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Volumn 32, Issue 3-4, 2015, Pages 161-172

Glycan structure and serum half-life of recombinant CTLA4Ig, an immunosuppressive agent, expressed in suspension-cultured rice cells with coexpression of human β1,4-galactosyltransferase and human CTLA4Ig

(22)  Kang, Seung Hoon a   Jung, Hahn Sun a   Lee, Song Jae a   Park, Cheon Ik a   Lim, Sang Min a   Park, Heajin b   Kim, Byung Sun b   Na, Kwang Heum b   Han, Gyeong Jin b   Bae, Jae Woo b   Park, Hyun Joo b   Bang, Keuk Chan b   Park, Byung Tae b   Hwang, Hye Seong b   Jung, In Soo c   Kim, Jae Il d   Oh, Doo Byung e   Kim, Dong Il f   Yagi, Hirokazu g   Kato, Koichi g,h   more..


Author keywords

Clearance; CTLA4Ig; Half life; Human 1,4 galactosyltransferase; N glycan; Plant cell culture

Indexed keywords

ABATACEPT; ALPHA 1,3 FUCOSE; BETA 1,2 XYLOSE; BETA 1,4 GALACTOSYLTRANSFERASE; FUCOSE; GALACTOSYLTRANSFERASE; GENOMIC DNA; GLYCAN; UNCLASSIFIED DRUG; XYLOSE; BETA1,4-GALACTOSYLTRANSFERASE, HUMAN; HYBRID PROTEIN; IMMUNOSUPPRESSIVE AGENT; POLYSACCHARIDE;

EID: 84929963973     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1007/s10719-015-9590-x     Document Type: Article
Times cited : (8)

References (44)
  • 1
    • 34250346068 scopus 로고    scopus 로고
    • From planta to pharma with glycosylation in the toolbox
    • 1:CAS:528:DC%2BD2sXmsFKhs7o%3D 17493697
    • Saint-Jore-Dupas, C., Faye, L., Gomord, V.: From planta to pharma with glycosylation in the toolbox. Trends Biotechnol. 25, 317-323 (2007)
    • (2007) Trends Biotechnol. , vol.25 , pp. 317-323
    • Saint-Jore-Dupas, C.1    Faye, L.2    Gomord, V.3
  • 2
    • 84879307489 scopus 로고    scopus 로고
    • N-glycosylation of plant-produced recombinant proteins
    • 1:CAS:528:DC%2BC3sXhsVyltr%2FP 23394562
    • Bosch, D., Castilho, A., Loos, A., Schots, A., Steinkellner, H.: N-glycosylation of plant-produced recombinant proteins. Curr. Pharm. Des. 19, 5503-5512 (2013)
    • (2013) Curr. Pharm. Des. , vol.19 , pp. 5503-5512
    • Bosch, D.1    Castilho, A.2    Loos, A.3    Schots, A.4    Steinkellner, H.5
  • 3
    • 0028224656 scopus 로고
    • Glycosylation of recombinant proteins: Problems and prospects
    • 1:CAS:528:DyaK2cXkslKhtLo%3D
    • Jenkins, N., Curling, E.M.: Glycosylation of recombinant proteins: problems and prospects. Enzym. Microb. Technol. 16, 354-364 (1994)
    • (1994) Enzym. Microb. Technol. , vol.16 , pp. 354-364
    • Jenkins, N.1    Curling, E.M.2
  • 6
    • 0034570433 scopus 로고    scopus 로고
    • N-glycosylation of recombinant pharmaceutical glycoproteins produced in transgenic plants: Towards an humanisation of plant N-glycans
    • 1:CAS:528:DC%2BD3MXns1egsw%3D%3D 11467331
    • Lerouge, P., Bardor, M., Pagny, S., Gomord, V., Faye, L.: N-glycosylation of recombinant pharmaceutical glycoproteins produced in transgenic plants: towards an humanisation of plant N-glycans. Curr. Pharm. Biotechnol. 1, 347-354 (2000)
    • (2000) Curr. Pharm. Biotechnol. , vol.1 , pp. 347-354
    • Lerouge, P.1    Bardor, M.2    Pagny, S.3    Gomord, V.4    Faye, L.5
