메뉴 건너뛰기




Volumn 11, Issue , 2011, Pages

Antibody degradation in tobacco plants: A predominantly apoplastic process

Author keywords

[No Author keywords available]

Indexed keywords

EXTRACTION CONDITIONS; HUMAN IGG; LEAF EXTRACTS; NICOTIANA TABACUM; PROTEASE INHIBITOR; PROTEOLYTIC ACTIVITIES; PROTEOLYTIC DEGRADATION; PROTEOLYTIC FRAGMENTS; PULSE-CHASE ANALYSIS; RECOMBINANT PROTEIN; SUBCELLULAR COMPARTMENTS; TISSUE DISRUPTION; TOBACCO PLANTS; TRANSGENIC PLANT LINES; TRANSGENIC PLANTS;

EID: 84855165591     PISSN: None     EISSN: 14726750     Source Type: Journal    
DOI: 10.1186/1472-6750-11-128     Document Type: Article
Times cited : (44)

References (46)
  • 1
    • 0028031827 scopus 로고
    • Assembly of monoclonal antibodies with IgG1 and IgA heavy chain domains in transgenic tobacco plants
    • Ma JK, Lehner T, Stabila P, Fux CI, Hiatt A. Assembly of monoclonal antibodies with IgG1 and IgA heavy chain domains in transgenic tobacco plants. Eur J Immunol 1994, 24(1):131-138.
    • (1994) Eur J Immunol , vol.24 , Issue.1 , pp. 131-138
    • Ma, J.K.1    Lehner, T.2    Stabila, P.3    Fux, C.I.4    Hiatt, A.5
  • 2
    • 0035811160 scopus 로고    scopus 로고
    • Characterization of monoclonal antibody fragments produced by plant cells
    • Sharp JM, Doran PM. Characterization of monoclonal antibody fragments produced by plant cells. Biotechnol Bioeng 2001, 73(5):338-346.
    • (2001) Biotechnol Bioeng , vol.73 , Issue.5 , pp. 338-346
    • Sharp, J.M.1    Doran, P.M.2
  • 4
    • 0141451936 scopus 로고    scopus 로고
    • Expression of Sea Anemone Equistatin in Potato. Effects of Plant Proteases on Heterologous Protein Production
    • Outchkourov NS, Rogelj B, Strukelj B, Jongsma MA. Expression of Sea Anemone Equistatin in Potato. Effects of Plant Proteases on Heterologous Protein Production. Plant Physiol 2003, 133(1):379-390.
    • (2003) Plant Physiol , vol.133 , Issue.1 , pp. 379-390
    • Outchkourov, N.S.1    Rogelj, B.2    Strukelj, B.3    Jongsma, M.A.4
  • 8
    • 14744298421 scopus 로고    scopus 로고
    • Protein modifications in the plant secretory pathway: current status and practical implications in molecular pharming
    • Faye L, Boulaflous A, Benchabane M, Gomord V, Michaud D. Protein modifications in the plant secretory pathway: current status and practical implications in molecular pharming. Vaccine 2005, 23(15):1770-1778.
    • (2005) Vaccine , vol.23 , Issue.15 , pp. 1770-1778
    • Faye, L.1    Boulaflous, A.2    Benchabane, M.3    Gomord, V.4    Michaud, D.5
  • 9
    • 11844252119 scopus 로고    scopus 로고
    • A cut above the rest: the regulatory function of plant proteases
    • Schaller A. A cut above the rest: the regulatory function of plant proteases. Planta 2004, 220(2):183-197.
    • (2004) Planta , vol.220 , Issue.2 , pp. 183-197
    • Schaller, A.1
  • 10
    • 44949258132 scopus 로고    scopus 로고
    • Plant Proteases: From Phenotypes to Molecular Mechanisms
    • van der Hoorn RAL. Plant Proteases: From Phenotypes to Molecular Mechanisms. Annual Review of Plant Biology 2008, 59(1):191-223.
