst, K.2
  • 35
    • 0042961259 scopus 로고
    • Zum Stoffwechsel der aufblühenden und welkenden Korolle der Prunkwinde Ipomoea purpurea. I. Beziehungen zwischen Gestaltwandel, Stofftransport, Atmung und Invertaseaktivität
    • Winkenbach F. Zum Stoffwechsel der aufblühenden und welkenden Korolle der Prunkwinde Ipomoea purpurea. I. Beziehungen zwischen Gestaltwandel, Stofftransport, Atmung und Invertaseaktivität. Ber. Schweizer. Bot. Gesellschaft 80 (1970) 374-390
    • (1970) Ber. Schweizer. Bot. Gesellschaft , vol.80 , pp. 374-390
    • Winkenbach, F.1
  • 36
    • 0842341464 scopus 로고
    • Zum Stoffwechsel der aufblühenden und welkenden Korolle der Prunkwinde Ipomoea purpurea. II. Funktion und de novo Synthese lysosomaler Enzyme beim Welken
    • Winkenbach F. Zum Stoffwechsel der aufblühenden und welkenden Korolle der Prunkwinde Ipomoea purpurea. II. Funktion und de novo Synthese lysosomaler Enzyme beim Welken. Ber. Schweizer. Bot. Gesellschaft 80 (1970) 391-406
    • (1970) Ber. Schweizer. Bot. Gesellschaft , vol.80 , pp. 391-406
    • Winkenbach, F.1
  • 37
    • 0034483033 scopus 로고    scopus 로고
    • Programmed cell death in plant reproduction
    • Wu H., and Cheung A.Y. Programmed cell death in plant reproduction. Plant Mol. Biol. 44 (2000) 267-281
    • (2000) Plant Mol. Biol. , vol.44 , pp. 267-281
    • Wu, H.1    Cheung, A.Y.2
  • 38
    • 4344670363 scopus 로고    scopus 로고
    • Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages
    • Yasuda Y., Li Z., Greenbaum D., Bogyo M., Weber E., and Brömme D. Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages. J. Biol. Chem. 279 (2004) 36761-36770
    • (2004) J. Biol. Chem. , vol.279 , pp. 36761-36770
    • Yasuda, Y.1    Li, Z.2    Greenbaum, D.3    Bogyo, M.4    Weber, E.5    Brömme, D.6


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