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Volumn 4, Issue 3, 2012, Pages 326-340

Quantitative evaluation of fucose reducing effects in a humanized antibody on Fcγ receptor binding and antibody-dependent cell-mediated cytotoxicity activities

Author keywords

Afucosylated antibody; Antibody dependent cellular cytotoxicity; Fc RIIIA; Fucosylation; Glycoform variants; Glycosylation; Monoclonal antibody

Indexed keywords

CD20 ANTIGEN; COMPLEMENT COMPONENT C1Q; FC RECEPTOR; FC RECEPTOR IIA; FC RECEPTOR IIB; FC RECEPTOR IIIA; FUCOSE; GLYCAN; MONOCLONAL ANTIBODY; UNCLASSIFIED DRUG;

EID: 84860911340     PISSN: 19420862     EISSN: 19420870     Source Type: Journal    
DOI: 10.4161/mabs.19941     Document Type: Article
Times cited : (108)

References (49)
  • 1
    • 67649394336 scopus 로고    scopus 로고
    • Recombinant antibody therapeutics: The impact of glycosylation on mechanisms of action
    • PMID:19552968
    • Jefferis R. Recombinant antibody therapeutics: the impact of glycosylation on mechanisms of action. Trends Pharmacol Sci 2009; 30:356-62; PMID:19552968; http://dx.doi.org/10.1016/j.tips.2009.04.007.
    • (2009) Trends Pharmacol Sci , vol.30 , pp. 356-362
    • Jefferis, R.1
  • 2
    • 48549090941 scopus 로고    scopus 로고
    • Terminal sugars of Fc glycans influence antibody effector functions of IgGs
    • PMID:18606225
    • Raju TS. Terminal sugars of Fc glycans influence antibody effector functions of IgGs. Curr Opin Immunol 2008; 20:471-8; PMID:18606225; http://dx.doi.org/10.1016/j.coi.2008.06.007.
    • (2008) Curr Opin Immunol , vol.20 , pp. 471-478
    • Raju, T.S.1
  • 3
    • 79551575923 scopus 로고    scopus 로고
    • Advances in the assessment and control of the effector functions of therapeutic antibodies
    • PMID:21283105
    • Jiang XR, Song A, Bergelson S, Arroll T, Parekh B, May K, et al. Advances in the assessment and control of the effector functions of therapeutic antibodies. Nat Rev Drug Discov 2011; 10:101-11; PMID:21283105; http://dx.doi.org/10.1038/nrd3365.
    • (2011) Nat Rev Drug Discov , vol.10 , pp. 101-111
    • Jiang, X.R.1    Song, A.2    Bergelson, S.3    Arroll, T.4    Parekh, B.5    May, K.6
  • 4
    • 0034691322 scopus 로고    scopus 로고
    • The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex
    • PMID:10917521
    • Sondermann P, Huber R, Oosthuizen V, Jacob U. The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex. Nature 2000; 406:267-73; PMID:10917521; http://dx.doi.org/10.1038/35018508.
    • (2000) Nature , vol.406 , pp. 267-273
    • Sondermann, P.1    Huber, R.2    Oosthuizen, V.3    Jacob, U.4
  • 5
    • 0035844212 scopus 로고    scopus 로고
    • The structure of a human type III Fcgamma receptor in complex with Fc
    • PMID:11297532
    • Radaev S, Motyka S, Fridman WH, Sautes-Fridman C, Sun PD. The structure of a human type III Fcgamma receptor in complex with Fc. J Biol Chem 2001; 276:16469-77; PMID:11297532; http://dx.doi.org/10.1074/jbc.M100350200.
    • (2001) J Biol Chem , vol.276 , pp. 16469-16477
    • Radaev, S.1    Motyka, S.2    Fridman, W.H.3    Sautes-Fridman, C.4    Sun, P.D.5
  • 6
    • 0035827222 scopus 로고    scopus 로고
    • Molecular basis for immune complex recognition: A comparison of Fc-receptor structures
    • PMID:11397093
    • Sondermann P, Kaiser J, Jacob U. Molecular basis for immune complex recognition: a comparison of Fc-receptor structures. J Mol Biol 2001; 309:737-49; PMID:11397093; http://dx.doi.org/10.1006/jmbi.2001.4670.