    • (2008) Annual Review of Plant Biology , vol.59 , Issue.1 , pp. 191-223
    • van der Hoorn, R.A.L.1
  • 11
    • 33645729021 scopus 로고    scopus 로고
    • Two new cysteine proteinases with specific expression patterns in mature and senescent tobacco (Nicotiana tabacum L.) leaves
    • Beyene G, Foyer CH, Kunert KJ. Two new cysteine proteinases with specific expression patterns in mature and senescent tobacco (Nicotiana tabacum L.) leaves. Journal of Experimental Botany 2006, 57(6):1431-1443.
    • (2006) Journal of Experimental Botany , vol.57 , Issue.6 , pp. 1431-1443
    • Beyene, G.1    Foyer, C.H.2    Kunert, K.J.3
  • 16
    • 58149385715 scopus 로고    scopus 로고
    • Targeting and post-translational processing of human alpha1-antichymotrypsin in BY-2 tobacco cultured cells
    • Benchabane M, Saint-Jore-Dupas C, Bardor M, Faye L, Michaud D, Gomord V. Targeting and post-translational processing of human alpha1-antichymotrypsin in BY-2 tobacco cultured cells. Plant Biotechnol J 2009, 7(2):146-160.
    • (2009) Plant Biotechnol J , vol.7 , Issue.2 , pp. 146-160
    • Benchabane, M.1    Saint-Jore-Dupas, C.2    Bardor, M.3    Faye, L.4    Michaud, D.5    Gomord, V.6
  • 17
    • 0032547704 scopus 로고    scopus 로고
    • Gel electrophoresis of proteolytic enzymes
    • Michaud D. Gel electrophoresis of proteolytic enzymes. Analytica Chimica Acta 1998, 372(1-2):173-185.
    • (1998) Analytica Chimica Acta , vol.372 , Issue.1-2 , pp. 173-185
    • Michaud, D.1
  • 18
    • 14744286603 scopus 로고    scopus 로고
    • Chloroplast-derived vaccine antigens and other therapeutic proteins
    • Daniell H, Chebolu S, Kumar S, Singleton M, Falconer R. Chloroplast-derived vaccine antigens and other therapeutic proteins. Vaccine 2005, 23(15):1779-1783.
    • (2005) Vaccine , vol.23 , Issue.15 , pp. 1779-1783
    • Daniell, H.1    Chebolu, S.2    Kumar, S.3    Singleton, M.4    Falconer, R.5
  • 19
    • 24144490427 scopus 로고    scopus 로고
    • Recombinant Pharmaceuticals from Plants: The Plant Endomembrane System as Bioreactor
    • Vitale A, Pedrazzini E. Recombinant Pharmaceuticals from Plants: The Plant Endomembrane System as Bioreactor. Molecular Interventions 2005, 5(4):216-225.
    • (2005) Molecular Interventions , vol.5 , Issue.4 , pp. 216-225
    • Vitale, A.1    Pedrazzini, E.2
  • 20
    • 2442625762 scopus 로고    scopus 로고
    • The plant vesicular transport engineering for production of useful recombinant proteins
    • Yoshida K, Matsui T, Shinmyo A. The plant vesicular transport engineering for production of useful recombinant proteins. Journal of Molecular Catalysis B: Enzymatic 2004, 28(4-6):167-171.
    • (2004) Journal of Molecular Catalysis B: Enzymatic , vol.28 , Issue.4-6 , pp. 167-171
    • Yoshida, K.1    Matsui, T.2    Shinmyo, A.3
  • 21
    • 1542351607 scopus 로고    scopus 로고
    • Targeting transgene expression in research, agricultural, and environmental applications: Promoters used in plant transformation
    • Potenza C, Aleman L, Sengupta-Gopalan C. Targeting transgene expression in research, agricultural, and environmental applications: Promoters used in plant transformation. In Vitro Cellular & Developmental Biology-Plant 2004, 40(1):1-22.
