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Research Article

Regulation of Antibody Production Mediated by Fcγ Receptors, IgG Binding Factors, and IgG Fc-Binding Autoantibodies

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Pages 191-225 | Published online: 26 Sep 2008

References

  • Möller G. Antibody mediated suppression of the immune response is determinant specific. Eur. J. Immunol. 1985; 15: 409
  • Zalcberg I., Silveira A. V., Möller G. Regulation of the antibody response to sheep erythrocytes by monoclonal IgG antibodies. Eur. J. Immunol. 1987; 17: 1343
  • Uhr J. W., Möller G. Regulatory effect of antibody on the immune response. Adv. Immunol. 1968; 8: 81
  • Voisin G. A. Role of antibody classes in the regulatory facilitation reaction. Immunol. Rev. 1980; 49: 3
  • Morgan E. L., Weigle W. O. Biological activities residing in the Fc region of immunoglobulin. Adv. Immunol. 1987; 40: 61
  • Jerne N. K. Idiotypic networks and other preconceived ideas. Immunol. Rev. 1984; 79: 5
  • Fridman W. H., Daeron M., Amigorena S., Rabourdin-Combe C., Neauport-Sautes C. Bases for an isotypic network. Mol. Immunol. 1986; 23: 1141
  • Brüggemann M., Rajewsky K. Regulation of the antibody response against hapten-coupled erythrocytes by monoclonal anti-hapten antibodies of various isotypes. Cell. Immunol. 1982; 71: 165
  • Heyman B., Wigzell H. Immunoregulation by monoclonal sheep erythrocyte specific IgG-antibodies: suppression is correlated to level of antigen binding and not to isotype. J. Immunol. 1984; 132: 1136
  • St. Sinclair N. K. C. Regulation of the immune response. I. Reduction in ability to inhibit longlasting IgG immunological priming after removal of the Fc fragment. J. Exp. Med. 1969; 129: 1183
  • Heyman B., Nose M., Weigle W. O. Carbohydrate chains on IgG2b: a requirement for efficient feedback immunosuppression. J. Immunol. 1985; 134: 4018
  • Feinstein A., Rowe A. J. Molecular mechanism of formation of an antigen-antibody complex. Nature 1965; 205: 147
  • Valentine R. C., Green M. M. Electron microscopy of and antibody-hapten complex. J. Mol. Biol 1997; 27: 615
  • Metzger H. Effect of antigen binding on the properties of antibody. Adv. Immunol. 1974; 18: 169
  • Huber R., Deisenhofer J., Colman P. M., Matsushima M., Palm W. Crystallographic structure studies of an IgG molecule and an Fc fragment. Nature 1976; 264: 415
  • Huber R., Deisenhofer J., Colman P. M., Matsushima M., Palm W. X-ray diffraction analysis of immunoglobulin structure. Das Immunsystem, F. Melchers, K. Rajewsky. Springer-Verlag, Berlin 1976
  • Schlessinger J., Steiberg I. Z., Givol D., Hochman J., Pecht I. Antigen-induced conformational changes in antibodies and in their Fab fragments studied by circular polarisation of fluorescence. Proc. Natl. Acad. Sci. U.S.A. 1975; 72: 2775
  • Pecht I. Recognition and allostery in the mechanism of antibody action. Das Immunsystem, F. Melchers, K. Rajewsky. Springer-Verlag, Berlin 1976; 41
  • Zavodszky P., Jaton J. C., Venyaminov Yu. S., Medgyesi G. A. Increase of conformational stability of two homogenous rabbit immunoglobulin G after hapten binding. Mol. Immunol. 1981; 18: 39
  • Willan K. J., Golding B., Givol D., Dweck R. A. Specific spin labeling of the Fc region of immunoglobulins. FEBS Lett. 1977; 80: 133
  • Jaton J. C., Wright J. K., Schmidt-Kessen A., Engel J. Interactions of monovalent and multivalent oligosaccharide tigands with homogenous anti-polysaccharide antibody and its possible effects on the conformation of the IgG molecule. Immunology 1978, J. Gergely, G. A. Medgyesi, S. R. Hollan. Akademiai Kiado, Budapest 1978; 277
  • Metzger H. The effect of antigen on antibodies: recent studies. Contemp. Top. Mol. Immunol. 1978; 1: 119
  • Jaton J. C., Huser H., Braun D. G., Givol D., Pecht I., Schlessinger J. Conformational changes induced in homogenous anti-Type III pneumococcal antibody by oligosaccharides in increasing size. Biochemistry 1975; 14: 5312
  • Jaton J. C., Huser H., Reisen W. F., Schlessinger J., Givol D. The binding of complement by complexes formed between a rabbit antibody and oligosaccharides of increasing size. J. Immunol. 1976; 116: 1363
