메뉴 건너뛰기




Volumn 192, Issue 2, 2014, Pages 581-588

Lack of galactosylation enhances the pathogenic activity of IgG1 but not IgG2a anti-erythrocyte autoantibodies

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENT COMPONENT C3; ERYTHROCYTE ANTIBODY; FC RECEPTOR; IMMUNOGLOBULIN G1 ANTIBODY; IMMUNOGLOBULIN G2A ANTIBODY; MONOCLONAL ANTIBODY;

EID: 84892696203     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1302488     Document Type: Article
Times cited : (21)

References (53)
  • 2
    • 0028169439 scopus 로고
    • Effect of altered CH2-associated carbohydrate structure on the functional properties and in vivo fate of chimeric mousehuman immunoglobulin G1
    • Wright, A., and S. L. Morrison. 1994. Effect of altered CH2-associated carbohydrate structure on the functional properties and in vivo fate of chimeric mousehuman immunoglobulin G1. J. Exp. Med. 180: 1087-1096.
    • (1994) J. Exp. Med. , vol.180 , pp. 1087-1096
    • Wright, A.1    Morrison, S.L.2
  • 3
  • 4
    • 0022414766 scopus 로고
    • Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG
    • DOI 10.1038/316452a0
    • Parekh, R. B., R. A. Dwek, B. J. Sutton, D. L. Fernandes, A. Leung, D. Stanworth, T. W. Rademacher, T. Mizuochi, T. Taniguchi, K. Matsuta, et al. 1985. Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG. Nature 316: 452-457. (Pubitemid 16238456)
    • (1985) Nature , vol.316 , Issue.6027 , pp. 452-457
    • Parekh, R.B.1    Dwek, R.A.2    Sutton, B.J.3
  • 5
    • 0025038766 scopus 로고
    • Structural changes in the oligosaccharide chains of IgG in autoimmune MRL/Mp-lpr/lpr mice
    • Mizuochi, T., J. Hamako, M. Nose, and K. Titani. 1990. Structural changes in the oligosaccharide chains of IgG in autoimmune MRL/Mp-lpr/lpr mice. J. Immunol. 145: 1794-1798. (Pubitemid 20336746)
    • (1990) Journal of Immunology , vol.145 , Issue.6 , pp. 1794-1798
    • Mizuochi, T.1    Hamako, J.2    Nose, M.3    Titani, K.4
  • 6
    • 0024642881 scopus 로고
    • A comparative analysis of disease-associated changes in the galactosylation of serum IgG
    • Parekh, R., D. Isenberg, G. Rook, I. Roitt, R. Dwek, and T. Rademacher. 1989. A comparative analysis of disease-associated changes in the galactosylation of serum IgG. J. Autoimmun. 2: 101-114.
    • (1989) J. Autoimmun. , vol.2 , pp. 101-114
    • Parekh, R.1    Isenberg, D.2    Rook, G.3    Roitt, I.4    Dwek, R.5    Rademacher, T.6
  • 7
    • 0025319470 scopus 로고
    • Agalactosyl IgG in inflammatory bowel disease: Correlation with C-reactive protein
    • Dubé, R., G. A. Rook, J. Steele, R. Brealey, R. Dwek, T. Rademacher, and J. Lennard-Jones. 1990. Agalactosyl IgG in inflammatory bowel disease: correlation with C-reactive protein. Gut 31: 431-434. (Pubitemid 20129442)
    • (1990) Gut , vol.31 , Issue.4 , pp. 431-434
    • Dube, R.1    Rook, G.A.W.2    Steele, J.3    Brealy, R.4    Dwek, R.5    Rademacher, T.6    Lennard-Jones, J.7
  • 9
    • 33646093725 scopus 로고    scopus 로고
    • Differential glycosylation of polyclonal IgG, IgG-Fc and IgGFab isolated from the sera of patients with ANCA-associated systemic vasculitis
    • Holland, M., H. Yagi, N. Takahashi, K. Kato, C. O. Savage, D. M. Goodall, and R. Jefferis. 2006. Differential glycosylation of polyclonal IgG, IgG-Fc and IgGFab isolated from the sera of patients with ANCA-associated systemic vasculitis. Biochim. Biophys. Acta 1760: 669-677.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 669-677
    • Holland, M.1    Yagi, H.2    Takahashi, N.3    Kato, K.4    Savage, C.O.5    Goodall, D.M.6    Jefferis, R.7
  • 11
  • 16
    • 84885204309 scopus 로고    scopus 로고
    • Association between galactosylation of immunoglobulin G and improvement of rheumatoid arthritis during pregnancy is independent of sialylation
    • Bondt, A., M. H. Selman, A. M. Deelder, J. M. Hazes, S. P. Willemsen, M. Wuhrer, and R. J. Dolhain. 2013. Association between galactosylation of immunoglobulin G and improvement of rheumatoid arthritis during pregnancy is independent of sialylation. J. Proteome Res. 12: 4522-4531.
