메뉴 건너뛰기




Volumn 181, Issue 5, 2008, Pages 3183-3192

Human anti-IgG1 hinge autoantibodies reconstitute the effector functions of proteolytically inactivated IgGs

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; ANTIGEN; AUTOANTIBODY; COMPLEMENT; IMMUNOGLOBULIN F(AB')2 FRAGMENT; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G; IMMUNOGLOBULIN G1 ANTIBODY; IMMUNOGLOBULIN G1 HINGE AUTOANTIBODY; IMMUNOGLOBULIN G3; PROTEINASE; UNCLASSIFIED DRUG; AUTOANTIGEN; PEPTIDE HYDROLASE;

EID: 51549095449     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.181.5.3183     Document Type: Article
Times cited : (39)

References (59)
  • 1
    • 39149138479 scopus 로고    scopus 로고
    • Proteolysis of purified IgGs by human and bacterial enzymes in vitro and the detection of specific proteolytic fragments of endogenous IgG in rheumatoid synovial fluid
    • Ryan, M. H., D. Petrone, J. F. Nemeth, E. Barnathan, L. Bjorck, and R. E. Jordan. 2008. Proteolysis of purified IgGs by human and bacterial enzymes in vitro and the detection of specific proteolytic fragments of endogenous IgG in rheumatoid synovial fluid. Mol. Immunol. 45: 1837-1846.
    • (2008) Mol. Immunol. , vol.45 , pp. 1837-1846
    • Ryan, M.H.1    Petrone, D.2    Nemeth, J.F.3    Barnathan, E.4    Bjorck, L.5    Jordan, R.E.6
  • 2
    • 0037007214 scopus 로고    scopus 로고
    • IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G
    • DOI 10.1093/emboj/21.7.1607
    • Von Pawel-Rammingen, U., B. P. Johansson, and L. Bjorck. 2002. IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G. EMBO J. 21: 1607-1615. (Pubitemid 34614617)
    • (2002) EMBO Journal , vol.21 , Issue.7 , pp. 1607-1615
    • Von Pawel-Rammingen, U.1    Johansson, B.P.2    Bjorck, L.3
  • 4
    • 0036533267 scopus 로고    scopus 로고
    • Selective cleavage of human IgG by the matrix metalloproteinases, matrilysin and stromelysin
    • DOI 10.1016/S0165-2478(01)00333-9, PII S0165247801003339
    • Gearing, A. J., S. J. Thorpe, K. Miller, M. Mangan, P. G. Varley, T. Dudgeon, G. Ward, C. Turner, and R. Thorpe. 2002. Selective cleavage of human IgG by matrix metalloproteinases, matrilysin and stromelysin. Immunol. Lett. 81: 41-48. (Pubitemid 34159039)
    • (2002) Immunology Letters , vol.81 , Issue.1 , pp. 41-48
    • Gearing, A.J.H.1    Thorpe, S.J.2    Miller, K.3    Mangan, M.4    Varley, P.G.5    Dudgeon, T.6    Ward, G.7    Turner, C.8    Thorpe, R.9
  • 8
    • 33747696575 scopus 로고    scopus 로고
    • IdeE, an IgG-endopeptidase of Streptococcus equi ssp. equi
    • DOI 10.1111/j.1574-6968.2006.00404.x
    • Lannergard, J., and B. Guss. 2006. IdeE, an IgG-endopeptidase of Streptococcus equi ssp. equi. FEMS Microbiol. Lett. 262: 230-235. (Pubitemid 44272800)
    • (2006) FEMS Microbiology Letters , vol.262 , Issue.2 , pp. 230-235
    • Lannergard, J.1    Guss, B.2
  • 10
    • 0028940351 scopus 로고
    • Proteolytic fragmentation with high specificity of mouse immunoglobulin G: Mapping of proteolytic cleavage sites in the hinge region
    • Yamaguchi, Y., H. Kim, K. Kato, K. Masuda, I. Shimada, and Y. Arata. 1995. Proteolytic fragmentation with high specificity of mouse immunoglobulin G: mapping of proteolytic cleavage sites in the hinge region. J. Immunol. Methods 181: 259-267.
