메뉴 건너뛰기




Volumn 58, Issue 18, 2010, Pages 10056-10063

Plant-produced trastuzumab inhibits the growth of HER2 positive cancer cells

Author keywords

Affinity purification; biopharming; biosimilar; HER2; Herceptin; Nicotiana benthamiana; plant produced mAb; therapeutic mAbs; trastuzumab

Indexed keywords

AFFINITY PURIFICATION; BIOPHARMING; BIOSIMILAR; HER2; HERCEPTIN; NICOTIANA BENTHAMIANA; PLANT-PRODUCED MAB; THERAPEUTIC MABS; TRASTUZUMAB;

EID: 77956630367     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf102284f     Document Type: Article
Times cited : (36)

References (54)
  • 2
    • 62149129236 scopus 로고    scopus 로고
    • Therapeutic antibodies: Successes, limitations and hopes for the future
    • Chames, P.; Van Regenmortel, M.; Weiss, E.; Baty, D. Therapeutic antibodies: successes, limitations and hopes for the future Br. J. Pharmacol. 2009, 157, 220-233
    • (2009) Br. J. Pharmacol. , vol.157 , pp. 220-233
    • Chames, P.1    Van Regenmortel, M.2    Weiss, E.3    Baty, D.4
  • 3
    • 64949085560 scopus 로고    scopus 로고
    • Therapeutic Antibodies: Current State and Future Trends: Is a Paradigm Change Coming Soon?
    • In;, Ed.; Humana Press: New York, NY
    • Dimitrov, D. S.; Marks, J. D. Therapeutic Antibodies: Current State and Future Trends: Is a Paradigm Change Coming Soon? In Therapeutic Antibodies; Dimitrov, A. S., Ed.; Humana Press: New York, NY, 2009; pp 1-27.
    • (2009) Therapeutic Antibodies , pp. 1-27
    • Dimitrov, D.S.1    Marks, J.D.2    Dimitrov, A.S.3
  • 4
    • 0035313152 scopus 로고    scopus 로고
    • Therapeutic antibody expression technology
    • Chadd, H. E.; Chamow, S. M. Therapeutic antibody expression technology Curr. Opin. Biotechnol. 2001, 12, 188-194
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 188-194
    • Chadd, H.E.1    Chamow, S.M.2
  • 6
    • 67849095742 scopus 로고    scopus 로고
    • Production of Antibodies in Plants: Approaches and Perspectives
    • In;, Ed.; Springer-Verlag: Berlin, Germany
    • Ko, K.; Brodzik, R.; Steplewski, Z. Production of Antibodies in Plants: Approaches and Perspectives. In Plant-Produced Microbial Vaccines; Karasev, A., Ed.; Springer-Verlag: Berlin, Germany, 2009; pp 55-78.
    • (2009) Plant-Produced Microbial Vaccines , pp. 55-78
    • Ko, K.1    Brodzik, R.2    Steplewski, Z.3    Karasev, A.4
  • 8
    • 38949210239 scopus 로고    scopus 로고
    • Preparing recombinant single chain antibodies
    • Leong, S. S.; Chen, W. N. Preparing recombinant single chain antibodies Chem. Eng. Sci. 2008, 63, 1401-1414
    • (2008) Chem. Eng. Sci. , vol.63 , pp. 1401-1414
    • Leong, S.S.1    Chen, W.N.2
  • 9
    • 70349765520 scopus 로고    scopus 로고
    • The production of biopharmaceuticals in plant systems
    • Karg, S. R.; Kallio, P. T. The production of biopharmaceuticals in plant systems Biotechnol. Adv. 2009, 27, 879-894
    • (2009) Biotechnol. Adv. , vol.27 , pp. 879-894
    • Karg, S.R.1    Kallio, P.T.2
  • 11
    • 34447527576 scopus 로고    scopus 로고
    • Affinity-based methodologies and ligands for antibody purification: Advances and perspectives
    • Roque, A. C.; Silva, C. S.; Taipa, M. Â. Affinity-based methodologies and ligands for antibody purification: advances and perspectives J. Chromatogr., A 2007, 1160, 44-55
    • (2007) J. Chromatogr., A , vol.1160 , pp. 44-55
    • Roque, A.C.1    Silva, C.S.2    Taipa, M.Â.3
  • 13
    • 34248176896 scopus 로고    scopus 로고
    • Biosimilars: Recent developments
    • Covic, A.; Kuhlmann, M. Biosimilars: recent developments Int. Urol. Nephrol. 2007, 39, 261-266
    • (2007) Int. Urol. Nephrol. , vol.39 , pp. 261-266
    • Covic, A.1    Kuhlmann, M.2
  • 14
    • 47349126691 scopus 로고    scopus 로고
    • Biosimilars: Policy, clinical, and regulatory considerations