    • (2013) J. Proteome Res. , vol.12 , pp. 4522-4531
    • Bondt, A.1    Selman, M.H.2    Deelder, A.M.3    Hazes, J.M.4    Willemsen, S.P.5    Wuhrer, M.6    Dolhain, R.J.7
  • 18
    • 0028971204 scopus 로고
    • The biological activity of human moncolonal IgG anti-D is reduced by beta-galactosidase treatment
    • Kumpel, B. M., Y. Wang, H. L. Griffiths, A. G. Hadley, and G. A. Rook. 1995. The biological activity of human monoclonal IgG anti-D is reduced by betagalactosidase treatment. Hum. Antibodies Hybridomas 6: 82-88. (Pubitemid 3008102)
    • (1995) Human Antibodies and Hybridomas , vol.6 , Issue.3 , pp. 82-88
    • Kumpel, B.M.1    Wang Yan2    Griffiths, H.L.3    Hadley, A.G.4    Rook, G.A.5
  • 19
    • 0029558207 scopus 로고
    • The effect of the removal of sialic acid, galactose and total carbohydrate on the functional activity of Campath-1H
    • DOI 10.1016/0161-5890(95)00118-2
    • Boyd, P. N., A. C. Lines, and A. K. Patel. 1995. The effect of the removal of sialic acid, galactose and total carbohydrate on the functional activity of Campath-1H. Mol. Immunol. 32: 1311-1318. (Pubitemid 26064897)
    • (1995) Molecular Immunology , vol.32 , Issue.17-18 , pp. 1311-1318
    • Boyd, P.N.1    Lines, A.C.2    Patel, A.K.3
  • 20
    • 0024993699 scopus 로고
    • Glycosylation of IgG, immune complexes and IgG subclasses in the MRl-lpr/lpr mouse model of rheumatoid arthritis
    • Bond, A., A. Cooke, and F. C. Hay. 1990. Glycosylation of IgG, immune complexes and IgG subclasses in the MRL-lpr/lpr mouse model of rheumatoid arthritis. Eur. J. Immunol. 20: 2229-2233. (Pubitemid 20368207)
    • (1990) European Journal of Immunology , vol.20 , Issue.10 , pp. 2229-2233
    • Bond, A.1    Cooke, A.2    Hay, F.C.3
  • 21
    • 0035720282 scopus 로고    scopus 로고
    • Abnormal IgG galactosylation in MRL-lpr/lpr mice: Pathogenic role in the development of arthritis
    • DOI 10.1046/j.1440-1827.2001.01306.x
    • Kuroda, Y., M. Nakata, S. Hirose, T. Shirai, M. Iwamoto, S. Izui, N. Kojima, and T. Mizuochi. 2001. Abnormal IgG galactosylation in MRL-lpr/lpr mice: pathogenic role in the development of arthritis. Pathol. Int. 51: 909-915. (Pubitemid 34175517)
    • (2001) Pathology International , vol.51 , Issue.12 , pp. 909-915
    • Kuroda, Y.1    Nakata, M.2    Hirose, S.3    Shirai, T.4    Iwamoto, M.5    Izui, S.6    Kojima, N.7    Mizuochi, T.8
  • 22
    • 0028962403 scopus 로고
    • Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein
    • Malhotra, R., M.R. Wormald, P.M. Rudd, P. B. Fischer, R. A. Dwek, and R. B. Sim. 1995. Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein. Nat. Med. 1: 237-243.