  • Gergely J., Medgyesi G. A., Füst G., Rajnavölgyi E. Constitution of immune complexes and their interaction with the complement system. Immunology 1978, J. Gergely, G. A. Medgyesi, R. S. Hollan. Akademiai Kiado, Budapest 1978; 293
  • Medgyesi G. A., Füst G., Gergely J., Jaton J. C. Activation of the classical complement pathway by homogenous anti-SIII antibody bound to bivalent or trivalent oligosaccharide antigens. Mol. Immunol. 1979; 16: 949
  • Pecht I., Ehrenberg B., Calef E., Arnon R. Conformational changes and complement activation induced upon antigen binding to antibodies. Biochem. Biophys. Res. Comm. 1977; 74: 1302
  • Metzger H. General aspects of antibody structure and function. Fc Receptors and the Action of Antibodies, H. Metzger. Telford Press, Caldwell, NJ 1990; 7
  • Metzger H. Antibodies as effector molecules. Harvey Lect. Ser. 1986; 80: 40
  • Sheriff S., Silverton E. W., Padlan E. A., Cohen G. H., Smith-Gill S. J., Finzel B. C., Davis D. R. Three-dimensional structure of an antibody-antigen complex. Proc. Natl. Acad. Sci. U.S.A. 1987; 84: 8075
  • Fischmann T., Souchon H., Riottot M. M., Tello D., Poljak R. J. Crystallization and preliminary X-ray diffraction studies of two new antigen-antibody (lysozyme-Fab) complexes. J. Mol. Biol. 1988; 203: 527
  • Wrigley N. G., Brown E. B., Skehel J. J. Electron microscopic evidence for the axial rotation and inter-domain flexibility of the Fab regions of IgG. J. Mol. Biol. 1983; 169: 771
  • Wade R. H., Taveau J. C., Lamy J. N. Concerning the axial rotation flexibility of the Fab regions of immunoglobulin G. J. Mol. Biol. 1989; 206: 349
  • Burton R. D. Antibody: the flexible adaptor molecule. TIBS 1990; 15: 64
  • Klein M., Haeffner-Cavaillon N., Isenman D. E., Rivat C., Navia M. A., Davies D. R., Dorrington K. J. Expression of biological effector functions by immunoglobulin G molecules lacking the hinge region. Proc. Natl. Acad. Sci. U.S.A. 1981; 78: 524
  • Dorrington K. J., Klein M. Aspects of immunoglobulin G structure relevant to its interaction with Fc receptors. Mol. Immunol. 1982; 19: 1215
  • Burton D. R. The conformation of antibodies. Fc Receptors and the Action of Antibodies, H. Metzger. Telford Press, Caldwell, NJ 1990; 31
  • Oi V. T., Vuong T. M., Hardy R., Reidler J., Dangl J., Herzenberg L. A., Stryer L. Correlation between segmental flexibility and effector function of antibodies. Nature (London) 1984; 307: 136
  • Dangl J. L., Wensel T. G., Morrison S. L., Stryer L., Herzenberg L. A., Oi V. T. Segmental flexibility and complement fixation of genetically engineered chimeric human, rabbit and mouse antibodies. EMBO J. 1988; 7: 1989
  • Rabat E. A., Wu T. T., Bilofsky H., Reid-Miller M., Perry H. Sequences of proteins of immunological interest. U.S. Department of Health and Human Services, Public Health Service, National Institutes of Health. 1983
  • Marquart M., Deisenhofer J., Huber R., Palm W. Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 and 1.9 Å resolution. J. Molec. Biol 1980; 141: 369
  • Burton D. R. Immunoglobulin G: functional sites. Mol. Immunol 1985; 22: 161
  • Birshtein B. K., Campbell R., Diamond B. Effects of immunoglobulin structure on Fc receptor binding: a mouse myeloma variant immunoglobulin with a γ2b-γ2a hybrid heavy chain having a complete γ2a Fc region fails to bind to γ2a Fc receptors on mouse macrophages. J. Immunol. 1982; 129: 610
  • Rademacher T. W., Dwelt R. A. Structural, functional and conformation analysis of immunoglobulin G-derived asparagine-linked oligosaccharides. Prog. Immun. 1984; 5: 95
  • Mizouchi T., Taniguchi T., Shimizu A., Kobata A. Structural and numerical variations of the carbohydrate moiety of immunoglobulin G. J. Immunol 1982; 129: 2016
  • Deisenhofer J. Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B protein A from Staphylococcus aureus at 2.9 and 2.8 Å resolution. Biochemistry 1981; 20: 2361
  • Sutton B. J., Phillips D. C. The three-dimensional structure of the carbohydrate within the Fc fragment of immunoglobulin G. Biochem. Soc. Trans. 1983; 11: 130
  • Leatherbarrow R. J., Rademacher T. W., Dwek R. A., Woof J. M., Clark A., Burton D. R., Richardson N., Feinstein A. Effector functions of a monoclonal aglycosylated mouse IgG2a: binding and activation of complement component CI and interaction with human monocyte Fc receptor. Molec. Immunol 1985; 22: 407