    • Gottlieb, S. Biosimilars: policy, clinical, and regulatory considerations Am. J. Health Syst. Pharm. 2008, 65, S2-S8
    • (2008) Am. J. Health Syst. Pharm. , vol.65
    • Gottlieb, S.1
  • 15
    • 50149099055 scopus 로고    scopus 로고
    • Plant science: Using tobacco to treat cancer
    • Arntzen, C. J. Plant science: Using tobacco to treat cancer Science 2008, 321, 1052-1053
    • (2008) Science , vol.321 , pp. 1052-1053
    • Arntzen, C.J.1
  • 16
    • 0037130921 scopus 로고    scopus 로고
    • Evolution of antibodies for environmental monitoring: From mice to plants
    • Churchill, R. L. T.; Sheedy, C.; Yau, K. Y. F.; Hall, J. C. Evolution of antibodies for environmental monitoring: from mice to plants Anal. Chim. Acta 2002, 468, 185-197
    • (2002) Anal. Chim. Acta , vol.468 , pp. 185-197
    • Churchill, R.L.T.1    Sheedy, C.2    Yau, K.Y.F.3    Hall, J.C.4
  • 17
    • 77956628637 scopus 로고    scopus 로고
    • Scale-Up of Plant-Derived Pharmaceuticals: Prospects for Commercial Production and for Global Health
    • In; Taylor and Francis Group: Boca Raton, FL
    • Hefferon, K. L. Scale-Up of Plant-Derived Pharmaceuticals: Prospects for Commercial Production and for Global Health. In Biopharmaceuticals in Plants: Toward the Next Century of Medicine; Taylor and Francis Group: Boca Raton, FL, 2010; pp 117-146.
    • (2010) Biopharmaceuticals in Plants: Toward the Next Century of Medicine , pp. 117-146
    • Hefferon, K.L.1
  • 20
    • 77949837380 scopus 로고    scopus 로고
    • Purification of plant-derived antibodies through direct immobilization of affinity ligands on cellulose
    • Hussack, G.; Grohs, B. M.; Almquist, K. C.; McLean, M. D.; Ghosh, R.; Hall, J. C. Purification of plant-derived antibodies through direct immobilization of affinity ligands on cellulose J. Agric. Food Chem. 2010, 58, 3451-3459
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 3451-3459
    • Hussack, G.1    Grohs, B.M.2    Almquist, K.C.3    McLean, M.D.4    Ghosh, R.5    Hall, J.C.6
  • 21
    • 0024959945 scopus 로고
    • Production of antibodies in transgenic plants
    • Hiatt, A.; Caffferkey, R.; Bowdish, K. Production of antibodies in transgenic plants Nature 1989, 342, 76-78
    • (1989) Nature , vol.342 , pp. 76-78
    • Hiatt, A.1    Caffferkey, R.2    Bowdish, K.3
  • 24
    • 62549147841 scopus 로고    scopus 로고
    • Persistent elimination of ErbB-2/HER2-overexpressing tumors using combinations of monoclonal antibodies: Relevance of receptor endocytosis
    • Ben-Kasus, T.; Schechter, B.; Lavi, S.; Yarden, Y.; Sela, M. Persistent elimination of ErbB-2/HER2-overexpressing tumors using combinations of monoclonal antibodies: relevance of receptor endocytosis Proc. Natl. Acad. Sci. U.S.A 2009, 106, 3294-3299
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 3294-3299
    • Ben-Kasus, T.1    Schechter, B.2    Lavi, S.3    Yarden, Y.4    Sela, M.5
  • 25
    • 37049183697 scopus 로고
    • Human breast cancer: Correlation of relapse and survival with amplification of the HER-2/neu oncogene
    • Slamon, D. J.; Clark, G. M.; Wong, S. G.; Levin, W. J.; Ullrich, A.; McGuire, W. L. Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene Science 1987, 235, 177-182
    • (1987) Science , vol.235 , pp. 177-182
    • Slamon, D.J.1    Clark, G.M.2    Wong, S.G.3    Levin, W.J.4    Ullrich, A.5    McGuire, W.L.6
  • 28
    • 0035874981 scopus 로고    scopus 로고
    • Trastuzumab (herceptin), a humanized anti-Her2 receptor monoclonal antibody, inhibits basal and activated Her2 ectodomain cleavage in breast cancer cells
    • Molina, M. A.; Codony-Servat, J.; Albanell, J.; Rojo, F.; Arribas, J.; Baselga, J. Trastuzumab (herceptin), a humanized anti-Her2 receptor monoclonal antibody, inhibits basal and activated Her2 ectodomain cleavage in breast cancer cells Cancer Res. 2001, 61, 4744-4749