  • 7
    • 0032602265 scopus 로고    scopus 로고
    • Structures of N-linked oligosaccharides of glycoproteins from tobacco BY2 suspension cultured cells
    • 1:CAS:528:DyaK1MXhtVCktrs%3D 10052119
    • Palacpac, N.Q., Kimura, Y., Fujiyama, K., Yoshida, T., Seki, T.: Structures of N-linked oligosaccharides of glycoproteins from tobacco BY2 suspension cultured cells. Biosci. Biotechnol. Biochem. 63, 35-39 (1999)
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 35-39
    • Palacpac, N.Q.1    Kimura, Y.2    Fujiyama, K.3    Yoshida, T.4    Seki, T.5
  • 8
    • 34248137611 scopus 로고    scopus 로고
    • Production of mouse monoclonal antibody with galactose-extended sugar chain by suspension cultured tobacco BY2 cells expressing human beta(1,4)-galactosyltransferase
    • 1:CAS:528:DC%2BD2sXlt1ertLc%3D 17481579
    • Fujiyama, K., Furukawa, A., Katsura, A., Misaki, R., Omasa, T., Seki, T.: Production of mouse monoclonal antibody with galactose-extended sugar chain by suspension cultured tobacco BY2 cells expressing human beta(1,4)-galactosyltransferase. Biochem. Biophys. Res. Commun. 358, 85-91 (2007)
    • (2007) Biochem. Biophys. Res. Commun. , vol.358 , pp. 85-91
    • Fujiyama, K.1    Furukawa, A.2    Katsura, A.3    Misaki, R.4    Omasa, T.5    Seki, T.6
  • 9
    • 0033551250 scopus 로고    scopus 로고
    • Stable expression of human beta1,4-galactosyltransferase in plant cells modifies N-linked glycosylation patterns
    • 16394 1:CAS:528:DyaK1MXjs1ylt7o%3D 10200324
    • Palacpac, N.Q., Yoshida, S., Sakai, H., Kimura, Y., Fujiyama, K., Yoshida, T., Seki, T.: Stable expression of human beta1,4-galactosyltransferase in plant cells modifies N-linked glycosylation patterns. Proc. Natl. Acad. Sci. U. S. A. 96, 4692-4697 (1999)
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 4692-4697
    • Palacpac, N.Q.1    Yoshida, S.2    Sakai, H.3    Kimura, Y.4    Fujiyama, K.5    Yoshida, T.6    Seki, T.7
  • 11
    • 0028858727 scopus 로고
    • CTLA4Ig: A novel immunoglobulin chimera with immunosuppressive properties
    • Robert, J.P., Peter, S.L.: CTLA4Ig: a novel immunoglobulin chimera with immunosuppressive properties. Methods 8, 116-123 (1995)
    • (1995) Methods , vol.8 , pp. 116-123
    • Robert, J.P.1    Peter, S.L.2
  • 14
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • 1:CAS:528:DC%2BD3sXjtFGjuw%3D%3D 12527303
    • Krapp, S., Mimura, Y., Jefferis, R., Huber, R., Sondermann, P.: Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. J. Mol. Biol. 325, 979-989 (2003)
    • (2003) J. Mol. Biol. , vol.325 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 15
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution
    • 1:CAS:528:DyaL3MXitVKqtrc%3D 7236608
    • Deisenhofer, J.: Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution. Biochemistry 20, 2361-2370 (1981)
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 16
    • 34047142084 scopus 로고    scopus 로고
    • Structural comparison of fucosylated and nonfucosylated Fc fragments of human immunoglobulin G1