  • Padlan E. A. X-ray diffraction studies of antibody constant regions. Fc Receptors and the Action of Antibodies, H. Metzger. Telford Press, Caldwell, NJ 1990; 12
  • Poljak R. J., Amzel L. M., Avey H. P., Chen B. L., Phizackerley R. P., Saul F. Three-dimensional structure of the Fab' fragment of a human immunoglobulin at 2.8 Å resolution. Proc. Natl. Acad. Sci. U.S.A. 1973; 70: 3305
  • Davies D. R., Metzger H. Structural basis of antibody function. Annu. Rev. Immunol. 1983; 1: 87
  • Williams A. F., Barclay A. N. The immunoglobulin superfamily — domains for cell surface recognition. Annu. Rev. Immunol 1988; 6: 381
  • Reid K. B. M. Proteins involved in the activation and control of the two path ways of human complement. Biochem. Soc. Trans. 1983; 11: 1
  • Schumaker V. N., Calcott M. A., Spiegelberg H. L., Müller-Eberhard H. J. Ultracentrifuge studies of the binding of IgG of different subclasses to the C1q subunit of the first component of complement. Biochemistry 1976; 16: 5175
  • Painter R. H., Foster D. B., Gardner B., Hughes-Jones N. C. Functional affinity constants of subfragments of immunoglobulin G for C1q. Molec. Immunol 1982; 19: 127
  • Burton D. R., Boyd J., Brampton A. D., Easterbrook-Smith S. B., Emanuel E. J., Novotny J., Rademacher T. W., van Schravendijk M. R., Sternberg M. J. E., Dwek R. A. The C1q receptor site on immunoglobulin G. Nature (London) 1980; 288: 338
  • Wright K. J., Tschopp J., Jaton J.-C., Engel J. Dimeric, trimeric and tetrameric complexes of immunoglobulin G fix complement. Biochem. J. 1980; 187: 775
  • Dower S. K., Segal D. M. C1q binding to antibody-coated cells: predictions from a simple multivalent model. Mol. Immunol 1981; 18: 823
  • Liberti P. A., Bausch D. M., Schoenberg L. M. On the mechanism of C1q binding to antibody. I. Aggregation and/or distortion of IgG vs. combining site transmitted effects. Mol. Immunol 1982; 19: 143
  • Colomb M., Porter R. R. Characterization of a plasmin-digest fragment of rabbit immunoglobulin gamma that binds antigen and complement. Biochem. J. 1975; 145: 177
  • Yasmen D., Ellerson J. R., Dorrington K. J., Painter R. H. The structure and function of immunoglobulin domains. IV. The distribution of some effector functions among the Cγ2 and C-γ3 homology regions of human immunoglobulin G. J. Immunol 1976; 116: 518
  • Boackle R. J., Johnson B. J., Caughman G. B. An IgG primary sequence exposure theory for complement activation using synthetic peptides. Nature (London) 1979; 282: 742
  • Pristowsky M. B., Kehoe J. M., Erickson B. W. Inhibition of the classical complement pathway by synthetic peptides from the second constant domain of the heavy chain of IgG. Biochemistry 1981; 20: 6349
  • Brunhouse R., Cebra J. J. Isotypes of IgG: comparison of the primary structures of isotypes which differ in their ability to activate complement. Molec. Immunol 1979; 16: 907
  • Lukas T. J., Munoz H., Erickson B. W. Inhibition of C1-mediated immune hemolysis by monomelic and dimeric peptides from the second constant domain of human immunoglobulin G. J. Immunol 1981; 127: 2555
  • Duncan A. R., Winter G. The binding site for C1q on IgG. Nature (London) 1988; 332: 563
  • Winkelhake J. L., Kunicki T. J., Elcomebe B. M., Asrerm R. H. Effects of pH treatments and deglycosylation of rabbit immunoglobulin G on the binding of C1q. J. Biol. Chem. 1980; 255: 2822
  • Nose M., Wlgzell H. Biological significance of carbohydrate chains on monoclonal antibodies. Proc. Natl. Acad. Sci. U.S.A. 1983; 80: 6632
  • Berken A., Benacerraf B. Properties of antibodies cytophilic for macrophages. J. Exp. Med. 1966; 146: 241
  • Lynch R. G., Sandor M., Waldschmidt T. J., Mathur A., Schaiff W. T., Berg D. J., Snapp K., Mueller A., Robinson M. G., Noben N., Rosenberg M. G. Lymphocyte Fc receptors: expression, regulation and function. Mol. Immunol. 1990; 27: 1167
  • Anderson C. L., Looney R. J. Human leukocyte IgG Fc receptors. Immunol. Today 1986; 7: 264
  • Anderson C. L. Isolation of the receptor for human IgG from a human monocyte cell line (U937) and from human peripheral blood monocytes. J. Exp. Med 1982; 156: 1794
  • Perussia B., Dayton E. T., Lazarus R., Fanning V., Trinchieri G. Immune interferon induces the receptor for IgG1 on human monocytic and myeloid cells. J. Exp. Med. 1983; 158: 1092