    • (1995) J. Immunol. Methods , vol.181 , pp. 259-267
    • Yamaguchi, Y.1    Kim, H.2    Kato, K.3    Masuda, K.4    Shimada, I.5    Arata, Y.6
  • 12
    • 10644276295 scopus 로고    scopus 로고
    • Enzymatic characterization of the streptococcal endopeptidase, ides, reveals that it is a cysteine protease with strict specificity for IgG cleavage due to exosite binding
    • DOI 10.1021/bi048284d
    • Vincents, B., U. von Pawel-Rammingen, L. Björck, and M. Abrahamson. 2004. Enzymatic characterization of the streptococcal endopeptidase, IdeS, reveals that it is a cysteine protease with strict specificity for IgG cleavage due to exosite binding. Biochemistry 43: 15540-15549. (Pubitemid 39647479)
    • (2004) Biochemistry , vol.43 , Issue.49 , pp. 15540-15549
    • Vincents, B.1    Von Pawel-Rammingen, U.2    Bjorck, L.3    Abrahamson, M.4
  • 13
    • 0020656366 scopus 로고
    • The IgA1 proteases of pathogenic bacteria
    • Plaut, A. G. 1983. The IgA1 proteases of pathogenic bacteria. Annu. Rev. Microbiol. 37: 603-622.
    • (1983) Annu. Rev. Microbiol. , vol.37 , pp. 603-622
    • Plaut, A.G.1
  • 15
    • 0037180757 scopus 로고    scopus 로고
    • Inflammation and cancer
    • Coussens, L. M., and Z. Werb. 2002. Inflammation and cancer. Nature 420: 860-867.
    • (2002) Nature , vol.420 , pp. 860-867
    • Coussens, L.M.1    Werb, Z.2
  • 16
    • 0037782348 scopus 로고    scopus 로고
    • Neutrophil elastase in human arthrosclerotic plaques: Production by macrophages
    • Dollery, C. M., C. A. Owen, G. K. Sukhova, A. Krettek, S. D. Shapiro, and P. Libby. 2003. Neutrophil elastase in human arthrosclerotic plaques: production by macrophages. Circulation 107: 2829-2836.
    • (2003) Circulation , vol.107 , pp. 2829-2836
    • Dollery, C.M.1    Owen, C.A.2    Sukhova, G.K.3    Krettek, A.4    Shapiro, S.D.5    Libby, P.6
  • 17
    • 0025948793 scopus 로고
    • Elimination from peripheral lymphoid tissues of self-reactive B lymphocytes recognizing membrane-bound antigens
    • Hartley, S. B., J. Crosbie, R. Brink, A. B. Kantor, A. Basten, and C. C. Goodnow. 1991. Elimination from peripheral lymphoid tissues of self-reactive B lymphocytes recognizing membrane-bound antigens. Nature 353: 765-769.
    • (1991) Nature , vol.353 , pp. 765-769
    • Hartley, S.B.1    Crosbie, J.2    Brink, R.3    Kantor, A.B.4    Basten, A.5    Goodnow, C.C.6
  • 18
    • 0027532192 scopus 로고
    • B lymphocytes may escape tolerance by revising their antigen receptors
    • Radic, M. Z., J. Erikson, S. Litwin, and M. Weigert. 1993. B lymphocytes may escape tolerance by revising their antigen receptors. J. Exp. Med. 177: 1165-1173.
    • (1993) J. Exp. Med. , vol.177 , pp. 1165-1173
    • Radic, M.Z.1    Erikson, J.2    Litwin, S.3    Weigert, M.4
  • 19
    • 0029006329 scopus 로고
    • Engagement of the antigen-receptor on immature murine B lymphocytes results in death by apoptosis
    • Norvell, A., L. Mandik, and J. G. Monroe. 1995. Engagement of the antigen-receptor on immature murine B lymphocytes results in death by apoptosis. J. Immunol. 154: 4404-4413.