    • (2001) J Mol Biol , vol.309 , pp. 737-749
    • Sondermann, P.1    Kaiser, J.2    Jacob, U.3
  • 7
    • 0037013743 scopus 로고    scopus 로고
    • Interaction sites on human IgG-Fc for FcgammaR: Current models
    • PMID:12008035
    • Jefferis R, Lund J. Interaction sites on human IgG-Fc for FcgammaR: current models. Immunol Lett 2002; 82:57-65; PMID:12008035; http://dx.doi.org/ 10.1016/S0165-2478(02)00019-6.
    • (2002) Immunol Lett , vol.82 , pp. 57-65
    • Jefferis, R.1    Lund, J.2
  • 8
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • PMID: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 2003; 325:979-89; PMID:12527303; http://dx.doi.org/10.1016/S0022-2836(02)01250-0.
    • (2003) J Mol Biol , vol.325 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 9
    • 0034050074 scopus 로고    scopus 로고
    • Species-specific variation in glycosylation of IgG: Evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics
    • PMID:10764836
    • Raju TS, Briggs JB, Borge SM, Jones AJ. Species-specific variation in glycosylation of IgG: evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics. Glycobiology 2000; 10:477-86; PMID:10764836; http://dx.doi.org/10.1093/glycob/10.5.477.
    • (2000) Glycobiology , vol.10 , pp. 477-486
    • Raju, T.S.1    Briggs, J.B.2    Borge, S.M.3    Jones, A.J.4
  • 10
    • 0035824579 scopus 로고    scopus 로고
    • Role of oligosaccharide residues of IgG1-Fc in Fcgamma RIIb binding
    • PMID:11567028
    • Mimura Y, Sondermann P, Ghirlando R, Lund J, Young SP, Goodall M, et al. Role of oligosaccharide residues of IgG1-Fc in Fcgamma RIIb binding. J Biol Chem 2001; 276:45539-47; PMID:11567028; http://dx.doi.org/10.1074/jbc.M107478200.
    • (2001) J Biol Chem , vol.276 , pp. 45539-45547
    • Mimura, Y.1    Sondermann, P.2    Ghirlando, R.3    Lund, J.4    Young, S.P.5    Goodall, M.6
  • 11
    • 0021041854 scopus 로고
    • Biological significance of carbohydrate chains on monoclonal antibodies
    • PMID:6579549
    • Nose M, Wigzell H. Biological significance of carbohydrate chains on monoclonal antibodies. Proc Natl Acad Sci USA 1983; 80:6632-6; PMID:6579549; http://dx.doi.org/10.1073/pnas.80.21.6632.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 6632-6636
    • Nose, M.1    Wigzell, H.2
  • 12
    • 0024438061 scopus 로고
    • Studies of aglycosylated chimeric mouse-human IgG. Role of carbohydrate in the structure and effector functions mediated by the human IgG constant region
    • PMID:2507634
    • Tao MH, Morrison SL. Studies of aglycosylated chimeric mouse-human IgG. Role of carbohydrate in the structure and effector functions mediated by the human IgG constant region. J Immunol 1989; 143:2595-601; PMID:2507634.
    • (1989) J Immunol , vol.143 , pp. 2595-2601
    • Tao, M.H.1    Morrison, S.L.2
  • 13
    • 0024544730 scopus 로고
    • Aglycosylation of human IgG1 and IgG3 monoclonal antibodies can eliminate recognition by human cells expressing Fcgamma RI and/or Fcgamma RII receptors
    • PMID:2524188
    • Walker MR, Lund J, Thompson KM, Jefferis R. Aglycosylation of human IgG1 and IgG3 monoclonal antibodies can eliminate recognition by human cells expressing Fcgamma RI and/or Fcgamma RII receptors. Biochem J 1989; 259:347-53; PMID:2524188.
    • (1989) Biochem J , vol.259 , pp. 347-353
    • Walker, M.R.1    Lund, J.2    Thompson, K.M.3    Jefferis, R.4
  • 14
    • 0021866261 scopus 로고
    • Effector functions of a monoclonal aglycosylated mouse IgG2a: Binding and activation of complement component C1 and interaction with human monocyte Fc receptor
    • PMID:4033665
    • Leatherbarrow RJ, Rademacher TW, Dwek RA, Woof JM, Clark A, Burton DR, et al. Effector functions of a monoclonal aglycosylated mouse IgG2a: binding and activation of complement component C1 and interaction with human monocyte Fc receptor. Mol Immunol 1985; 22:407-15; PMID:4033665; http://dx.doi.org/10.1016/ 0161-5890(85)90125-7.