    • (2001) Cancer Res. , vol.61 , pp. 4744-4749
    • Molina, M.A.1    Codony-Servat, J.2    Albanell, J.3    Rojo, F.4    Arribas, J.5    Baselga, J.6
  • 29
    • 0034745353 scopus 로고    scopus 로고
    • Cytoplasmic localization of p21Cip1/WAF1 by Akt-induced phosphorylation in HER-2/neu-overexpressing cells
    • Zhou, B. P.; Liao, Y.; Xia, W.; Spohn, B.; Lee, M. H.; Hung, M. C. Cytoplasmic localization of p21Cip1/WAF1 by Akt-induced phosphorylation in HER-2/neu-overexpressing cells Nat. Cell Biol. 2001, 3, 245-252
    • (2001) Nat. Cell Biol. , vol.3 , pp. 245-252
    • Zhou, B.P.1    Liao, Y.2    Xia, W.3    Spohn, B.4    Lee, M.H.5    Hung, M.C.6
  • 30
    • 0038607569 scopus 로고    scopus 로고
    • The role of cyclin-dependent kinase inhibitor p27Kip1 in anti-HER2 antibody-induced G1 cell cycle arrest and tumor growth inhibition
    • Le, X.; Claret, F.; Lammayot, A.; Tian, L.; Deshpande, D.; LaPushin, R.; Tari, A. M.; Bast, R. C. The role of cyclin-dependent kinase inhibitor p27Kip1 in anti-HER2 antibody-induced G1 cell cycle arrest and tumor growth inhibition J. Biol. Chem. 2003, 278, 23441-23450
    • (2003) J. Biol. Chem. , vol.278 , pp. 23441-23450
    • Le, X.1    Claret, F.2    Lammayot, A.3    Tian, L.4    Deshpande, D.5    Lapushin, R.6    Tari, A.M.7    Bast, R.C.8
  • 33
    • 0032850677 scopus 로고    scopus 로고
    • Multinational study of the efficacy and safety of humanized anti-HER2 monoclonal antibody in women who have HER2-overexpressing metastatic breast cancer that has progressed after chemotherapy for metastatic disease
    • Cobleigh, M. A.; Vogel, C. L.; Tripathy, D.; Robert, N. J.; Scholl, S.; Fehrenbacher, L.; Wolter, J. M.; Paton, V.; Shak, S.; Lieberman, G.; Slamon, D. J. Multinational study of the efficacy and safety of humanized anti-HER2 monoclonal antibody in women who have HER2-overexpressing metastatic breast cancer that has progressed after chemotherapy for metastatic disease J. Clin. Oncol. 1999, 17, 2639-2648
    • (1999) J. Clin. Oncol. , vol.17 , pp. 2639-2648
    • Cobleigh, M.A.1    Vogel, C.L.2    Tripathy, D.3    Robert, N.J.4    Scholl, S.5    Fehrenbacher, L.6    Wolter, J.M.7    Paton, V.8    Shak, S.9    Lieberman, G.10    Slamon, D.J.11
  • 36
    • 32844471433 scopus 로고    scopus 로고
    • Expression of an anti-botulinum toxin A neutralizing single-chain Fv recombinant antibody in transgenic tobacco
    • Almquist, K. C.; McLean, M. D.; Niu, Y.; Byrne, G.; Olea-Popelka, F. C.; Murrant, C.; Barclay, J.; Hall, J. C. Expression of an anti-botulinum toxin A neutralizing single-chain Fv recombinant antibody in transgenic tobacco Vaccine 2006, 24, 2079-2086
    • (2006) Vaccine , vol.24 , pp. 2079-2086
    • Almquist, K.C.1    McLean, M.D.2    Niu, Y.3    Byrne, G.4    Olea-Popelka, F.C.5    Murrant, C.6    Barclay, J.7    Hall, J.C.8
  • 37
    • 35948970963 scopus 로고    scopus 로고
    • A human anti-Pseudomonas aeruginosa serotype O6ad immunoglobulin G1 expressed in transgenic tobacco is capable of recruiting immune system effector function in vitro
    • McLean, M. D.; Almquist, K. C.; Niu, Y.; Kimmel, R.; Lai, Z.; Schreiber, J. R.; Hall, J. C. A human anti-Pseudomonas aeruginosa serotype O6ad immunoglobulin G1 expressed in transgenic tobacco is capable of recruiting immune system effector function in vitro Antimicrob. Agents Chemother. 2007, 51, 3322-3328
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 3322-3328
    • McLean, M.D.1    Almquist, K.C.2    Niu, Y.3    Kimmel, R.4    Lai, Z.5    Schreiber, J.R.6    Hall, J.C.7
  • 38
    • 24344449929 scopus 로고    scopus 로고