  • Frey J., Engelhardt W. Characterization and structural analysis of Fc receptors of human monocytes, a monoblast cell line (U937) and a myeloblast cell line (HL-60) by monoclonal antibody. Eur. J. Immunol. 1987; 17: 583
  • Allen J. M., Seed B. Nucleotide sequence of three cDNAs for the human high affinity Fc receptor (FcRI). Nucleic Acid Res. 1988; 16: 11824
  • Allen J. M., Seed B. Isolation and expression of functional high-affinity Fc receptor complementary DNAs. Science 1989; 243: 378
  • Rosenfeld S. I., Looney R. J., Leddy J. P., Abraham D. C., Anderson C. L. Human platelet Fc receptor for immunoglobulin G. Identification as a 40,000-molecular-weight membrane protein shared by monocytes. J. Clin. Invest. 1985; 76: 2317
  • Looney R. J., Abraham G. N., Anderson C. L. Human monocytes and U937 cells bear two distinct Fc receptors for IgG. J. Immunol. 1986; 136: 1641
  • Tax W. J. M., Willems H. W., Reekers P. P. M., Capel P. J. A., Koene R. A. P. Polymorphism in mitogenic effect of IgG1 monoclonal antibodies against T3 antigen on human T cells. Nature 1983; 304: 445
  • Lewis V. A., Koch T., Plutner H., Mellman I. A complementary cDNA clone for a macrophage-lymphocyte Fc receptor. Nature 1986; 324: 372
  • Seki T. Identification of multiple isoforms of the low-affinity human IgG Fc receptor. Immunogenetics 1989; 30: 5
  • Brooks D. G., Qiu W. Q., Luster A. D., Ravetch J. V. Structure and expression of human IgG FcRII (CD32). Functional heterogeneity is encoded by the alternatively spliced products of multiple genes. J. Exp. Med. 1989; 170: 1369
  • Stuart S. G., Trounstine M. L., Vaux D. J. T., Koch T., Martens C. L., Mellman I., Moore K. W. Isolation and expression of cDNA clones encoding a human receptor for IgG (Fc-γRII). J. Exp. Med. 1987; 166: 1668
  • Stengelin S., Stamenkovic I., Seed B. Isolation of cDNAs for two distinct human Fc receptors by ligand affinity cloning. EMBO J. 1988; 7: 1053
  • Engelhardt W., Geerds C., Frey J. Distribution, inducibility and biological function of the cloned and expressed human βFc receptor II. Eur. J. Immunol. 1990; 20: 1367
  • Ravetch J. V., Anderson C. L. Fc-γR family: proteins, transcripts, and genes. Fc Receptors and the Action of Antibodies, H. Metzger. Telford Press, Caldwell, NJ 1990; 211
  • Perussia B., Acuto O., Terhorst C., Faust J., Lazarus R., Fanning V., Trinchieri G. Human natural killer cells analyzed by B73.1, a monoclonal antibody blocking Fc receptor function. II. Studies of B73.1 antibody-antigen interaction on the lymphocyte membrane. J. Immunol. 1983; 130: 2142
  • Clarkson S. B., Ory P. A. CD16. Developmentally regulated IgG Fc receptors on cultured human monocytes. J. Exp. Med. 1988; 167: 408
  • Lanier L. L., Ruitenberg J. J., Phillips J. H. Functional and biochemical analysis of CD 16 antigen on natural killer cells and granulocytes. J. Immunol. 1988; 141: 3478
  • Karas S. P., Rosse W. F., Kurlander R. J. Characterization of the IgG-Fc receptor on human platelets. Blood 1982; 60: 1277
  • Fleit H. B., Wright S. D., Unkeless J. C. Human neutrophil Fc receptor distribution and structure. Proc. Natl. Acad. Sci. U.S.A. 1982; 79: 3275
  • Huizinga T. W. J., van der Schoot C. E., Jost C., Klaassen R., Kleljer M., von dem Borne Kr E. G., Roos D., Tetteroo P. A. T. The PI-linked receptor FcRIII is released on stimulation of neutrophils. Nature 1988; 333: 667
  • Selvaraj P., Rossed W. F., Silber R., Springer T. A. The major Fc receptor in blood has a phosphatidylinositol anchor and is deficient in paroxysmal nocturnal hemoglobinuria. Nature 1988; 333: 565
  • Ravetch J. V., Perussia B. Alternative membrane forms of FcγRIII(CD16) on human NK cells and neutrophils: cell-type specific expression of two genes which differ in single nucleotide substitutions. J. Exp. Med. 1989; 170: 481
  • Simmons, Seed B. The Fc receptor of natural killer cells is a phospholipid-linked membrane protein. Nature 1988; 333: 568
  • Peltz A. G., Grundy H. O., Lebo R. V., Yssel H., Barsh G. S., Moore K. W. Human FcγRIII: cloning, expression, and identification of the chromosomal locus of two Fc receptors for IgG. Proc. Natl. Acad. Sci. U.S.A. 1989; 86: 1013