    • (1985) Mol Immunol , vol.22 , pp. 407-415
    • Leatherbarrow, R.J.1    Rademacher, T.W.2    Dwek, R.A.3    Woof, J.M.4    Clark, A.5    Burton, D.R.6
  • 15
    • 33646070900 scopus 로고    scopus 로고
    • Modulation of therapeutic antibody effector functions by glycosylation engineering: Influence of Golgi enzyme localization domain and co-expression of heterologous beta1,4-N-acetylglucosaminyltransferase III and Golgi alpha-mannosidase II
    • PMID:16435400
    • Ferrara C, Brünker P, Suter T, Moser S, Püntener U, Umaña P. Modulation of therapeutic antibody effector functions by glycosylation engineering: influence of Golgi enzyme localization domain and co-expression of heterologous beta1,4-N-acetylglucosaminyltransferase III and Golgi alpha-mannosidase II. Biotechnol Bioeng 2006; 93:851-61; PMID:16435400; http://dx.doi.org/10.1002/bit.20777.
    • (2006) Biotechnol Bioeng , vol.93 , pp. 851-861
    • Ferrara, C.1    Brünker, P.2    Suter, T.3    Moser, S.4    Püntener, U.5    Umaña, P.6
  • 16
    • 0028830782 scopus 로고
    • Oligosaccharide-protein interactions in IgG can modulate recognition by Fc gamma receptors
    • PMID:7821750
    • Lund J, Takahashi N, Pound JD, Goodall M, Nakagawa H, Jefferis R. Oligosaccharide-protein interactions in IgG can modulate recognition by Fc gamma receptors. FASEB J 1995; 9:115-9; PMID:7821750.
    • (1995) FASEB J , vol.9 , pp. 115-119
    • Lund, J.1    Takahashi, N.2    Pound, J.D.3    Goodall, M.4    Nakagawa, H.5    Jefferis, R.6
  • 17
    • 0035844221 scopus 로고    scopus 로고
    • Recognition of IgG by Fcgamma receptor. The role of Fc glycosylation and the binding of peptide inhibitors
    • PMID:11297533
    • Radaev S, Sun PD. Recognition of IgG by Fcgamma receptor. The role of Fc glycosylation and the binding of peptide inhibitors. J Biol Chem 2001; 276:16478-83; PMID:11297533; http://dx.doi.org/10.1074/jbc.M100351200.
    • (2001) J Biol Chem , vol.276 , pp. 16478-16483
    • Radaev, S.1    Sun, P.D.2
  • 18
    • 0031028909 scopus 로고    scopus 로고
    • Variations in oligosaccharide-protein interactions in immunoglobulin G determine the site-specific glycosylation profiles and modulate the dynamic motion of the Fc oligosaccharides
    • PMID:9063885
    • Wormald MR, Rudd PM, Harvey DJ, Chang SC, Scragg IG, Dwek RA. Variations in oligosaccharide-protein interactions in immunoglobulin G determine the site-specific glycosylation profiles and modulate the dynamic motion of the Fc oligosaccharides. Biochemistry 1997; 36:1370-80; PMID:9063885; http://dx.doi.org/10.1021/bi9621472.
    • (1997) Biochemistry , vol.36 , pp. 1370-1380
    • Wormald, M.R.1    Rudd, P.M.2    Harvey, D.J.3    Chang, S.C.4    Scragg, I.G.5    Dwek, R.A.6
  • 19
    • 0036605631 scopus 로고    scopus 로고
    • A study of immunoglobulin G glycosylation in monoclonal and polyclonal species by electrospray and matrix-assisted laser desorption/ionization mass spectrometry
    • PMID:12018942
    • Saba JA, Kunkel JP, Jan DC, Ens WE, Standing KG, Butler M, et al. A study of immunoglobulin G glycosylation in monoclonal and polyclonal species by electrospray and matrix-assisted laser desorption/ionization mass spectrometry. Anal Biochem 2002; 305:16-31; PMID:12018942; http://dx.doi.org/10.1006/abio. 2002.5651.
