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Volumn 36, Issue 1, 2014, Pages 181-190

Production and secretion of a heterologous protein by turnip hairy roots with superiority over tobacco hairy roots

Author keywords

Agrobacterium rhizogenes; Brassica; GFP; Green fluorescent protein; Hairy roots; Heterologous protein production; Protein; Secretion; Tobacco hairy roots

Indexed keywords

AGROBACTERIUM RHIZOGENES; BRASSICA; GFP; GREEN FLUORESCENT PROTEIN; HAIRY ROOTS; HETEROLOGOUS PROTEIN PRODUCTION; SECRETION;

EID: 84891650125     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-013-1335-y     Document Type: Article
Times cited : (25)

References (40)
  • 1
    • 33644821844 scopus 로고    scopus 로고
    • Green fluorescent protein as an efficient selection marker for Agrobacterium rhizogenes mediated carrot transformation
    • Baranski R, Klocke E, Schumann G (2006) Green fluorescent protein as an efficient selection marker for Agrobacterium rhizogenes mediated carrot transformation. Plant Cell Rep 25: 190-197.
    • (2006) Plant Cell Rep , vol.25 , pp. 190-197
    • Baranski, R.1    Klocke, E.2    Schumann, G.3
  • 3
    • 0031391390 scopus 로고    scopus 로고
    • Molecular farming in plants: oilseeds as vehicles for the production of pharmaceutical proteins
    • Boothe JG, Saponja JA, Parmentier DL (1997) Molecular farming in plants: oilseeds as vehicles for the production of pharmaceutical proteins. Drug Dev Res 42: 172-181.
    • (1997) Drug Dev Res , vol.42 , pp. 172-181
    • Boothe, J.G.1    Saponja, J.A.2    Parmentier, D.L.3
  • 4
    • 0037264969 scopus 로고    scopus 로고
    • Therapeutic antibodies for human diseases at the dawn of the twenty-first century
    • Brekke OH, Sandlie I (2003) Therapeutic antibodies for human diseases at the dawn of the twenty-first century. Nature Rev Drug Discov 2: 52-62.
    • (2003) Nature Rev Drug Discov , vol.2 , pp. 52-62
    • Brekke, O.H.1    Sandlie, I.2
  • 5
    • 0020075619 scopus 로고
    • Agrobacterium rhizogenes inserts T-DNA into the genomes of the host plant root cells
    • Chilton MD, Tepfer DA, Petit A, David D, Casse-Delbart F, Tempé J (1982) Agrobacterium rhizogenes inserts T-DNA into the genomes of the host plant root cells. Nature 295: 432-434.
    • (1982) Nature , vol.295 , pp. 432-434
    • Chilton, M.D.1    Tepfer, D.A.2    Petit, A.3    David, D.4    Casse-Delbart, F.5    Tempé, J.6
  • 6
    • 0027093631 scopus 로고
    • Modified binary plant transformation vectors with the wild-type gene encoding NPTII
    • Datla RSS, Hammerlindl JK, Panchuk B, Pelcher LE, Keller W (1992) Modified binary plant transformation vectors with the wild-type gene encoding NPTII. Gene 211: 383-384.
    • (1992) Gene , vol.211 , pp. 383-384
    • Datla, R.S.S.1    Hammerlindl, J.K.2    Panchuk, B.3    Pelcher, L.E.4    Keller, W.5
  • 7
    • 81155131098 scopus 로고    scopus 로고
    • Hairy roots cultures from different Solanaceous species have varying capacities to produce E coli B-subunit heat-labile toxin antigen
    • De Guzman G, Walmsley AM, Webster DE, Hamill JD (2011) Hairy roots cultures from different Solanaceous species have varying capacities to produce E coli B-subunit heat-labile toxin antigen. Biotechnol Lett 33: 2495-2502.
    • (2011) Biotechnol Lett , vol.33 , pp. 2495-2502
    • De Guzman, G.1    Walmsley, A.M.2    Webster, D.E.3    Hamill, J.D.4