    • 1:CAS:528:DC%2BD2sXjvFemsL0%3D 17368483
    • Matsumiya, S., Yamaguchi, Y., Saito, J., Nagano, M., Sasakawa, H., Otaki, S., Satoh, M., Shitara, K., Kato, K.: Structural comparison of fucosylated and nonfucosylated Fc fragments of human immunoglobulin G1. J. Mol. Biol. 368, 767-779 (2007)
    • (2007) J. Mol. Biol. , vol.368 , pp. 767-779
    • Matsumiya, S.1    Yamaguchi, Y.2    Saito, J.3    Nagano, M.4    Sasakawa, H.5    Otaki, S.6    Satoh, M.7    Shitara, K.8    Kato, K.9
  • 17
    • 80054944116 scopus 로고    scopus 로고
    • Structural basis for improved efficacy of therapeutic antibodies upon defucosylation of their Fc glycans
    • 3258418 1:CAS:528:DC%2BC3MXhsFSjsrzO 22023369
    • Mizushima, T., Yagi, H., Takemoto, E., Shibata-Koyama, M., Isoda, Y., Iida, S., Masuda, K., Satoh, M., Kato, K.: Structural basis for improved efficacy of therapeutic antibodies upon defucosylation of their Fc glycans. Genes Cells 16, 1071-1080 (2011)
    • (2011) Genes Cells , vol.16 , pp. 1071-1080
    • Mizushima, T.1    Yagi, H.2    Takemoto, E.3    Shibata-Koyama, M.4    Isoda, Y.5    Iida, S.6    Masuda, K.7    Satoh, M.8    Kato, K.9
  • 18
    • 0029558207 scopus 로고
    • The effect of the removal of sialic acid, galactose and total carbohydrate on the functional activity of Campath-1H
    • 1:CAS:528:DyaK28Xhs1aiu78%3D 8643100
    • Boyd, P.N., Lines, A.C., Patel, A.K.: The effect of the removal of sialic acid, galactose and total carbohydrate on the functional activity of Campath-1H. Mol. Immunol. 32, 1311-1318 (1995)
    • (1995) Mol. Immunol. , vol.32 , pp. 1311-1318
    • Boyd, P.N.1    Lines, A.C.2    Patel, A.K.3
  • 19
    • 0031033895 scopus 로고    scopus 로고
    • Effect of glycosylation on antibody function: Implications for genetic engineering
    • 1:CAS:528:DyaK2sXhtFCiurc%3D 9032990
    • Wright, A., Morrison, S.L.: Effect of glycosylation on antibody function: implications for genetic engineering. Trends Biotechnol. 15, 26-32 (1997)
    • (1997) Trends Biotechnol. , vol.15 , pp. 26-32
    • Wright, A.1    Morrison, S.L.2
  • 20
    • 0025674184 scopus 로고
    • Near identity of HeLa cell galactosyltransferase with the human placental enzyme
    • 332820 1:CAS:528:DyaK3MXksVGjtr8%3D 2124683
    • Watzele, G., Berger, E.G.: Near identity of HeLa cell galactosyltransferase with the human placental enzyme. Nucleic Acids Res. 18, 7174 (1990)
    • (1990) Nucleic Acids Res. , vol.18 , pp. 7174
    • Watzele, G.1    Berger, E.G.2
  • 21
    • 33750094693 scopus 로고    scopus 로고
    • Three methods for the introduction of foreign DNA into Agrobacterium
    • 16988332
    • Wise, A.A., Liu, Z., Binns, A.N.: Three methods for the introduction of foreign DNA into Agrobacterium. Methods Mol. Biol. 343, 43-53 (2006)
    • (2006) Methods Mol. Biol. , vol.343 , pp. 43-53
    • Wise, A.A.1    Liu, Z.2    Binns, A.N.3
  • 22
    • 1842720144 scopus 로고    scopus 로고
    • A large-scale Agrobacterium-mediated transformation procedure with a strong positive-negative selection for gene targeting in rice (Oryza sativa L.)