    • (2002) Anal Biochem , vol.305 , pp. 16-31
    • Saba, J.A.1    Kunkel, J.P.2    Jan, D.C.3    Ens, W.E.4    Standing, K.G.5    Butler, M.6
  • 20
    • 0022414766 scopus 로고
    • Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG
    • PMID:3927174
    • Parekh RB, Dwek RA, Sutton BJ, Fernandes DL, Leung A, Stanworth D, et al. Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG. Nature 1985; 316:452-7; PMID:3927174; http://dx.doi.org/10.1038/316452a0.
    • (1985) Nature , vol.316 , pp. 452-457
    • Parekh, R.B.1    Dwek, R.A.2    Sutton, B.J.3    Fernandes, D.L.4    Leung, A.5    Stanworth, D.6
  • 21
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • PMID:3896128
    • Kornfeld R, Kornfeld S. Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem 1985; 54:631-64; PMID:3896128; http://dx.doi.org/10.1146/ annurev.bi.54.070185.003215.
    • (1985) Annu Rev Biochem , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 22
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity
    • PMID:11986321
    • Shields RL, Lai J, Keck R, O'Connell LY, Hong K, Meng YG, et al. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J Biol Chem 2002; 277:26733-40; PMID:11986321; http://dx.doi.org/10.1074/jbc.M202069200.
    • (2002) J Biol Chem , vol.277 , pp. 26733-26740
    • Shields, R.L.1    Lai, J.2    Keck, R.3    O'Connell, L.Y.4    Hong, K.5    Meng, Y.G.6
  • 23
    • 4644245701 scopus 로고    scopus 로고
    • Enhancement of the antibody-dependent cellular cytotoxicity of low-fucose IgG1 Is independent of FcgammaRIIIa functional polymorphism
    • PMID:15448014
    • Niwa R, Hatanaka S, Shoji-Hosaka E, Sakurada M, Kobayashi Y, Uehara A, et al. Enhancement of the antibody-dependent cellular cytotoxicity of low-fucose IgG1 Is independent of FcgammaRIIIa functional polymorphism. Clin Cancer Res 2004; 10:6248-55; PMID:15448014; http://dx.doi.org/10.1158/1078-0432.CCR-04- 0850.
    • (2004) Clin Cancer Res , vol.10 , pp. 6248-6255
    • Niwa, R.1    Hatanaka, S.2    Shoji-Hosaka, E.3    Sakurada, M.4    Kobayashi, Y.5    Uehara, A.6
  • 24
    • 16844381436 scopus 로고    scopus 로고
    • Enhanced natural killer cell binding and activation by low-fucose IgG1 antibody results in potent antibody-dependent cellular cytotoxicity induction at lower antigen density
    • PMID:15788684
    • Niwa R, Sakurada M, Kobayashi Y, Uehara A, Matsushima K, Ueda R, et al. Enhanced natural killer cell binding and activation by low-fucose IgG1 antibody results in potent antibody-dependent cellular cytotoxicity induction at lower antigen density. Clin Cancer Res 2005; 11:2327-36; PMID:15788684; http://dx.doi.org/10.1158/1078-0432.CCR-04-2263.
    • (2005) Clin Cancer Res , vol.11 , pp. 2327-2336
    • Niwa, R.1    Sakurada, M.2    Kobayashi, Y.3    Uehara, A.4    Matsushima, K.5    Ueda, R.6
  • 25
    • 28444495153 scopus 로고    scopus 로고
    • IgG subclass-independent improvement of antibody-dependent cellular cytotoxicity by fucose removal from Asn297-linked oligosaccharides
    • PMID:16219319
    • Niwa R, Natsume A, Uehara A, Wakitani M, Iida S, Uchida K, et al. IgG subclass-independent improvement of antibody-dependent cellular cytotoxicity by fucose removal from Asn297-linked oligosaccharides. J Immunol Methods 2005; 306:151-60; PMID:16219319; http://dx.doi.org/10.1016/j.jim.2005.08.009.
    • (2005) J Immunol Methods , vol.306 , pp. 151-160
    • Niwa, R.1    Natsume, A.2    Uehara, A.3    Wakitani, M.4    Iida, S.5    Uchida, K.6
  • 26
    • 10844222497 scopus 로고    scopus 로고
    • Engineering Chinese hamster ovary cells to maximize effector function of produced antibodies using FUT8 siRNA
    • PMID:15515168
    • Mori K, Kuni-Kamochi R, Yamane-Ohnuki N, Wakitani M, Yamano K, Imai H, et al. Engineering Chinese hamster ovary cells to maximize effector function of produced antibodies using FUT8 siRNA. Biotechnol Bioeng 2004; 88:901-8; PMID:15515168; http://dx.doi.org/10.1002/bit.20326.