    • Increasing expression of an anti-picloram single-chain variable fragment (ScFv) antibody and resistance to picloram in transgenic tobacco (Nicotiana tabacum)
    • Olea-Popelka, F.; McLean, M. D.; Horsman, J.; Almquist, K.; Brandle, J. E.; Hall, J. C. Increasing expression of an anti-picloram single-chain variable fragment (ScFv) antibody and resistance to picloram in transgenic tobacco (Nicotiana tabacum) J. Agric. Food Chem. 2005, 53, 6683-6690
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 6683-6690
    • Olea-Popelka, F.1    McLean, M.D.2    Horsman, J.3    Almquist, K.4    Brandle, J.E.5    Hall, J.C.6
  • 39
    • 0001695171 scopus 로고
    • Isolation and characterization of the genes encoding basic and acidic Chitinase in Arabidopsis thaliana
    • Samac, D. A.; Hironaka, C. M.; Yallaly, P. E.; Shah, D. M. Isolation and characterization of the genes encoding basic and acidic Chitinase in Arabidopsis thaliana Plant Physiol. 1990, 93, 907-914
    • (1990) Plant Physiol. , vol.93 , pp. 907-914
    • Samac, D.A.1    Hironaka, C.M.2    Yallaly, P.E.3    Shah, D.M.4
  • 40
    • 24944498904 scopus 로고    scopus 로고
    • Systemic Agrobacterium tumefaciens-mediated transfection of viral replicons for efficient transient expression in plants
    • Marillonnet, S.; Thoeringer, C.; Kandzia, R.; Klimyuk, V.; Gleba, Y. Systemic Agrobacterium tumefaciens-mediated transfection of viral replicons for efficient transient expression in plants Nat. Biotechnol. 2005, 23, 718-723
    • (2005) Nat. Biotechnol. , vol.23 , pp. 718-723
    • Marillonnet, S.1    Thoeringer, C.2    Kandzia, R.3    Klimyuk, V.4    Gleba, Y.5
  • 42
    • 77953999126 scopus 로고    scopus 로고
    • Production of antibodies in plants: Status after twenty years
    • De Muynck, B.; Navarre, C.; Boutry, M. Production of antibodies in plants: status after twenty years Plant Biotechnol. J. 2010, 8, 529-563
    • (2010) Plant Biotechnol. J. , vol.8 , pp. 529-563
    • De Muynck, B.1    Navarre, C.2    Boutry, M.3
  • 44
    • 65549113489 scopus 로고    scopus 로고
    • Fees delay pharmed drug
    • Gilbert, N. Fees delay pharmed drug Nature 2009, 458, 951
    • (2009) Nature , vol.458 , pp. 951
    • Gilbert, N.1
  • 47
    • 0035811160 scopus 로고    scopus 로고
    • Characterization of monoclonal antibody fragments produced by plant cells
    • Sharp, J. M.; Doran, P. M. Characterization of monoclonal antibody fragments produced by plant cells Biotechnol. Bioeng. 2001, 73, 338-346
    • (2001) Biotechnol. Bioeng. , vol.73 , pp. 338-346
    • Sharp, J.M.1    Doran, P.M.2
  • 50
    • 34249823666 scopus 로고    scopus 로고
    • Functional analysis of the broadly neutralizing human anti-HIV-1 antibody 2F5 produced in transgenic BY-2 suspension cultures
    • Sack, M.; Paetz, A.; Kunert, R.; Bomble, M.; Hesse, F.; Stiegler, G.; Fischer, R.; Katinger, H.; Stoeger, E.; Rademacher, T. Functional analysis of the broadly neutralizing human anti-HIV-1 antibody 2F5 produced in transgenic BY-2 suspension cultures FASEB J. 2007, 21, 1655-1664
    • (2007) FASEB J. , vol.21 , pp. 1655-1664
    • Sack, M.1    Paetz, A.2    Kunert, R.3    Bomble, M.4    Hesse, F.5    Stiegler, G.6    Fischer, R.7    Katinger, H.8    Stoeger, E.9    Rademacher, T.10
  • 54
    • 57649129498 scopus 로고    scopus 로고
    • Expression of rat beta(1,4)-N-acetylglucosaminyltransferase III in Nicotiana tabacum remodels the plant-specific N-glycosylation
    • Frey, A. D.; Karg, S. R.; Kallio, P. T. Expression of rat beta(1,4)-N-acetylglucosaminyltransferase III in Nicotiana tabacum remodels the plant-specific N-glycosylation Plant Biotechnol. J. 2009, 7, 33-48
    • (2009) Plant Biotechnol. J. , vol.7 , pp. 33-48
    • Frey, A.D.1    Karg, S.R.2    Kallio, P.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.