    • (1995) J. Immunol. , vol.154 , pp. 4404-4413
    • Norvell, A.1    Mandik, L.2    Monroe, J.G.3
  • 20
    • 0041689676 scopus 로고    scopus 로고
    • Predominant autoantibody production by early human B cell precursors
    • DOI 10.1126/science.1086907
    • Wardemann, H., S. Yurasov, A. Schaefer, J. W. Young, E. Meffre, and M. C. Nussenzweig. 2003. Predominant autoantibody production by early human B cell precursors. Science 301: 1374-1377. (Pubitemid 37075812)
    • (2003) Science , vol.301 , Issue.5638 , pp. 1374-1377
    • Wardemann, H.1    Yurasov, S.2    Schaefer, A.3    Young, J.W.4    Meffre, E.5    Nussenzweig, M.C.6
  • 22
    • 0026502690 scopus 로고
    • Monoclonal IgM rheumatoid factors bind IgG at a discontinuous epitope comprised of amino acid loops from heavy-chain constant-region domains 2 and 3
    • Artandi, S. E., K. L. Calame, S. L. Morrison, and V. R. Bonagura. 1992. Monoclonal IgM rheumatoid factors bind IgG at a discontinuous epitope comprised of amino acid loops from heavy-chain constant-region domains 2 and 3. Proc. Natl. Acad. Sci. USA 89: 94-98.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 94-98
    • Artandi, S.E.1    Calame, K.L.2    Morrison, S.L.3    Bonagura, V.R.4
  • 23
    • 0029587683 scopus 로고
    • The immunogenicity of the 7E3 murine monoclonal Fab antibody fragment variable region is dramatically reduced in humans by substitution of human for murine constant regions
    • Knight, D. M., C. Wagner, R. Jordan, M. F. McAleer, R. DeRita, D. N. Fass, B. S. Coller, H. F. Weisman, and J. Ghrayeb. 1995. The immunogenicity of the 7E3 murine monoclonal Fab antibody fragment variable region is dramatically reduced in humans by substitution of human for murine constant regions. Mol. Immunol. 32: 1271-1281.
    • (1995) Mol. Immunol. , vol.32 , pp. 1271-1281
    • Knight, D.M.1    Wagner, C.2    Jordan, R.3    McAleer, M.F.4    DeRita, R.5    Fass, D.N.6    Coller, B.S.7    Weisman, H.F.8    Ghrayeb, J.9
  • 25
    • 0021838045 scopus 로고
    • Anti-Fab antibodies in humans: Predominance of minor immunoglobulin G subclasses in rheumatoid arthritis
    • Persselin, J. E., and R. H. Stevens. 1985. Anti-Fab antibodies in humans: predominance of minor immunoglobulin G subclasses in rheumatoid arthritis. J. Clin. Invest. 76: 723-730.
    • (1985) J. Clin. Invest. , vol.76 , pp. 723-730
    • Persselin, J.E.1    Stevens, R.H.2
  • 27
    • 0021838045 scopus 로고
    • Anti-Fab antibodies in humans: Predominance of minor immunoglobulin G subclasses in rheumatoid arthritis
    • Persselin, J. E., and R. H. Stevens. 1985. Anti-Fab antibodies in humans: predominance of minor immunoglobulin G subclasses in rheumatoid arthritis. J. Clin. Invest. 76: 723-730.
    • (1985) J. Clin. Invest. , vol.76 , pp. 723-730
    • Persselin, J.E.1    Stevens, R.H.2
  • 28
    • 0038428649 scopus 로고    scopus 로고
    • Immunosuppressive anti-immunoglobulin autoantibodies: Specificity, gene structure and function in health and disease
    • Terness, P., D. Navolan, C. Dufter, M. Welschof, and G. Opelz. 2002. Immunosuppressive anti-immunoglobulin autoantibodies: specificity, gene structure and function in health and disease. Cell. Mol. Biol. 48: 271-278.
    • (2002) Cell. Mol. Biol. , vol.48 , pp. 271-278
    • Terness, P.1    Navolan, D.2    Dufter, C.3    Welschof, M.4    Opelz, G.5
  • 31
    • 4444231656 scopus 로고    scopus 로고
    • Comparison of selected analytical techniques for protein sizing, quantitation and molecular weight determination
    • DOI 10.1016/j.jbbm.2004.01.007, PII S0165022X04000107
    • Goetz, H., M. Kuschel, T. Wulff, C. Sauber, C. Miller, S. Fisher, and C. Woodward. 2004. Comparison of selected analytical techniques for protein sizing, quantitation and molecular weight determination. J. Biochem. Biophys. Methods 60: 281-293. (Pubitemid 39179383)
    • (2004) Journal of Biochemical and Biophysical Methods , vol.60 , Issue.3 , pp. 281-293
    • Goetz, H.1    Kuschel, M.2    Wulff, T.3    Sauber, C.4    Miller, C.5    Fisher, S.6    Woodward, C.7
  • 33
    • 33751253486 scopus 로고    scopus 로고
    • Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality
    • 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.
    • (2007) Mol. Immunol. , vol.44 , pp. 1524-1534
    • Scallon, B.J.1    Tam, S.H.2    McCarthy, S.G.3    Cai, A.N.4    Raju, T.S.5
  • 35
    • 0020585579 scopus 로고
    • Characterization of anti-Fab′ antibodies in human sera: Identification of soluble immune complexes that contain hidden anti-KLH and blocking anti-immunoglobulins following immunization with keyhole limpet haemocyanin
    • Birdsall, H. H., and R. D. Rossen. 1983. Characterization of anti-Fab′ antibodies in human sera: identification of soluble immune complexes that contain hidden anti-KLH and blocking anti-immunoglobulins following immunization with keyhole limpet haemocyanin. Clin. Exp. Immunol. 53: 497-504.