  • 8
    • 84877963943 scopus 로고    scopus 로고
    • Therapeutically important proteins from in vitro plant tissue culture systems
    • Doran PM (2013) Therapeutically important proteins from in vitro plant tissue culture systems. Curr Med Chem 20: 1047-1055.
    • (2013) Curr Med Chem , vol.20 , pp. 1047-1055
    • Doran, P.M.1
  • 10
    • 0041473693 scopus 로고    scopus 로고
    • Rhizosecretion of recombinant proteins from plant hairy roots
    • Gaume A, Komarnytsky S, Borisjuk N, Raskin I (2003) Rhizosecretion of recombinant proteins from plant hairy roots. Plant Cell Rep 21: 1188-1193.
    • (2003) Plant Cell Rep , vol.21 , pp. 1188-1193
    • Gaume, A.1    Komarnytsky, S.2    Borisjuk, N.3    Raskin, I.4
  • 11
    • 64349114245 scopus 로고    scopus 로고
    • Emerging trends in plasma-free manufacturing of recombinant protein therapeutics expressed in mammalian cells
    • Grillberger L, Kreil TR, Nasr S, Reiter M (2009) Emerging trends in plasma-free manufacturing of recombinant protein therapeutics expressed in mammalian cells. Biotechnol J 4: 186-201.
    • (2009) Biotechnol J , vol.4 , pp. 186-201
    • Grillberger, L.1    Kreil, T.R.2    Nasr, S.3    Reiter, M.4
  • 12
    • 0029449650 scopus 로고
    • Tools for expressing foreign genes in plants
    • Guerineau F (1995) Tools for expressing foreign genes in plants. Methods Mol Biol 49: 1-32.
    • (1995) Methods Mol Biol , vol.49 , pp. 1-32
    • Guerineau, F.1
  • 13
    • 0025845499 scopus 로고
    • Effects of deletions in the cauliflower mosaic virus polyadenylation sequence on the choice of the polyadenylation sites in tobacco protoplasts
    • Guerineau F, Brooks L, Mullineaux P (1991) Effects of deletions in the cauliflower mosaic virus polyadenylation sequence on the choice of the polyadenylation sites in tobacco protoplasts. Mol Gen Genet 226: 141-144.
    • (1991) Mol Gen Genet , vol.226 , pp. 141-144
    • Guerineau, F.1    Brooks, L.2    Mullineaux, P.3
  • 14
    • 8344236780 scopus 로고    scopus 로고
    • Plant cell cultures for the production of recombinant proteins
    • Hellwig S, Drossard J, Twyman RM, Fischer R (2004) Plant cell cultures for the production of recombinant proteins. Nature Biotechnol 22: 1415-1422.
    • (2004) Nature Biotechnol , vol.22 , pp. 1415-1422
    • Hellwig, S.1    Drossard, J.2    Twyman, R.M.3    Fischer, R.4
  • 15
    • 0037146488 scopus 로고    scopus 로고
    • Highly sensitive and fast protein detection with Coomassie brilliant blue in sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Kang D, Gho YS, Suh M, Kang C (2002) Highly sensitive and fast protein detection with Coomassie brilliant blue in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Bull Korean Chem Soc 23: 1511-1512.
    • (2002) Bull Korean Chem Soc , vol.23 , pp. 1511-1512
    • Kang, D.1    Gho, Y.S.2    Suh, M.3    Kang, C.4
  • 16
    • 80051786735 scopus 로고    scopus 로고
    • A mechanistic understanding of production instability in CHO cell lines expressing recombinant monoclonal antibodies
    • Kim M, O'Callaghan PM, Droms KA, James DC (2011a) A mechanistic understanding of production instability in CHO cell lines expressing recombinant monoclonal antibodies. Biotechnol Bioeng 108: 2434-2446.
    • (2011) Biotechnol Bioeng , vol.108 , pp. 2434-2446
    • Kim, M.1    O'Callaghan, P.M.2    Droms, K.A.3    James, D.C.4
  • 17