    • 1:CAS:528:DC%2BD2cXis1Ghurc%3D 14740168
    • Terada, R., Asao, H., Iida, S.: A large-scale Agrobacterium-mediated transformation procedure with a strong positive-negative selection for gene targeting in rice (Oryza sativa L.). Plant Cell Rep. 22, 653-659 (2004)
    • (2004) Plant Cell Rep. , vol.22 , pp. 653-659
    • Terada, R.1    Asao, H.2    Iida, S.3
  • 23
    • 46149140783 scopus 로고
    • Protoplast culture of rice (Oryza sativa L.) using media solidified with agarose
    • Thompson, J.A., Abdullah, R., Cocking, E.C.: Protoplast culture of rice (Oryza sativa L.) using media solidified with agarose. Plant Sci. 47, 123-133 (1986)
    • (1986) Plant Sci. , vol.47 , pp. 123-133
    • Thompson, J.A.1    Abdullah, R.2    Cocking, E.C.3
  • 24
    • 0028950435 scopus 로고
    • Identification of neutral and sialyl N-linked oligosaccharide structures from human serum glycoproteins using three kinds of high-performance liquid chromatography
    • 1:CAS:528:DyaK2MXks1CktLo%3D 7785764
    • Nakagawa, H., Kawamura, Y., Kato, K., Shimada, I., Arata, Y., Takahashi, N.: Identification of neutral and sialyl N-linked oligosaccharide structures from human serum glycoproteins using three kinds of high-performance liquid chromatography. Anal. Biochem. 226, 130-138 (1995)
    • (1995) Anal. Biochem. , vol.226 , pp. 130-138
    • Nakagawa, H.1    Kawamura, Y.2    Kato, K.3    Shimada, I.4    Arata, Y.5    Takahashi, N.6
  • 25
    • 0142134975 scopus 로고    scopus 로고
    • GALAXY (glycoanalysis by the three axes of MS and chromatography): A web application that assists structural analyses of N-glycans
    • 1:CAS:528:DC%2BD3sXosF2mtLg%3D
    • Takahashi, N., Kato, K.: GALAXY (glycoanalysis by the three axes of MS and chromatography): a web application that assists structural analyses of N-glycans. Trends Glycosci. Glycotechnol. 15, 235-251 (2003)
    • (2003) Trends Glycosci. Glycotechnol. , vol.15 , pp. 235-251
    • Takahashi, N.1    Kato, K.2
  • 26
    • 84895124460 scopus 로고    scopus 로고
    • Type and branched pattern of N-glycans and their structural effect on the chicken egg allergen ovotransferrin: A comparison with ovomucoid
    • 1:CAS:528:DC%2BC3sXhsVSns7zO 24014058
    • Hwang, H.S., Kim, B.S., Park, H., Park, H.Y., Choi, H.D., Kim, H.H.: Type and branched pattern of N-glycans and their structural effect on the chicken egg allergen ovotransferrin: a comparison with ovomucoid. Glycoconj. J. 31, 41-50 (2014)
    • (2014) Glycoconj. J. , vol.31 , pp. 41-50
    • Hwang, H.S.1    Kim, B.S.2    Park, H.3    Park, H.Y.4    Choi, H.D.5    Kim, H.H.6
  • 27
    • 33845294049 scopus 로고    scopus 로고
    • Characterization of human cytotoxic T lymphocyte-associated antigen 4-immunoglobulin (hCTLA4Ig) expressed in transgenic rice cell suspension cultures
    • 1:CAS:528:DC%2BD28Xht1GmsrvL 17072529
    • Jung, H.S., Koo, J.K., Lee, S.J., Park, C.I., Shin, J.Y., Kim, M.H., Tan, H.K., Lim, S.M., Kim, D.I.: Characterization of human cytotoxic T lymphocyte-associated antigen 4-immunoglobulin (hCTLA4Ig) expressed in transgenic rice cell suspension cultures. Biotechnol. Lett. 28, 2039-2048 (2006)