    • (2004) In Vitro Cellular & Developmental Biology-Plant , vol.40 , Issue.1 , pp. 1-22
    • Potenza, C.1    Aleman, L.2    Sengupta-Gopalan, C.3
  • 23
    • 33747144853 scopus 로고    scopus 로고
    • Cosecretion of Protease Inhibitor Stabilizes Antibodies Produced by Plant Roots
    • Komarnytsky S, Borisjuk N, Yakoby N, Garvey A, Raskin I. Cosecretion of Protease Inhibitor Stabilizes Antibodies Produced by Plant Roots. Plant Physiol 2006, 141(4):1185-1193.
    • (2006) Plant Physiol , vol.141 , Issue.4 , pp. 1185-1193
    • Komarnytsky, S.1    Borisjuk, N.2    Yakoby, N.3    Garvey, A.4    Raskin, I.5
  • 26
    • 18744402497 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation of ricin A chain has unique and plant-specific features
    • Di Cola A, Frigerio L, Lord JM, Roberts LM, Ceriotti A. Endoplasmic reticulum-associated degradation of ricin A chain has unique and plant-specific features. Plant Physiol 2005, 137(1):287-296.
    • (2005) Plant Physiol , vol.137 , Issue.1 , pp. 287-296
    • Di Cola, A.1    Frigerio, L.2    Lord, J.M.3    Roberts, L.M.4    Ceriotti, A.5
  • 27
    • 33744947552 scopus 로고    scopus 로고
    • Monoclonal antibody form and function: manufacturing the right antibodies for treating drug abuse
    • Peterson E, Owens SM, Henry RL. Monoclonal antibody form and function: manufacturing the right antibodies for treating drug abuse. AAPS J 2006, 8(2):E383-390.
    • (2006) AAPS J , vol.8 , Issue.2
    • Peterson, E.1    Owens, S.M.2    Henry, R.L.3
  • 28
    • 49349108593 scopus 로고    scopus 로고
    • Fluorescent protein fusions to a human immunodeficiency virus monoclonal antibody reveal its intracellular transport through the plant endomembrane system
    • Irons SL, Nuttall J, Floß DM, Frigerio L, Kotzer AM, Hawes C. Fluorescent protein fusions to a human immunodeficiency virus monoclonal antibody reveal its intracellular transport through the plant endomembrane system. Plant Biotechnology Journal 2008, 6(7):649-662.
    • (2008) Plant Biotechnology Journal , vol.6 , Issue.7 , pp. 649-662
    • Irons, S.L.1    Nuttall, J.2    Floß, D.M.3    Frigerio, L.4    Kotzer, A.M.5    Hawes, C.6
  • 29
    • 49349095531 scopus 로고    scopus 로고
    • Considerations for extraction of monoclonal antibodies targeted to different subcellular compartments in transgenic tobacco plants
    • Hassan S, Van Dolleweerd CJ, Ioakeimidis F, Keshavarz-Moore E, Ma JK-C. Considerations for extraction of monoclonal antibodies targeted to different subcellular compartments in transgenic tobacco plants. Plant Biotechnology Journal 2008, 6(7):733-748.
    • (2008) Plant Biotechnology Journal , vol.6 , Issue.7 , pp. 733-748
    • Hassan, S.1    Van Dolleweerd, C.J.2    Ioakeimidis, F.3    Keshavarz-Moore, E.4    Ma, J.K.-.C.5
  • 30
    • 32644461200 scopus 로고    scopus 로고
    • Loss of secreted antibody from transgenic plant tissue cultures due to surface adsorption
    • Doran PM. Loss of secreted antibody from transgenic plant tissue cultures due to surface adsorption. Journal of Biotechnology 2006, 122(1):39-54.
    • (2006) Journal of Biotechnology , vol.122 , Issue.1 , pp. 39-54
    • Doran, P.M.1
  • 31
    • 84873073357 scopus 로고    scopus 로고
    • Monoclonal Antibody Form and Function: Manufacturing the Right Antibodies for Treating Drug Abuse
    • Springer New York, Rapaka RS, Sadée W
    • Peterson E, Owens SM, Henry RL. Monoclonal Antibody Form and Function: Manufacturing the Right Antibodies for Treating Drug Abuse. Drug Addiction 2008, 87-100. Springer New York, Rapaka RS, Sadée W.