  • Perussia B., Tutt M. M., Qiu W. Q., Kuziel W. A., Tucker P. W., Trinchieri G., Bennett M., Ravetch J. V., Kumar V. Murine natural killer cells express functional Fc receptor II encoded by the FcγRa gene. J. Exp. Med. 1989; 170: 73
  • Scallon J. B., Scigliano E., Freedman V. H., Miedel M. C., Pan Y.-C. E., Unkeless J. C., Kochan J. P. A human immunoglobulin G receptor exists in both polypeptide-anchored and phosphatidylinositol-glycan-anchored forms. Proc. Natl. Acad. Sci. U.S.A. 1989; 86: 5079
  • Werner G., von dem Borne A. E. G. K., Bos M. J. E., Tromp J. F., van der Plas-van Dalen C. M., Visser F. J., Engelfriet C. P., Tetteroo P. A. T. Localization of the human NA1 alloantigen on neutrophil Fc-gamma receptors. Leukocyte Typing III, Vol. 3, Human Myeloid and Hematopoietic Cells, E. L. Reihertz, B. F. Haynes, L. M. Nadler, I. D. Bernstein. Springer-Verlag, New York 1988; 109
  • Tetteroo P. A. T., van der Schoot C. E., Visser F. J., Bos M. J. E., von dem Borne A. E. G. K. Three different types of Fcγ receptors on human leukocytes defined by workshop antibodies: FcγRloW on neutrophils, FcγRlow of K/NK lymphocytes, and FcγRII. Leukocyte Typing III. White Cell Differentiation Antigens, A. J. McMichael. Oxford University Press, OxfordUK 1987; 702
  • Fanger M. W., Shen L., Graziano R. F., Guyre P. M. Cytotoxicity mediated by human Fc receptors for IgG. Immunol. Today 1989; 10: 92
  • Anderson P., Morimoto C., Breitmeyer J. B., Schlossman S. F. Regulatory interactions between members of the immunoglobulin superfamily. Immunol. Today 1988; 9: 199
  • Miettinen H. M., Rose J. K., Mellman I. Fc receptor isoforms exhibit distinct abilities for coated pit localization as a result of cytoplasmic domain heterogeneity. Cell 1989; 58: 317
  • Kimberly R. P., Tappe N. J., Merriam L. T., Redecha P. B., Edberg J. C., Schwartzman S., Valinsky J. E. Carbohydrates on human Fcγ receptors. Independence of the classical IgG and non-classical lectin-binding sites on human Fcγ RIII expressed on neutrophils. J. Immunol. 1989; 142: 3923
  • Salmon J. E., Kapur S., Kimberly R. P. Opsonin-independent ligation of Fc receptors: the 3G8-bearing receptors on neutrophils mediate the phagocytosis of concanavalin A-treated erythrocytes and non-opsonize. Escherichia coli, J. Exp. Med. 1987; 166: 1798
  • Hoxie J. A., Mathews D. M., Callahan J., Cassel D. L., Cooper R. A. Transient modulation and internalization of T4 antigen induced by phorbol esters. J. Immunol. 1986; 137: 1194
  • Alcantra O., Phillips J. L., Bolt D. H. Phorbol diesters and transferrin modulate lymphoblastoid cell transferrin receptor expression by two different mechanisms. J. Cell. Physiol. 1986; 129: 329
  • Hunziker W., Koch T., Whitney J. A., Mellman I. Fc receptor phosphorylation during receptor-mediated B-cell activation. Nature (London) 1990; 345: 628
  • Sarmay G., Pecht I., Gergely J. Phosphorylation of type II Fcγ receptor on activated human B lymphocytes. Int. Immunol 1990; 2: 1235
  • Gergely J., Sarmay G. Production of soluble FcγR by activated B lymphocytes. Pathobiology, in press
  • Okafor G. O., Turner M. W., Hay F. C. Localization of monocyte binding site of human immunoglobulin G. Nature (London) 1974; 248: 228
  • Alexander M. D., Andrews J. A., Leslie R. G. Q., Wood H. W. The binding of human and guinea pig IgG subclasses to homologous macrophages and monocyte receptors. Immunology 1978; 35: 115
  • Barnett-Foster D. E., Dorrington K. J., Painter R. H. Structure and function of immunoglobulin domains. VIII. An analysis of the structural requirements in human IgG1 for binding to the Fc receptor of human monocytes. J. Immunol. 1980; 124: 2186
  • Woof J. M., Nik Jaafar M. I., Jefferis R., Burton D. R. The monocyte binding domain(s) on human immunoglobulin G. Mol. Immunol. 1984; 21: 523
  • Ciccimara F., Rosen F. S., Merler E. Localisation of the IgG effector site for monocyte receptors. Proc. Natl. Acad. Sci. U.S.A. 1975; 72: 2081
  • Ratcliffe A., Stanworth D. R. The use of synthetic gamma chain peptides in the localization of the binding site(s) on human IgG1 for the Fc receptors of homologous monocytes and heterologous mouse macrophages. Immunol. Lett. 1982; 4: 215
  • Nik Jaafar M. I., Lowe J. A., Ling N. R., Jefferis R. Immunogenic and antigenic epitopes of immunoglobulins. V. Reactivity of a panel of monoclonal antibodies with subfragments of human Fc and abnormal paraproteins having deletions. Mol. Immunol. 1982; 20: 679