    • (2004) Biotechnol Bioeng , vol.88 , pp. 901-908
    • Mori, K.1    Kuni-Kamochi, R.2    Yamane-Ohnuki, N.3    Wakitani, M.4    Yamano, K.5    Imai, H.6
  • 27
    • 4644245850 scopus 로고    scopus 로고
    • Establishment of FUT8 knockout Chinese hamster ovary cells: An ideal host cell line for producing completely defucosylated antibodies with enhanced antibody-dependent cellular cytotoxicity
    • PMID:15352059
    • Yamane-Ohnuki N, Kinoshita S, Inoue-Urakubo M, Kusunoki M, Iida S, Nakano R, et al. Establishment of FUT8 knockout Chinese hamster ovary cells: an ideal host cell line for producing completely defucosylated antibodies with enhanced antibody-dependent cellular cytotoxicity. Biotechnol Bioeng 2004; 87:614-22; PMID:15352059; http://dx.doi.org/10.1002/bit.20151.
    • (2004) Biotechnol Bioeng , vol.87 , pp. 614-622
    • Yamane-Ohnuki, N.1    Kinoshita, S.2    Inoue-Urakubo, M.3    Kusunoki, M.4    Iida, S.5    Nakano, R.6
  • 28
    • 34247378189 scopus 로고    scopus 로고
    • Quantitative in vivo comparisons of the Fc gamma receptor-dependent agonist activities of different fucosylation variants of an immunoglobulin G antibody
    • PMID:17466910
    • Scallon B, McCarthy S, Radewonuk J, Cai A, Naso M, Raju TS, et al. Quantitative in vivo comparisons of the Fc gamma receptor-dependent agonist activities of different fucosylation variants of an immunoglobulin G antibody. Int Immunopharmacol 2007; 7:761-72; PMID:17466910; http://dx.doi.org/10.1016/j. intimp.2007.01.014.
    • (2007) Int Immunopharmacol , vol.7 , pp. 761-772
    • Scallon, B.1    McCarthy, S.2    Radewonuk, J.3    Cai, A.4    Naso, M.5    Raju, T.S.6
  • 29
    • 70449711386 scopus 로고    scopus 로고
    • Defucosylated anti-CCR4 monoclonal antibody exerts potent ADCC against primary ATLL cells mediated by autologous human immune cells in NOD/Shi-scid, IL-2R gamma(null) mice in vivo
    • PMID:19748990
    • Ito A, Ishida T, Utsunomiya A, Sato F, Mori F, Yano H, et al. Defucosylated anti-CCR4 monoclonal antibody exerts potent ADCC against primary ATLL cells mediated by autologous human immune cells in NOD/Shi-scid, IL-2R gamma(null) mice in vivo. J Immunol 2009; 183:4782-91; PMID:19748990; http://dx.doi.org/10.4049/jimmunol.0900699.
    • (2009) J Immunol , vol.183 , pp. 4782-4791
    • Ito, A.1    Ishida, T.2    Utsunomiya, A.3    Sato, F.4    Mori, F.5    Yano, H.6
  • 30
    • 34250682223 scopus 로고    scopus 로고
    • Enhanced Fc-dependent cellular cytotoxicity of Fc fusion proteins derived from TNF receptor II and LFA-3 by fucose removal from Asn-linked oligosaccharides
    • PMID:17038352
    • Shoji-Hosaka E, Kobayashi Y, Wakitani M, Uchida K, Niwa R, Nakamura K, et al. Enhanced Fc-dependent cellular cytotoxicity of Fc fusion proteins derived from TNF receptor II and LFA-3 by fucose removal from Asn-linked oligosaccharides. J Biochem 2006; 140:777-83; PMID:17038352; http://dx.doi.org/10.1093/jb/mvj207.