    • (2008) Drug Addiction , pp. 87-100
    • Peterson, E.1    Owens, S.M.2    Henry, R.L.3
  • 32
    • 0020541752 scopus 로고
    • Intracellular distribution and degradation of immunoglobulin G and immunoglobulin G fragments injected into HeLa cells
    • McGarry T, Hough R, Rogers S, Rechsteiner M. Intracellular distribution and degradation of immunoglobulin G and immunoglobulin G fragments injected into HeLa cells. The Journal of Cell Biology 1983, 96(2):338-346.
    • (1983) The Journal of Cell Biology , vol.96 , Issue.2 , pp. 338-346
    • McGarry, T.1    Hough, R.2    Rogers, S.3    Rechsteiner, M.4
  • 33
    • 0021042615 scopus 로고
    • On the fragmentation of monoclonal IgG1, IgG2a, and IgG2b from BALB/c mice
    • Parham P. On the fragmentation of monoclonal IgG1, IgG2a, and IgG2b from BALB/c mice. The Journal of Immunology 1983, 131(6):2895-2902.
    • (1983) The Journal of Immunology , vol.131 , Issue.6 , pp. 2895-2902
    • Parham, P.1
  • 34
    • 0029064183 scopus 로고
    • Evidence that the hinge region plays a role in maintaining serum levels of the murine IgG1 molecule
    • Kim J-K, Tsen M-F, Ghetie V, Sally Ward E. Evidence that the hinge region plays a role in maintaining serum levels of the murine IgG1 molecule. Molecular Immunology 1995, 32(7):467-475.
    • (1995) Molecular Immunology , vol.32 , Issue.7 , pp. 467-475
    • Kim, J.-.K.1    Tsen, M.-.F.2    Ghetie, V.3    Sally Ward, E.4
  • 35
    • 38549103628 scopus 로고    scopus 로고
    • Protein quality control in the early secretory pathway
    • Anelli T, Sitia R. Protein quality control in the early secretory pathway. EMBO J 2008, 27(2):315-327.
    • (2008) EMBO J , vol.27 , Issue.2 , pp. 315-327
    • Anelli, T.1    Sitia, R.2
  • 37
    • 33645737420 scopus 로고    scopus 로고
    • Golgi-Mediated Vacuolar Sorting of the Endoplasmic Reticulum Chaperone BiP May Play an Active Role in Quality Control within the Secretory Pathway
    • Pimpl P, Taylor JP, Snowden C, Hillmer S, Robinson DG, Denecke J. Golgi-Mediated Vacuolar Sorting of the Endoplasmic Reticulum Chaperone BiP May Play an Active Role in Quality Control within the Secretory Pathway. Plant Cell 2006, 18(1):198-211.
    • (2006) Plant Cell , vol.18 , Issue.1 , pp. 198-211
    • Pimpl, P.1    Taylor, J.P.2    Snowden, C.3    Hillmer, S.4    Robinson, D.G.5    Denecke, J.6
  • 38
    • 0037325964 scopus 로고    scopus 로고
    • Fusion with HDEL protects cell wall invertase from early degradation when N-glycosylation is inhibited
    • Pagny S, Denmat-Ouisse LA, Gomord V, Faye L. Fusion with HDEL protects cell wall invertase from early degradation when N-glycosylation is inhibited. Plant Cell Physiol 2003, 44(2):173-182.