    • (1995) Nat. Med. , vol.1 , pp. 237-243
    • Malhotra, R.1    Wormald, M.R.2    Rudd, P.M.3    Fischer, P.B.4    Dwek, R.A.5    Sim, R.B.6
  • 24
    • 0030458140 scopus 로고    scopus 로고
    • Immunoglobulin G-mediated inflammatory responses develop normally in complement-deficient mice
    • DOI 10.1084/jem.184.6.2385
    • Sylvestre, D. L., R. Clynes, M. Ma, H. Warren, M. C. Carroll, and J. V. Ravetch. 1996. Immunoglobulin G-mediated inflammatory responses develop normally in complement-deficient mice. J. Exp. Med. 184: 2385-2392. (Pubitemid 27023737)
    • (1996) Journal of Experimental Medicine , vol.184 , Issue.6 , pp. 2385-2392
    • Sylvestre, D.1    Clynes, R.2    Ma, M.3    Warren, H.4    Carroll, M.C.5    Ravetch, J.V.6
  • 25
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • DOI 10.1126/science.1129594
    • Kaneko, Y., F. Nimmerjahn, and J. V. Ravetch. 2006. Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science 313: 670-673. (Pubitemid 44201145)
    • (2006) Science , vol.313 , Issue.5787 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 26
    • 84866104409 scopus 로고    scopus 로고
    • The role of sialic acid as a modulator of the anti-inflammatory activity of IgG
    • Böhm, S., I. Schwab, A. Lux, and F. Nimmerjahn. 2012. The role of sialic acid as a modulator of the anti-inflammatory activity of IgG. Semin. Immunopathol. 34: 443-453.
    • (2012) Semin. Immunopathol. , vol.34 , pp. 443-453
    • Böhm, S.1    Schwab, I.2    Lux, A.3    Nimmerjahn, F.4
  • 27
    • 33751253486 scopus 로고    scopus 로고
    • Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality
    • DOI 10.1016/j.molimm.2006.09.005, PII S0161589006005839
    • Scallon, B. J., S. H. Tam, S. G. McCarthy, A. N. Cai, and T. S. Raju. 2007. Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality. Mol. Immunol. 44: 1524-1534. (Pubitemid 44792756)
    • (2007) Molecular Immunology , vol.44 , Issue.7 , pp. 1524-1534
    • Scallon, B.J.1    Tam, S.H.2    McCarthy, S.G.3    Cai, A.N.4    Raju, T.S.5
  • 29
    • 79959555556 scopus 로고    scopus 로고
    • Enrichment of sialylated IgG by lectin fractionation does not enhance the efficacy of immunoglobulin G in a murine model of immune thrombocytopenia
    • Guhr, T., J. Bloem, N. I. Derksen, M. Wuhrer, A. H. Koenderman, R. C. Aalberse, and T. Rispens. 2011. Enrichment of sialylated IgG by lectin fractionation does not enhance the efficacy of immunoglobulin G in a murine model of immune thrombocytopenia. PLoS ONE 6: e21246.
    • (2011) PLoS ONE , vol.6
    • Guhr, T.1    Bloem, J.2    Derksen, N.I.3    Wuhrer, M.4    Koenderman, A.H.5    Aalberse, R.C.6    Rispens, T.7
  • 30
    • 84865030107 scopus 로고    scopus 로고
    • Sialylation-independent mechanism involved in the amelioration of murine immune thrombocytopenia using intravenous gammaglobulin
    • Leontyev, D., Y. Katsman, X. Z. Ma, S. Miescher, F. Käsermann, and D. R. Branch. 2012. Sialylation-independent mechanism involved in the amelioration of murine immune thrombocytopenia using intravenous gammaglobulin. Transfusion 52: 1799-1805.