    • (2006) J Biochem , vol.140 , pp. 777-783
    • Shoji-Hosaka, E.1    Kobayashi, Y.2    Wakitani, M.3    Uchida, K.4    Niwa, R.5    Nakamura, K.6
  • 31
    • 33646740982 scopus 로고    scopus 로고
    • Nonfucosylated therapeutic IgG1 antibody can evade the inhibitory effect of serum immunoglobulin G on antibody-dependent cellular cytotoxicity through its high binding to FcgammaRIIIa
    • PMID:16675584
    • Iida S, Misaka H, Inoue M, Shibata M, Nakano R, Yamane-Ohnuki N, et al. Nonfucosylated therapeutic IgG1 antibody can evade the inhibitory effect of serum immunoglobulin G on antibody-dependent cellular cytotoxicity through its high binding to FcgammaRIIIa. Clin Cancer Res 2006; 12:2879-87; PMID:16675584; http://dx.doi.org/10.1158/1078-0432.CCR-05-2619.
    • (2006) Clin Cancer Res , vol.12 , pp. 2879-2887
    • Iida, S.1    Misaka, H.2    Inoue, M.3    Shibata, M.4    Nakano, R.5    Yamane-Ohnuki, N.6
  • 32
    • 28444437100 scopus 로고    scopus 로고
    • Fucose removal from complex-type oligosaccharide enhances the antibody-dependent cellular cytotoxicity of single-geneencoded antibody comprising a single-chain antibody linked the antibody constant region
    • PMID:16236307
    • Natsume A, Wakitani M, Yamane-Ohnuki N, Shoji-Hosaka E, Niwa R, Uchida K, et al. Fucose removal from complex-type oligosaccharide enhances the antibody-dependent cellular cytotoxicity of single-geneencoded antibody comprising a single-chain antibody linked the antibody constant region. J Immunol Methods 2005; 306:93-103; PMID:16236307; http://dx.doi.org/10.1016/j. jim.2005.07.025.
    • (2005) J Immunol Methods , vol.306 , pp. 93-103
    • Natsume, A.1    Wakitani, M.2    Yamane-Ohnuki, N.3    Shoji-Hosaka, E.4    Niwa, R.5    Uchida, K.6
  • 33
    • 70649084992 scopus 로고    scopus 로고
    • The state of the art: Immune-mediated mechanisms of monoclonal antibodies in cancer therapy
    • PMID:19809433
    • Griggs J, Zinkewich-Peotti K. The state of the art: immune-mediated mechanisms of monoclonal antibodies in cancer therapy. Br J Cancer 2009; 101:1807-12; PMID:19809433; http://dx.doi.org/10.1038/ sj.bjc.6605349.
    • (2009) Br J Cancer , vol.101 , pp. 1807-1812
    • Griggs, J.1    Zinkewich-Peotti, K.2
  • 34
    • 73349085919 scopus 로고    scopus 로고
    • Understanding the mechanisms behind trastuzumab therapy for human epidermal growth factor receptor 2-positive breast cancer
    • PMID:19884552
    • Spector NL, Blackwell KL. Understanding the mechanisms behind trastuzumab therapy for human epidermal growth factor receptor 2-positive breast cancer. J Clin Oncol 2009; 27:5838-47; PMID:19884552; http://dx.doi.org/10.1200/JCO.2009. 22.1507.
    • (2009) J Clin Oncol , vol.27 , pp. 5838-5847
    • Spector, N.L.1    Blackwell, K.L.2
  • 35
    • 0037474276 scopus 로고    scopus 로고
    • The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity
    • PMID:12427744
    • Shinkawa T, Nakamura K, Yamane N, Shoji-Hosaka E, Kanda Y, Sakurada M, et al. The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity. J Biol Chem 2003; 278:3466-73; PMID:12427744; http://dx.doi.org/10.1074/jbc.M210665200.
    • (2003) J Biol Chem , vol.278 , pp. 3466-3473
    • Shinkawa, T.1    Nakamura, K.2    Yamane, N.3    Shoji-Hosaka, E.4    Kanda, Y.5    Sakurada, M.6
  • 36
    • 79957790057 scopus 로고    scopus 로고
    • Development of a quantitative, cell-line based assay to measure ADCC activity mediated by therapeutic antibodies
    • PMID:21570725
    • Schnueriger A, Grau R, Sondermann P, Schreitmueller T, Marti S, Zocher M. Development of a quantitative, cell-line based assay to measure ADCC activity mediated by therapeutic antibodies. Mol Immunol 2011; 48:1512-7; PMID:21570725; http://dx.doi.org/10.1016/j.molimm.2011.04.010.