    • (2006) Biotechnol. Lett. , vol.28 , pp. 2039-2048
    • Jung, H.S.1    Koo, J.K.2    Lee, S.J.3    Park, C.I.4    Shin, J.Y.5    Kim, M.H.6    Tan, H.K.7    Lim, S.M.8    Kim, D.I.9
  • 28
    • 0031596341 scopus 로고    scopus 로고
    • Core alpha1,3-fucose is a key part of the epitope recognized by antibodies reacting against plant N-linked oligosaccharides and is present in a wide variety of plant extracts
    • 1:CAS:528:DyaK1cXksFClurg%3D 9621106
    • Wilson, I.B., Harthill, J.E., Mullin, N.P., Ashford, D.A., Altmann, F.: Core alpha1,3-fucose is a key part of the epitope recognized by antibodies reacting against plant N-linked oligosaccharides and is present in a wide variety of plant extracts. Glycobiology 8, 651-661 (1998)
    • (1998) Glycobiology , vol.8 , pp. 651-661
    • Wilson, I.B.1    Harthill, J.E.2    Mullin, N.P.3    Ashford, D.A.4    Altmann, F.5
  • 29
    • 0027934095 scopus 로고
    • Recent progress in molecular cloning of glycosyltransferase genes of eukaryotes
    • 1:CAS:528:DyaK2MXlsFyjuw%3D%3D 7968681
    • Narimatsu, H.: Recent progress in molecular cloning of glycosyltransferase genes of eukaryotes. Microbiol. Immunol. 38, 489-504 (1994)
    • (1994) Microbiol. Immunol. , vol.38 , pp. 489-504
    • Narimatsu, H.1
  • 30
    • 48549090941 scopus 로고    scopus 로고
    • Terminal sugars of Fc glycans influence antibody effector functions of IgGs
    • 1:CAS:528:DC%2BD1cXpslSltL0%3D 18606225
    • Raju, T.S.: Terminal sugars of Fc glycans influence antibody effector functions of IgGs. Curr. Opin. Immunol. 20, 471-478 (2008)
    • (2008) Curr. Opin. Immunol. , vol.20 , pp. 471-478
    • Raju, T.S.1
  • 31
    • 33947545682 scopus 로고    scopus 로고
    • Sialic acids: Carbohydrate moieties that influence the biological and physical properties of biopharmaceutical proteins and living cells
    • 1:CAS:528:DC%2BD2sXjs1Ontb4%3D 17395092
    • Byrne, B., Donohoe, G.G., O'Kennedy, R.: Sialic acids: carbohydrate moieties that influence the biological and physical properties of biopharmaceutical proteins and living cells. Drug Discov. Today 12, 319-326 (2007)
    • (2007) Drug Discov. Today , vol.12 , pp. 319-326
    • Byrne, B.1    Donohoe, G.G.2    O'Kennedy, R.3
  • 35
    • 0000592224 scopus 로고
    • Substrate specificities of N-acetylglucosaminyl-, fucosyl-, and xylosyltransferases that modify glycoproteins in the Golgi apparatus of bean cotyledons
    • 1056769 1:CAS:528:DyaL2sXlvFeqs7c%3D 16665602
    • Johnson, K.D., Chrispeels, M.J.: Substrate specificities of N-acetylglucosaminyl-, fucosyl-, and xylosyltransferases that modify glycoproteins in the Golgi apparatus of bean cotyledons. Plant Physiol. 84, 1301-1308 (1987)
    • (1987) Plant Physiol. , vol.84 , pp. 1301-1308
    • Johnson, K.D.1    Chrispeels, M.J.2
  • 36
    • 16844385133 scopus 로고    scopus 로고
    • Modification of plant N-glycans processing: The future of producing therapeutic protein by transgenic plants