    • (1983) Clin. Exp. Immunol. , vol.53 , pp. 497-504
    • Birdsall, H.H.1    Rossen, R.D.2
  • 37
    • 1842474888 scopus 로고    scopus 로고
    • Tissue factor-factor VIIa-specific up-regulation of IL-8 expression in MDA-MB-231 cells is mediated by PAR-2 and results in increased cell migration
    • Hjortoe, G. M., L. C. Petersen, T. Albrektsen, B. B. Sorensen, P. L. Norby, S. K. Mandal, U. R. Pendurthi, and L. V. Rao. 2004. Tissue factor-factor VIIa-specific up-regulation of IL-8 expression in MDA-MB-231 cells is mediated by PAR-2 and results in increased cell migration. Blood 103: 3029-3037.
    • (2004) Blood , vol.103 , pp. 3029-3037
    • Hjortoe, G.M.1    Petersen, L.C.2    Albrektsen, T.3    Sorensen, B.B.4    Norby, P.L.5    Mandal, S.K.6    Pendurthi, U.R.7    Rao, L.V.8
  • 40
    • 0028012535 scopus 로고
    • Isotypes and IgG subclasses of anti-Fab antibodies in human immunodeficiency virus infected hemophilia patients
    • Susal, C., H. H. Oberg, V. Daniel, C. Dorr, P. Terness, A. Huth-Kuhne, R. Zimmermann, and G. Opelz. 1994. Isotypes and IgG subclasses of anti-Fab antibodies in human immunodeficiency virus-infected hemophilia patients. Vox Sang. 66: 37-45. (Pubitemid 24017155)
    • (1994) Vox Sanguinis , vol.66 , Issue.1 , pp. 37-45
    • Susal, C.1    Oberg, H.-H.2    Daniel, V.3    Dorr, C.4    Terness, P.5    Huth-Kuhne, A.6    Zimmermann, R.7    Opelz, G.8
  • 41
    • 0018824004 scopus 로고
    • Kinetics of the different susceptibilities of the four human immunoglobulin G subclasses to proteolysis by human lysosomal elastase
    • Baici, A., M. Knopfel, K. Fehr, F. Skvaril, and A. Boni. 1980. Kinetics of the different susceptibilities of the four human immunoglobulin G subclasses to proteolysis by human lysosomal elastase. Scand. J. Immunol. 12: 41-50. (Pubitemid 10071938)
    • (1980) Scandinavian Journal of Immunology , vol.12 , Issue.1 , pp. 41-50
    • Baici, A.1    Knoepfel, M.2    Fehr, K.3
  • 42
    • 13544250803 scopus 로고    scopus 로고
    • Immune thrombocytopenia caused by glycoprotein IIb/IIIa inhibitors
    • Aster, R. H. 2005. Immune thrombocytopenia caused by glycoprotein IIb/IIIa inhibitors. Chest 127: 53S-59S.
    • (2005) Chest , vol.127
    • Aster, R.H.1
  • 44
    • 37549036732 scopus 로고    scopus 로고
    • Fcγ receptors as regulators of immune responses
    • Nimmerjahn, F., and J. V. Ravetch. 2008. Fcγ receptors as regulators of immune responses. Nat. Rev. Immunol. 8: 34-47.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 34-47
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 46
    • 36849001338 scopus 로고    scopus 로고
    • Isotype selection in antibody engineering
    • Salfeld, J. G. 2007. Isotype selection in antibody engineering. Nat. Biotechnol. 25: 1369-1372.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 1369-1372
    • Salfeld, J.G.1
  • 47
    • 34748865088 scopus 로고    scopus 로고
    • Antibody therapeutics: Isotype and glycoform selection
    • DOI 10.1517/14712598.7.9.1401
    • Jefferis, R. 2007. Antibody therapeutics: isotype and glycoform selection. Expert Opin. Biol. Ther. 7: 1401-1413. (Pubitemid 47475656)
    • (2007) Expert Opinion on Biological Therapy , vol.7 , Issue.9 , pp. 1401-1413
    • Jefferis, R.1
  • 48
    • 0032810008 scopus 로고    scopus 로고
    • Recombinant human IgG molecules lacking Fcγ receptor I binding and monocyte triggering activities
    • Armour, K. L., M. R. Clark, A. G. Hadley, and L. M. Williamson. 1999. Recombinant human IgG molecules lacking Fcγ receptor I binding and monocyte triggering activities. Eur. J. Immunol. 29: 2613-2624.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 2613-2624
    • Armour, K.L.1    Clark, M.R.2    Hadley, A.G.3    Williamson, L.M.4
  • 49
    • 0142226958 scopus 로고    scopus 로고
    • Differential binding to human FcγRIIa and FcγRIIb receptors by human IgG wildtype and mutant antibodies
    • Armour, K. L., J. G. van de Winkel, L. M. Williamson, and M. R. Clark. 2003. Differential binding to human FcγRIIa and FcγRIIb receptors by human IgG wildtype and mutant antibodies. Mol. Immunol. 40: 585-593.