    • (2011) Mol Immunol , vol.48 , pp. 1512-1517
    • Schnueriger, A.1    Grau, R.2    Sondermann, P.3    Schreitmueller, T.4    Marti, S.5    Zocher, M.6
  • 37
    • 33646172632 scopus 로고    scopus 로고
    • The carbohydrate at FcgammaRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms
    • PMID:16330541
    • Ferrara C, Stuart F, Sondermann P, Brünker P, Umaña P. The carbohydrate at FcgammaRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms. J Biol Chem 2006; 281:5032-6; PMID:16330541; http://dx.doi.org/10.1074/jbc.M510171200.
    • (2006) J Biol Chem , vol.281 , pp. 5032-5036
    • Ferrara, C.1    Stuart, F.2    Sondermann, P.3    Brünker, P.4    Umaña, P.5
  • 38
    • 37549036732 scopus 로고    scopus 로고
    • Fcgamma receptors as regulators of immune responses
    • PMID:18064051
    • Nimmerjahn F, Ravetch JV. Fcgamma receptors as regulators of immune responses. Nat Rev Immunol 2008; 8:34-47; PMID:18064051; http://dx.doi.org/10. 1038/nri2206.
    • (2008) Nat Rev Immunol , vol.8 , pp. 34-47
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 39
    • 33845590523 scopus 로고    scopus 로고
    • Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: The high-mannose, hybrid and complex types
    • PMID:17012310
    • Kanda Y, Yamada T, Mori K, Okazaki A, Inoue M, Kitajima-Miyama K, et al. Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: the high-mannose, hybrid and complex types. Glycobiology 2007; 17:104-18; PMID:17012310; http://dx.doi.org/10.1093/glycob/cwl057.
    • (2007) Glycobiology , vol.17 , pp. 104-118
    • Kanda, Y.1    Yamada, T.2    Mori, K.3    Okazaki, A.4    Inoue, M.5    Kitajima-Miyama, K.6
  • 40
    • 33645218704 scopus 로고    scopus 로고
    • Engineered antibody Fc variants with enhanced effector function
    • PMID:16537476
    • Lazar GA, Dang W, Karki S, Vafa O, Peng JS, Hyun L, et al. Engineered antibody Fc variants with enhanced effector function. Proc Natl Acad Sci USA 2006; 103:4005-10; PMID:16537476; http://dx.doi.org/10.1073/pnas.0508123103.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 4005-4010
    • Lazar, G.A.1    Dang, W.2    Karki, S.3    Vafa, O.4    Peng, J.S.5    Hyun, L.6
  • 41
    • 0036464719 scopus 로고    scopus 로고
    • Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcgammaRIIIa gene
    • PMID:11806974
    • Cartron G, Dacheux L, Salles G, Solal-Celigny P, Bardos P, Colombat P, et al. Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcgammaRIIIa gene. Blood 2002; 99:754-8; PMID:11806974; http://dx.doi.org/10.1182/blood.V99.3.754.
    • (2002) Blood , vol.99 , pp. 754-758
    • Cartron, G.1    Dacheux, L.2    Salles, G.3    Solal-Celigny, P.4    Bardos, P.5    Colombat, P.6
  • 42
    • 0642373290 scopus 로고    scopus 로고
    • Two immunoglobulin G fragment C receptor polymorphisms independently predict response to rituximab in patients with follicular lymphoma
    • PMID:12975461
    • Weng WK, Levy R. Two immunoglobulin G fragment C receptor polymorphisms independently predict response to rituximab in patients with follicular lymphoma. J Clin Oncol 2003; 21:3940-7; PMID:12975461; http://dx.doi.org/10. 1200/JCO.2003.05.013.
    • (2003) J Clin Oncol , vol.21 , pp. 3940-3947
    • Weng, W.K.1    Levy, R.2
  • 43
    • 4444372733 scopus 로고    scopus 로고
    • Pilot study of the mechanism of action of preoperative trastuzumab in patients with primary operable breast tumors overexpressing HER2
    • PMID:15355889
    • Gennari R, Menard S, Fagnoni F, Ponchio L, Scelsi M, Tagliabue E, et al. Pilot study of the mechanism of action of preoperative trastuzumab in patients with primary operable breast tumors overexpressing HER2. Clin Cancer Res 2004; 10:5650-5; PMID:15355889; http://dx.doi.org/10.1158/1078-0432.CCR-04-0225.