  • Nik Jaafar M. I., Lowe J. A., Ling N. R., Jefferis R. Immunogenic and antigenic epitopes of immunoglobulins. VII. The topographical distribution of Fc epitopes and the relationship of an isoallotypic specificity to the presence of histidine 435. Mol. Immunol. 1984; 21: 137
  • Brüggemann M., Williams G. T., Bindon C. I., Clark M. R., Walker M. R., Jefferis R., Waldmann H., Neuberger M. S. Comparison of the effector functions of human immunoglobulins using a matched set of chimeric antibodies. J. Exp. Med. 1987; 166: 1351
  • Jefferis R., Lund J., Pound J. Molecular definition of interaction sites on human IgG for Fc receptors (huFcγR). Mol. Immun. 1990; 27: 1237
  • Partridge L. J., Woof J. M., Jefferis R., Burton D. R. The use of anti-IgG monoclonal antibodies in mapping the monocyte receptor site for IgG. Mol. Immun. 1986; 23: 1365
  • Woof J. M., Partridge L. J., Jefferis R., Burton D. R. Localization of the monocyte-binding region on human immunoglobulin G. Mol. Immunol. 1986; 23: 319
  • Spiegelberg H. L., Perlmann H., Perlmann P. Interaction of K lymphocytes with myeloma proteins of different IgG subclasses. J. Immunol. 1976; 116: 1464
  • Gergely J., Sarmay G. IgG-Fc-receptors: ligand binding and lysis induction. Immunol. Lett. 1989; 20: 1
  • Sarmay G., Benczur M., Petranyi G Y., Klein E., Kahn M., Stanworth D. R., Gergely J. Ligand inhibition studies on the role of Fc receptors in antibody-dependent cell-mediated cytotoxicity. Mol. Immunol 1984; 21: 43
  • Sarmay G., Jefferis R., Klein E., Benczur M., Gergely J. Mapping of the functional topography of Fc with monoclonal antibodies: localization of epitopes interacting with the binding sites of Fc receptors on human K cells. Eur. J. Immunol. 1985; 15: 1037
  • Erdei A., Benczur M., Fabry Zs., Dierich M. P., Gergely J. C3 cleaved by, membrane proteases binds to C3b acceptors expressed on Con A-stimulated human lymphocytes and enhances antibody dependent cellular cytotoxicity. Scand. J. Immunol 1984; 20: 125
  • Sarmay G., Jefferis R., Gergely J. CH2 and CH3 domain deleted IgG1 paraproteins inhibit differently Fc receptor mediated binding and lysis. Immunol. Lett. 1986; 12: 307
  • Rozsnyai Z., Sarmay G., Walker M., Maslanka K., Valasek Z., Jefferis R., Gergely J. Distinctive role of IgG1 and IgG3 isotypes in Fc R-mediated functions. Immunology 1989; 66: 491
  • Sarmay G., Rozsnyay Z., Gergely J. FcγRII expression and release on resting and activated human B lymphocytes. Mol. Immunol 1990; 27: 1195
  • Sarmay G., Istvan L., Gergely J. Shedding and reappearance of Fc, C3 and SRBC receptors on peripheral lymphocytes from normal donors and chronic lymphatic leukaemia (CLL) patients. Immunology 1978; 34: 315
  • Sandor M L, Füst G., Medgyesi G. A., Gergely J. Isolation and characterization of Fc receptor shed from human peripheral mononuclear blood cells. Immunology 1978; 35: 559
  • Uher F., Jancso A., Sandor M., Pinter K., Biro E., Gergely J. Interaction between actomyosin complexes and Fc receptors on human peripheral mononuclear cells. Immunol. Lett. 1981; 2: 213
  • Sarmay G., Benczur M., Petranyi G Y., Klein E., Kahn M., Stanworth D. R., Gergely J. Ligand inhibition studies on the role of Fc receptors in antibody-dependent cell-mediated cytotoxicity. Mol. Immunol 1984; 21: 43
  • Sandor M., Füst G., Medgyesi G. A., Erdei A., Gergely J. The heterogeneity of Fc receptors of human peripheral mononuclear cells. Immunology 1978; 38: 353
  • Sandor M., Füst G., Medgyesi G. A., Gergely J. Isolation and characterization of Fc receptor shed from human peripheral mononuclear blood cells. Immunology 1978; 35: 559
  • Sarmay G., Rozsnyai Z., Szabo I., Biro A., Gergely J. Modulation of type II Fcγ receptor expression on activated human B lymphocytes. Eur. J. Immunol 1991; 21: 241
  • Walker M. R., Woof J. M., Brüggemann M., Jefferis R., Burton D. R. Interaction of human chimeric antibodies with the human FcRI and FcRII receptors: requirements for antibody-mediated host-target cell interaction. Mol. Immunol 1989; 26: 403
  • Salmon J. E., Kimberly R. P. Phagocytosis of concanavalin A-treated erythrocytes is mediated by the Fcγ receptor. J. Immunol 1986; 137: 456