    • 1:CAS:528:DC%2BD2MXjslGit7s%3D 15499575
    • Chen, M., Liu, X., Wang, Z., Song, J., Qi, Q., Wang, P.G.: Modification of plant N-glycans processing: the future of producing therapeutic protein by transgenic plants. Med. Res. Rev. 25, 343-360 (2005)
    • (2005) Med. Res. Rev. , vol.25 , pp. 343-360
    • Chen, M.1    Liu, X.2    Wang, Z.3    Song, J.4    Qi, Q.5    Wang, P.G.6
  • 38
    • 0033571091 scopus 로고    scopus 로고
    • Binding and uptake of agalactosyl IgG by mannose receptor on macrophages and dendritic cells
    • 10553068
    • Dong, X., Storkus, W.J., Salter, R.D.: Binding and uptake of agalactosyl IgG by mannose receptor on macrophages and dendritic cells. J. Immunol. 163, 5427-5434 (1999)
    • (1999) J. Immunol. , vol.163 , pp. 5427-5434
    • Dong, X.1    Storkus, W.J.2    Salter, R.D.3
  • 39
    • 0032055988 scopus 로고    scopus 로고
    • Effect of C2-associated carbohydrate structure on Ig effector function: Studies with chimeric mouse-human IgG1 antibodies in glycosylation mutants of Chinese hamster ovary cells
    • 9531299
    • Wright, A., Morrison, S.L.: Effect of C2-associated carbohydrate structure on Ig effector function: studies with chimeric mouse-human IgG1 antibodies in glycosylation mutants of Chinese hamster ovary cells. J. Immunol. 160, 3393-3402 (1998)
    • (1998) J. Immunol. , vol.160 , pp. 3393-3402
    • Wright, A.1    Morrison, S.L.2
  • 41
    • 79958837668 scopus 로고    scopus 로고
    • High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans
    • 1:CAS:528:DC%2BC3MXnsFWlur8%3D 21421994
    • Goetze, A.M., Liu, Y.D., Zhang, Z., Shah, B., Lee, E., Bondarenko, P.V., Flynn, G.C.: High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans. Glycobiology 21, 949-959 (2011)
    • (2011) Glycobiology , vol.21 , pp. 949-959
    • Goetze, A.M.1    Liu, Y.D.2    Zhang, Z.3    Shah, B.4    Lee, E.5    Bondarenko, P.V.6    Flynn, G.C.7
  • 43
    • 0034691229 scopus 로고    scopus 로고
    • Ammonium alters N-glycan structures of recombinant TNFR-IgG: Degradative versus biosynthetic mechanisms
    • 1:CAS:528:DC%2BD3cXjs1ygtLw%3D 10799988
    • Gawlitzek, M., Ryll, T., Lofgren, J., Sliwkowski, M.B.: Ammonium alters N-glycan structures of recombinant TNFR-IgG: degradative versus biosynthetic mechanisms. Biotechnol. Bioeng. 68, 637-646 (2000)
    • (2000) Biotechnol. Bioeng. , vol.68 , pp. 637-646
    • Gawlitzek, M.1    Ryll, T.2    Lofgren, J.3    Sliwkowski, M.B.4
  • 44
    • 34547630740 scopus 로고    scopus 로고
    • Influence of culture medium supplementation of tobacco NT1 cell suspension cultures on the N-glycosylation of human secreted alkaline phosphatase
    • 1:CAS:528:DC%2BD2sXotleqsbk%3D 17238209
    • Becerra-Arteaga, A., Shuler, M.L.: Influence of culture medium supplementation of tobacco NT1 cell suspension cultures on the N-glycosylation of human secreted alkaline phosphatase. Biotechnol. Bioeng. 97, 1585-1593 (2007)
    • (2007) Biotechnol. Bioeng. , vol.97 , pp. 1585-1593
    • Becerra-Arteaga, A.1    Shuler, M.L.2


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