    • (2012) Transfusion , vol.52 , pp. 1799-1805
    • Leontyev, D.1    Katsman, Y.2    Ma, X.Z.3    Miescher, S.4    Käsermann, F.5    Branch, D.R.6
  • 32
    • 0025676294 scopus 로고
    • Monoclonal anti-erythrocyte autoantibodies derived from NZB mice cause autoimmune hemolytic anemia by two distinct pathogenic mechanisms
    • Shibata, T., T. Berney, L. Reininger, Y. Chicheportiche, S. Ozaki, T. Shirai, and S. Izui. 1990. Monoclonal anti-erythrocyte autoantibodies derived from NZB mice cause autoimmune hemolytic anemia by two distinct pathogenic mechanisms. Int. Immunol. 2: 1133-1141.
    • (1990) Int. Immunol. , vol.2 , pp. 1133-1141
    • Shibata, T.1    Berney, T.2    Reininger, L.3    Chicheportiche, Y.4    Ozaki, S.5    Shirai, T.6    Izui, S.7
  • 36
    • 40749113672 scopus 로고    scopus 로고
    • Differential contribution of three activating IgG Fc receptors (FcgammaRI, FcgammaRIII, and FcgammaRIV) to IgG2a-and IgG2b-induced autoimmune hemolytic anemia in mice
    • Baudino, L., F. Nimmerjahn, S. Azeredo da Silveira, E. Martinez-Soria, T. Saito, M. Carroll, J. V. Ravetch, J. S. Verbeek, and S. Izui. 2008. Differential contribution of three activating IgG Fc receptors (FcgammaRI, FcgammaRIII, and FcgammaRIV) to IgG2a-and IgG2b-induced autoimmune hemolytic anemia in mice. J. Immunol. 180: 1948-1953.
    • (2008) J. Immunol. , vol.180 , pp. 1948-1953
    • Baudino, L.1    Nimmerjahn, F.2    Azeredo Da-Silveira, S.3    Martinez-Soria, E.4    Saito, T.5    Carroll, M.6    Ravetch, J.V.7    Verbeek, J.S.8    Izui, S.9
  • 37
    • 0032217049 scopus 로고    scopus 로고
    • FcγRIII (CD16)-deficient mice show IgG isotype-dependent protection to experimental autoimmune hemolytic anemia
    • Meyer, D., C. Schiller, J. Westermann, S. Izui, W. L. W. Hazenbos, J. S. Verbeek, R. E. Schmidt, and J. E. Gessner. 1998. FcgammaRIII (CD16)-deficient mice show IgG isotype-dependent protection to experimental autoimmune hemolytic anemia. Blood 92: 3997-4002. (Pubitemid 28544311)
    • (1998) Blood , vol.92 , Issue.11 , pp. 3997-4002
    • Meyer, D.1    Schiller, G.2    Westermann, J.3    Izui, S.4    Hazenbos, W.L.W.5    Verbeek, J.S.6    Schmidt, R.E.7    Gessner, J.E.8
  • 39
    • 0029558338 scopus 로고
    • Studies of group B streptococcal infection in mice deficient in complement component C3 or C4 demonstrate an essential role for complement in both innate and acquired immunity
    • DOI 10.1073/pnas.92.25.11490
    • Wessels, M. R., P. Butko, M. Ma, H. B. Warren, A. L. Lage, and M. C. Carroll. 1995. Studies of group B streptococcal infection in mice deficient in complement component C3 or C4 demonstrate an essential role for complement in both innate and acquired immunity. Proc. Natl. Acad. Sci. USA 92: 11490-11494. (Pubitemid 26014139)
    • (1995) Proceedings of the National Academy of Sciences of the United States of America , vol.92 , Issue.25 , pp. 11490-11494
    • Wessels, M.R.1    Butko, P.2    Ma, M.3    Warren, H.B.4    Lage, A.L.5    Carroll, M.C.6