  • Fridman W. H., Golstein P. Immunoglobulin-binding factor present on and produced by thy-mus-processed lymphocytes (T cells). Cell. Immunol 1974; 11: 424
  • Fridman W. H., Sautes C. Immunoglobulin-binding factors. Fc Receptors and the Action of Antibodies, H. Metzger. Telford Press, Caldwell, NJ 1990; 335
  • Le Thui Thi Bich, Samarut C., Brochier J., Fridman W. H., Revillard J. P. Suppression of mitogen induced peripheral B cell differentiation by soluble receptors for Fc IgG released from lymphocytes. Eur. J. Immunol 1980; 10: 894
  • Neauport-Sautes C., Dupuis D., Fridman W. H. Specificity of Fc receptors on activated T cells. Relation with released immunoglobulin binding factor. Eur. J. Immunol 1975; 5: 849
  • Pure E., Durie C. J., Summerill C. K., Unkeless J. C. Identification of soluble Fc receptors in mouse serum and the conditioned medium of stimulated B cells. J. Exp. Med. 1984; 160: 1836
  • Calvo C., Watanabe F., Metivier D., Senik A. Human monocyte-cell line U937 releases suppressive IgG BF. Eur. J. Immunol 1986; 16: 25
  • Le Thui Thi Bich, Samarut C., Rabourdin-Combe C., Revillard J. P. The suppressive activity of FcγRs is not related to their T cell origin. Cell. Immunol 1982; 68: 252
  • Fridman W. H. Ed., Structures and functions of low affinity Fc receptors. Chem. Immunol. 1989; 47
  • Daeron M., Neauport-Sautes C., Yodoi J., Moncuit J., Fridman W. H. Receptors for immunoglobulin isotypes (FcR) on murine T cells. II. Multiple FcR induction on hybridoma T cell clones. Eur. J. Immunol 1985; 15: 668
  • Hoover R. G., Gebel H. M., Dieckgraefe B. K., Hickman S., Rebbe N. F., Hirayama N., Ovary Z., Lynch R. G. Occurrence and potential significance of increased number of T cells with Fc receptors in myeloma. Immunol. Rev. 1981; 56: 115
  • Khayat D., Dux Z., Anavi R., Shlomo Y., Witz I. P., Ran M. Circulating cell free Fcγ2b/1 receptor in normal mouse serum: its detection and specificity. J. Immunol 1984; 132: 2496
  • Khayat D., Geffrier C., Yoon S., Scigliano E., Soubran C., Weil M., Unkeless J. C. Soluble circulating Fcγ receptor in human serum, a new ELISA assay for specific and quantitative detection. J. Immunol. 1987; 100: 235
  • Sarfati M., Bron D., Lagneaux L., Fonteyn C., Frost H., Delespesse G. Elevation of Ige-binding factors in serum of patients with B-cell derived chronic lymphoid leukemia. Blood 1988; 71: 94
  • Blank U., Daeron M., Galinha A., Fridman W. H., Sautes C. The carbohydrate moieties of suppressor IgG binding factor released by murine T cells. Mol. Immunol 1987; 24: 1061
  • Blank U., Daeron M., Galinha A., Malard V., Fridman W. H., Sautes C. Identification of the FcγRII related component of murine IgG-BF. Mol. Immunol 1989; 26: 107
  • Daeron M., Neauport-Sautes C., Blank U., Fridman W. H. 2.4G2 a monoclonal antibody to macrophage Fcγ receptors reacts with murine T cell Fcγ receptors and IgG-binding factors. Eur. J. Immunol 1986; 16: 1545
  • Sautes C., Varin N., Hogarth P. M., Unkeless J. C., Teillaud C., Even J., Lynch A., Fridman W. H. Molecular and functional studies of recombinant soluble Fcγ receptors. Mol. Immunol 1990; 27: 1201
  • Levinson A. I., Martin J. Rheumatoid factor: Dr. Jekyll or Mr. Hyde. Br. J. Rheum. 1988; 27: 83
  • Poncet P., Matthes T., Billecoco A., Dighiero G. Immunochemical studies of poly specific natural autoantibodies: charge, lipid reactivity, F(ab')2 fragment activity and complement fixation. Mol. Immunol 1988; 25: 981
  • Heller G., Kolodny M. H., Lepow I. H., Jacobson A. S., Rivera M. E., Marks G. H. The haemagglutination test for rheumatoid arthritis. IV. Characterization of the rheumatoid agglutinating factors by analysis of serum fractions prepared by ethanol fractionation. J. Immunol 1955; 74: 340
  • Hartman A. B., Mallett C. P., Srinivasappa J., Prabhakar B. S., Notkins A. L., Smith-Gill S. J. Organ reactive autoantibodies from non-immunized adult Ba1b/c mice are polyreactive and express non-biased VH gene usage. Mol. Immunol. 1989; 26: 359
  • Rousseau P. G., Mallett C. P., Smith-Gill S. J. A substantial proportion of the adult Ba1b/c available B cell repertoire consists of multireactive B cells. Mol. Immunol 1989; 26: 003
  • Lydyard P. M., Quartey-Papafio R., Bröker B., Mackenzie L., Jouquan J., Blaschek M. A., Steele J., Petrou M., Collins P., Isenberg D., Youinou P. Y. The antibody repertoire of early human B cells. I. High frequency of autoreactivity and polyreactivity. Scand. J. Immunol 1990; 31: 33