    • (2004) Clin Cancer Res , vol.10 , pp. 5650-5655
    • Gennari, R.1    Menard, S.2    Fagnoni, F.3    Ponchio, L.4    Scelsi, M.5    Tagliabue, E.6
  • 44
    • 42949157368 scopus 로고    scopus 로고
    • Immunoglobulin G fragment C receptor polymorphisms and clinical efficacy of trastuzumab-based therapy in patients with HER-2/neu-positive metastatic breast cancer
    • PMID:18347005
    • Musolino A, Naldi N, Bortesi B, Pezzuolo D, Capelletti M, Missale G, et al. Immunoglobulin G fragment C receptor polymorphisms and clinical efficacy of trastuzumab-based therapy in patients with HER-2/neu-positive metastatic breast cancer. J Clin Oncol 2008; 26:1789-96; PMID:18347005; http://dx.doi.org/10.1200/ JCO.2007.14.8957.
    • (2008) J Clin Oncol , vol.26 , pp. 1789-1796
    • Musolino, A.1    Naldi, N.2    Bortesi, B.3    Pezzuolo, D.4    Capelletti, M.5    Missale, G.6
  • 45
    • 33947611087 scopus 로고    scopus 로고
    • Glycosylation of therapeutic proteins in different production systems
    • PMID:17391433
    • Werner RG, Kopp K, Schlueter M. Glycosylation of therapeutic proteins in different production systems. Acta Paediatr Suppl 2007; 96:17-22; PMID:17391433; http://dx.doi.org/10.1111/j.1651-2227.2007.00199.x.
    • (2007) Acta Paediatr Suppl , vol.96 , pp. 17-22
    • Werner, R.G.1    Kopp, K.2    Schlueter, M.3
  • 46
    • 2442586731 scopus 로고    scopus 로고
    • Carbohydrate analysis of a chimeric recombinant monoclonal antibody by capillary electrophoresis with laser-induced fluorescence detection
    • PMID:10575965
    • Ma S, Nashabeh W. Carbohydrate analysis of a chimeric recombinant monoclonal antibody by capillary electrophoresis with laser-induced fluorescence detection. Anal Chem 1999; 71:5185-92; PMID:10575965; http://dx.doi.org/10. 1021/ac990376z.
    • (1999) Anal Chem , vol.71 , pp. 5185-5192
    • Ma, S.1    Nashabeh, W.2
  • 47
    • 33746889823 scopus 로고    scopus 로고
    • A high throughput electrochemiluminescent cell-binding assay for therapeutic anti-CD20 antibody selection
    • PMID:16814318
    • Lu Y, Wong WL, Meng YG. A high throughput electrochemiluminescent cell-binding assay for therapeutic anti-CD20 antibody selection. J Immunol Methods 2006; 314:74-9; PMID:16814318; http://dx.doi.org/10.1016/j.jim.2006.05. 011.
    • (2006) J Immunol Methods , vol.314 , pp. 74-79
    • Lu, Y.1    Wong, W.L.2    Meng, Y.G.3
  • 48
    • 0035794194 scopus 로고    scopus 로고
    • High resolution mapping of the binding site on human IgG1 for Fc gamma RI, Fc gamma RII, Fc gamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fcgamma R
    • PMID:11096108
    • Shields RL, Namenuk AK, Hong K, Meng YG, Rae J, Briggs J, et al. High resolution mapping of the binding site on human IgG1 for Fc gamma RI, Fc gamma RII, Fc gamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fcgamma R. J Biol Chem 2001; 276:6591-604; PMID:11096108; http://dx.doi.org/10.1074/jbc.M009483200.
    • (2001) J Biol Chem , vol.276 , pp. 6591-6604
    • Shields, R.L.1    Namenuk, A.K.2    Hong, K.3    Meng, Y.G.4    Rae, J.5    Briggs, J.6
  • 49
    • 0034655265 scopus 로고    scopus 로고
    • Mapping of the C1q binding site on rituxan, a chimeric antibody with a human IgG1 Fc
    • PMID:10754313
    • Idusogie EE, Presta LG, Gazzano-Santoro H, Totpal K, Wong PY, Ultsch M, et al. Mapping of the C1q binding site on rituxan, a chimeric antibody with a human IgG1 Fc. J Immunol 2000; 164:4178-84; PMID:10754313.
    • (2000) J Immunol , vol.164 , pp. 4178-4184
    • Idusogie, E.E.1    Presta, L.G.2    Gazzano-Santoro, H.3    Totpal, K.4    Wong, P.Y.5    Ultsch, M.6


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