  • 42
    • 39449136167 scopus 로고    scopus 로고
    • Comprehensive approach to structural and functional glycomics based on chemoselective glycoblotting and sequential tag conversion
    • DOI 10.1021/ac702124d
    • Furukawa, J.-I., Y. Shinohara, H. Kuramoto, Y. Miura, H. Shimaoka, M. Kurogochi, M. Nakano, and S.-I. Nishimura. 2008. Comprehensive approach to structural and functional glycomics based on chemoselective glycoblotting and sequential tag conversion. Anal. Chem. 80: 1094-1101. (Pubitemid 351272343)
    • (2008) Analytical Chemistry , vol.80 , Issue.4 , pp. 1094-1101
    • Furukawa, J.-I.1    Shinohara, Y.2    Kuramoto, H.3    Miura, Y.4    Shimaoka, H.5    Kurogochi, M.6    Nakano, M.7    Nishimura, S.-I.8
  • 43
  • 44
    • 34250313689 scopus 로고    scopus 로고
    • Rapid and simple solid-phase esterification of sialic acid residues for quantitative glycomics by mass spectrometry
    • DOI 10.1002/chem.200601872
    • Miura, Y., Y. Shinohara, J. Furukawa, N. Nagahori, and S. Nishimura. 2007. Rapid and simple solid-phase esterification of sialic acid residues for quantitative glycomics by mass spectrometry. Chemistry 13: 4797-4804. (Pubitemid 46910621)
    • (2007) Chemistry - A European Journal , vol.13 , Issue.17 , pp. 4797-4804
    • Miura, Y.1    Shinohara, Y.2    Furukawa, J.-I.3    Nagahori, N.4    Nishimura, S.-I.5
  • 47
    • 0025289675 scopus 로고
    • Variable region sequences of pathogenic anti-mouse red blood cell autoantibodies from autoimmune NZB mice
    • DOI 10.1002/eji.1830200410
    • Reininger, L., T. Shibata, S. Ozaki, T. Shirai, J.-C. Jaton, and S. Izui. 1990. Variable region sequences of pathogenic anti-mouse red blood cell autoantibodies from autoimmune NZB mice. Eur. J. Immunol. 20: 771-777. (Pubitemid 20167031)
    • (1990) European Journal of Immunology , vol.20 , Issue.4 , pp. 771-777
    • Reininger, L.1    Shibata, T.2    Ozaki, S.3    Shirai, T.4    Jaton, J.-C.5    Izui, S.6
  • 49
    • 0030470557 scopus 로고    scopus 로고
    • Multiple interactions of IgG with its core oligosaccharide can modulate recognition by complement and human fcγ receptor I and influence the synthesis of its oligosaccharide chains
    • Lund, J., N. Takahashi, J. D. Pound, M. Goodall, and R. Jefferis. 1996. Multiple interactions of IgG with its core oligosaccharide can modulate recognition by complement and human Fc g receptor I and influence the synthesis of its oligosaccharide chains. J. Immunol. 157: 4963-4969. (Pubitemid 126449574)
    • (1996) Journal of Immunology , vol.157 , Issue.11 , pp. 4963-4969
    • Lund, J.1    Takahashi, N.2    Pound, J.D.3    Goodall, M.4    Jefferis, R.5
  • 52
    • 0028672732 scopus 로고
    • Molecular basis of Fc receptor function
    • Hulett, M. D., and P. M. Hogarth. 1994. Molecular basis of Fc receptor function. Adv. Immunol. 57: 1-127.
    • (1994) Adv. Immunol. , vol.57 , pp. 1-127
    • Hulett, M.D.1    Hogarth, P.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.