    • (2003) Plant Cell Physiol , vol.44 , Issue.2 , pp. 173-182
    • Pagny, S.1    Denmat-Ouisse, L.A.2    Gomord, V.3    Faye, L.4
  • 39
    • 46849111804 scopus 로고    scopus 로고
    • The human immunodeficiency virus antigen Nef forms protein bodies in leaves of transgenic tobacco when fused to zeolin
    • de Virgilio M, De Marchis F, Bellucci M, Mainieri D, Rossi M, Benvenuto E, Arcioni S, Vitale A. The human immunodeficiency virus antigen Nef forms protein bodies in leaves of transgenic tobacco when fused to zeolin. J Exp Bot 2008, 59(10):2815-2829.
    • (2008) J Exp Bot , vol.59 , Issue.10 , pp. 2815-2829
    • de Virgilio, M.1    De Marchis, F.2    Bellucci, M.3    Mainieri, D.4    Rossi, M.5    Benvenuto, E.6    Arcioni, S.7    Vitale, A.8
  • 40
    • 0037971075 scopus 로고    scopus 로고
    • The C-terminal Extension of a Hybrid Immunoglobulin A/G Heavy Chain Is Responsible for Its Golgi-mediated Sorting to the Vacuole
    • Hadlington JL, Santoro A, Nuttall J, Denecke J, Ma JK-C, Vitale A, Frigerio L. The C-terminal Extension of a Hybrid Immunoglobulin A/G Heavy Chain Is Responsible for Its Golgi-mediated Sorting to the Vacuole. Mol Biol Cell 2003, 14(6):2592-2602.
    • (2003) Mol Biol Cell , vol.14 , Issue.6 , pp. 2592-2602
    • Hadlington, J.L.1    Santoro, A.2    Nuttall, J.3    Denecke, J.4    Ma, J.K.-.C.5    Vitale, A.6    Frigerio, L.7
  • 42
    • 34547876491 scopus 로고    scopus 로고
    • Expression of a Constitutively Activated Plasma Membrane H+-ATPase Alters Plant Development and Increases Salt Tolerance
    • Gevaudant F, Duby G, von Stedingk E, Zhao R, Morsomme P, Boutry M. Expression of a Constitutively Activated Plasma Membrane H+-ATPase Alters Plant Development and Increases Salt Tolerance. Plant Physiol 2007, 144(4):1763-1776.
    • (2007) Plant Physiol , vol.144 , Issue.4 , pp. 1763-1776
    • Gevaudant, F.1    Duby, G.2    von Stedingk, E.3    Zhao, R.4    Morsomme, P.5    Boutry, M.6
  • 43
    • 46049101277 scopus 로고    scopus 로고
    • Identification of peptidases in Nicotiana tabacum leaf intercellular fluid
    • Delannoy M, Alves G, Vertommen D, Ma J, Boutry M, Navarre C. Identification of peptidases in Nicotiana tabacum leaf intercellular fluid. Proteomics 2008, 8(11):2285-2298.
    • (2008) Proteomics , vol.8 , Issue.11 , pp. 2285-2298
    • Delannoy, M.1    Alves, G.2    Vertommen, D.3    Ma, J.4    Boutry, M.5    Navarre, C.6
  • 44
    • 68349144160 scopus 로고    scopus 로고
    • A membrane-bound matrix-metalloproteinase from Nicotiana tabacum cv. BY-2 is induced by bacterial pathogens
    • Schiermeyer A, Hartenstein H, Mandal M, Otte B, Wahner V, Schillberg S. A membrane-bound matrix-metalloproteinase from Nicotiana tabacum cv. BY-2 is induced by bacterial pathogens. BMC Plant Biology 2009, 9(1):83.
    • (2009) BMC Plant Biology , vol.9 , Issue.1 , pp. 83
    • Schiermeyer, A.1    Hartenstein, H.2    Mandal, M.3    Otte, B.4    Wahner, V.5    Schillberg, S.6
  • 45
    • 0036676947 scopus 로고    scopus 로고
    • Legumains and their functions in plants
    • Müntz K, Shutov AD. Legumains and their functions in plants. Trends in Plant Science 2002, 7(8):340-344.
    • (2002) Trends in Plant Science , vol.7 , Issue.8 , pp. 340-344
    • Müntz, K.1    Shutov, A.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.