    • (2003) Mol. Immunol. , vol.40 , pp. 585-593
    • Armour, K.L.1    Van De Winkel, J.G.2    Williamson, L.M.3    Clark, M.R.4
  • 51
    • 0025762394 scopus 로고
    • The binding affinity of human IgG for its high affinity Fc receptor is determined by multiple amino acids in the CH2 domain and is modulated by the hinge region
    • Canfield, S. M., and S. L. Morrison. 1991. The binding affinity of human IgG for its high affinity Fc receptor is determined by multiple amino acids in the CH2 domain and is modulated by the hinge region. J. Exp. Med. 173: 1483-1491.
    • (1991) J. Exp. Med. , vol.173 , pp. 1483-1491
    • Canfield, S.M.1    Morrison, S.L.2
  • 52
    • 0028970836 scopus 로고
    • The N-terminal end of the CH2 domain of chimeric human IgG1 anti-HLA-DR is necessary for C1q, Fc γ RI and Fc γ RIII binding
    • Morgan, A., N. D. Jones, A. M. Nesbitt, L. Chaplin, M. W. Bodmer, and J. S. Emtage. 1995. The N-terminal end of the CH2 domain of chimeric human IgG1 anti-HLA-DR is necessary for C1q, Fc γ RI and Fc γ RIII binding. Immunology 86: 319-324.
    • (1995) Immunology , vol.86 , pp. 319-324
    • Morgan, A.1    Jones, N.D.2    Nesbitt, A.M.3    Chaplin, L.4    Bodmer, M.W.5    Emtage, J.S.6
  • 53
    • 0031014785 scopus 로고    scopus 로고
    • IgG effector mechanisms
    • Clark, M. R. 1997. IgG effector mechanisms. Chem. Immunol. 65: 88-110.
    • (1997) Chem. Immunol. , vol.65 , pp. 88-110
    • Clark, M.R.1
  • 57
    • 0023739306 scopus 로고
    • Enhanced cytotoxicity against colon carcinoma by combinations of noncompeting monoclonal antibodies to the 17-1A antigen
    • Fogler, W. E., M. R. Klinger, K. G. Abraham, H. G. Gottlinger, G. Riethmuller, and P. E. Daddona. 1988. Enhanced cytotoxicity against colon carcinoma by combinations of noncompeting monoclonal antibodies to the 17-1A antigen. Cancer Res. 48: 6303-6308.
    • (1988) Cancer Res. , vol.48 , pp. 6303-6308
    • Fogler, W.E.1    Klinger, M.R.2    Abraham, K.G.3    Gottlinger, H.G.4    Riethmuller, G.5    Daddona, P.E.6
  • 58
    • 30344434022 scopus 로고    scopus 로고
    • High concentrations of therapeutic IgG1 antibodies are needed to compensate for inhibition of antibody-dependent cellular cytotoxicity by excess endogenous immunoglobulin G
    • DOI 10.1016/j.molimm.2005.07.010, PII S0161589005002865
    • Preithner, S., S. Elm, S. Lippold, M. Locher, A. Wolf, A. J. da Silva, P. A. Baeuerle, and N. S. Prang. 2006. High concentrations of therapeutic IgG1 antibodies are needed to compensate for inhibition of antibody-dependent cellular cytotoxicity by excess endogenous immunoglobulin G. Mol. Immunol. 43: 1183-1193. (Pubitemid 43063171)
    • (2006) Molecular Immunology , vol.43 , Issue.8 , pp. 1183-1193
    • Preithner, S.1    Elm, S.2    Lippold, S.3    Locher, M.4    Wolf, A.5    Silva, A.J.D.6    Baeuerle, P.A.7    Prang, N.S.8
  • 59


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.