    • 78650175360 scopus 로고    scopus 로고
    • Production of functional recombinant bovine trypsin in transgenic rice cell suspension cultures
    • Kim NS, Yu HY, Chung ND, Shin YJ, Kwon TH, Yang MS (2011b) Production of functional recombinant bovine trypsin in transgenic rice cell suspension cultures. Protein Express Purif 76: 121-126.
    • (2011) Protein Express Purif , vol.76 , pp. 121-126
    • Kim, N.S.1    Yu, H.Y.2    Chung, N.D.3    Shin, Y.J.4    Kwon, T.H.5    Yang, M.S.6
  • 18
    • 19444372752 scopus 로고    scopus 로고
    • Plant biopharming of monoclonal antibodies
    • Ko K, Koprowski H (2005) Plant biopharming of monoclonal antibodies. Virus Res 111: 93-100.
    • (2005) Virus Res , vol.111 , pp. 93-100
    • Ko, K.1    Koprowski, H.2
  • 20
  • 21
    • 4644363275 scopus 로고    scopus 로고
    • Production of recombinant proteins by hairy roots cultured in plastic sleeve bioreactors
    • Medina-Bolivar F, Cramer C (2004) Production of recombinant proteins by hairy roots cultured in plastic sleeve bioreactors. Methods Mol Biol 267: 351-363.
    • (2004) Methods Mol Biol , vol.267 , pp. 351-363
    • Medina-Bolivar, F.1    Cramer, C.2
  • 22
    • 0025049063 scopus 로고
    • A rapid and highly efficient method for the preparation of competent Escherichia coli cells
    • Nishimura A, Morita M, Nishimura Y, Sugino Y (1990) A rapid and highly efficient method for the preparation of competent Escherichia coli cells. Nucleic Acids Res 18: 6169.
    • (1990) Nucleic Acids Res , vol.18 , pp. 6169
    • Nishimura, A.1    Morita, M.2    Nishimura, Y.3    Sugino, Y.4
  • 24
    • 78651475481 scopus 로고    scopus 로고
    • The multiplicity of hairy root cultures: prolific possibilities
    • Ono NN, Tian L (2011) The multiplicity of hairy root cultures: prolific possibilities. Plant Sci 180: 439-446.
    • (2011) Plant Sci , vol.180 , pp. 439-446
    • Ono, N.N.1    Tian, L.2
  • 25
    • 61349167735 scopus 로고    scopus 로고
    • Immunoprophylaxis against important diseases of horses, farm animals and birds
    • Patel JR, Heldens JGM (2009) Immunoprophylaxis against important diseases of horses, farm animals and birds. Vaccines 27: 1797-1810.
    • (2009) Vaccines , vol.27 , pp. 1797-1810
    • Patel, J.R.1    Heldens, J.G.M.2
  • 26
    • 37149020754 scopus 로고    scopus 로고
    • Long-term maintenance of a transgenic Catharanthus roseus hairy root line
    • Peebles CA, Gibson SI, Shanks JV, San KY (2007) Long-term maintenance of a transgenic Catharanthus roseus hairy root line. Biotechnol Prog 23: 1517-1518.
    • (2007) Biotechnol Prog , vol.23 , pp. 1517-1518
    • Peebles, C.A.1    Gibson, S.I.2    Shanks, J.V.3    San, K.Y.4
  • 27
    • 79953704799 scopus 로고    scopus 로고
    • Transgenic crops for the production of recombinant vaccines and anti-microbial antibodies
    • Peters J, Stoger E (2011) Transgenic crops for the production of recombinant vaccines and anti-microbial antibodies. Hum Vaccin 7: 367-374.
    • (2011) Hum Vaccin , vol.7 , pp. 367-374
    • Peters, J.1    Stoger, E.2
  • 29
    • 17644390191 scopus 로고    scopus 로고
    • Vaccines: past, present and future
    • Plotkin SA (2005) Vaccines: past, present and future. Nature Med 11: S5-S11.
    • (2005) Nature Med , vol.11
    • Plotkin, S.A.1
  • 31
    • 0035543343 scopus 로고    scopus 로고
    • Strategies for enhancing monoclonal antibody accumulation in plant cell and organ cultures
    • Sharp JM, Doran PM (2001) Strategies for enhancing monoclonal antibody accumulation in plant cell and organ cultures. Biotechnol Prog 17: 979-992.
    • (2001) Biotechnol Prog , vol.17 , pp. 979-992
    • Sharp, J.M.1    Doran, P.M.2
  • 32
    • 70349765665 scopus 로고    scopus 로고
    • Foreign protein production using plant cell and organ cultures: advantages and limitations
    • Shih SMH, Doran PM (2009) Foreign protein production using plant cell and organ cultures: advantages and limitations. Biotechnol Adv 27: 1036-1042.
    • (2009) Biotechnol Adv , vol.27 , pp. 1036-1042
    • Shih, S.M.H.1    Doran, P.M.2
  • 33
    • 0037572329 scopus 로고    scopus 로고
    • High level of expression of recombinant human granulocyte-macrophage colony stimulating factor in transgenic rice cell suspension culture
    • Shin YJ, Hong SY, Kwon TH, Jang YS, Yang MS (2003) High level of expression of recombinant human granulocyte-macrophage colony stimulating factor in transgenic rice cell suspension culture. Biotechnol Bioeng 82: 778-783.
    • (2003) Biotechnol Bioeng , vol.82 , pp. 778-783
    • Shin, Y.J.1    Hong, S.Y.2    Kwon, T.H.3    Jang, Y.S.4    Yang, M.S.5
  • 34
    • 15244351004 scopus 로고    scopus 로고
    • Overview of monoclonal antibodies in cancer therapy: present and promise
    • Stern M, Herrmann R (2005) Overview of monoclonal antibodies in cancer therapy: present and promise. Crit Rev Oncol Hematol 54: 11-29.
    • (2005) Crit Rev Oncol Hematol , vol.54 , pp. 11-29
    • Stern, M.1    Herrmann, R.2
  • 35
    • 33845756751 scopus 로고    scopus 로고
    • Approaches to achieve high-level heterologous protein production in plants
    • Streatfield SJ (2007) Approaches to achieve high-level heterologous protein production in plants. Plant Biotechnol J 5: 2-15.
    • (2007) Plant Biotechnol J , vol.5 , pp. 2-15
    • Streatfield, S.J.1
  • 37
    • 0021738226 scopus 로고
    • Fluorescein isothiocyanate-labeled casein assay for proteolytic enzymes
    • Twining SS (1984) Fluorescein isothiocyanate-labeled casein assay for proteolytic enzymes. Anal Biochem 143: 30-34.
    • (1984) Anal Biochem , vol.143 , pp. 30-34
    • Twining, S.S.1
  • 38
    • 0031554422 scopus 로고    scopus 로고
    • Production of monoclonal antibodies by tobacco hairy roots
    • Wongsamuth R, Doran PM (1997) Production of monoclonal antibodies by tobacco hairy roots. Biotechnol Bioeng 54: 401-415.
    • (1997) Biotechnol Bioeng , vol.54 , pp. 401-415
    • Wongsamuth, R.1    Doran, P.M.2
  • 39
    • 61649119662 scopus 로고    scopus 로고
    • Hairy-root organ cultures for the production of human acetylcholinesterase
    • Woods RR, Geyer BC, Mor TS (2008) Hairy-root organ cultures for the production of human acetylcholinesterase. BMC Biotechnol 8: 95.
    • (2008) BMC Biotechnol , vol.8 , pp. 95
    • Woods, R.R.1    Geyer, B.C.2    Mor, T.S.3
  • 40
    • 84864941692 scopus 로고    scopus 로고
    • Green factory: plants as bioproduction platforms for recombinant proteins
    • Xu J, Dolan MC, Medrano G, Cramer CL, Weathers PJ (2012) Green factory: plants as bioproduction platforms for recombinant proteins. Biotechnol Adv 30: 1171-1184.
    • (2012) Biotechnol Adv , vol.30 , pp. 1171-1184
    • Xu, J.1    Dolan, M.C.2    Medrano, G.3    Cramer, C.L.4    Weathers, P.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.