  • Fernandez P.-A., Ternyck T., Avrameas S. Immunochemical studies of a murine polyreactive IgG2b autoantibody with rheumatoid factor activity. Mol Immunol 1989; 26: 539
  • Shlomshik M. J., Nemazee D. A., Sato V. I., Van Snick J., Carson D. A., Weigert M. Variable region sequences of murine IgM anti-IgG monoclonal autoantibodies (rheumatoid factors). A structural explanation for the high frequency of IgM anti-IgG B cells. J. Exp. Med. 1986; 164: 407
  • Manheimer-Lory A. J., Monestier M., Bellon B., Alt F. W., Bona C. A. Fine specificity, idiotypy, and nature of cloned heavy-chain variable region genes of murine monoclonal rheumatoid factor antibodies. Proc. Natl. Acad. Sci. U.S.A. 1986; 83: 8293
  • Monestier M., Manheimer-Lory A., Bellon B., Painter C., Dang H., Talal N., Zanetti M., Schwartz R., Pisetsky D., Kuppers R., Rose N., Brochler J., Klareskog L., Holmdahl R., Erlanger B., Alt F., Bona C. Shared idiotypes and restricted immunoglobulin variable region heavy chain genes characterize murine autoantibodies of various specificities. J. Clin. Invest. 1986; 78: 753
  • Burastero S. E., Casali P., Wilder R., Notkins A. L. Monoreactive high affinity and polyreactive low affinity rheumatoid factors are produced by CD5+ B cells from patients with rheumatoid arthritis. J. Exp. Med. 1988; 168: 1979
  • Nakamura M., Burastero S. E., Notkins A. L., Casali P. Human monoclonal rheumatoid factor-like antibodies from CD5+ (Leu-1)+ B cells are polyreactive. J. Immunol 1988; 140: 4180
  • Hayakawa K., Hardy R. R., Honda M., Herzenberg L., Steinberg A. D., Herzenberg L. A. Ly-1 B cells: functionally distinct lymphocytes that secrete IgM autoantibodies. Proc. Natl Acad. Sci. U.S.A. 1984; 81: 2494
  • Hardy R. R., Hayakawa K., Shimizu M., Yamasaki K., Kishimoto T. Rheumatoid factor secretion from human Leu-1+ B cells. Science 1987; 236: 81
  • Pereira P., Coutinho A. I-E-linked control of spontaneous rheumatoid factor production in normal mice. J. Exp. Med. 1989; 170: 1825
  • Van Snick J. L., Masson P. L. Age-dependent production of IgA and IgM autoantibodies against IgG2a in a colony of 129/Sv mice. J. Exp. Med. 1979; 149: 1519
  • Van Snick J. L., Masson P. L. Incidence and specificities of IgA and IgM anti-IgG autoantibodies in various mouse strains and colonies. J. Exp. Med. 1980; 151: 45
  • Van Snick J. A gene linked to the IgG-C locus controls the production of rheumatoid factor in the mouse. J. Exp. Med. 1981; 153: 738
  • Dresser D. W. Most IgM-producing cells in the mouse secrete autoantibodies (rheumatoid factor). Nature 1978; 274: 480
  • Vischer T. L. Neutral proteinases induce rheumatoid factor production in mouse spleen cell cultures. Clin. Exp. Immunol. 1984; 55: 99
  • Dziarski R. Preferential induction of autoantibody secretion in polyclonal activation by peptidoglycan and lipopolysaccharide. J. Immunol. 1982; 128: 1018
  • Dziarski E. Anti-immunoglobulin autoantibodies are not preferentially induced in polyclonal activation of human and mouse lymphocytes, and more anti-DNA and anti-erythrocyte autoantibodies are induced in polyclonal activation of mouse than human lymphocytes. J. Immunol. 1984; 133: 2537
  • Levinson A. I. Nature of stimulus for rheumatoid factor production. Autoantibodies to Immunoglobulins, F. Shakib. S. Karger, Basel 1989; 26, Monogr. Allergy
  • Shokri F., Mageed R. A., Maziak B. R., Jefferis R. Expression of VHIII-associated cross-reactive idiotype on human B lymphocytes. Association with staphylococcal protein A binding and Staphylococcus aureus Cowan I stimulation. J. Immunol. 1991; 146: 936
  • Izui S., Kelley V. E., Masuda K., Yoshida H., Roths J. B., Murphy E. D. Induction of various autoantibodies by mutant gene 1pr in several strains of mice. J. Immunol. 1984; 133: 227
  • Carson D. A. Rheumatoid factor. Textbook of Rheumatology, W. N. Kelly, E. D. Harris, S. Ruddy. W. B. Saunders, Philadelphia 1985; 664
  • Carson D. A., Chen P. P., Fox R. I., Kipps T. J., Jirik F., Godfien R. D., Silverman G., Radoux V., Fong S. Rheumatoid factor and immune networks. Ann. Rev. Immunol. 1987; 5: 109
  • Hang L. M., Theofilopoulos A. N., Dixon F. J. A spontaneous rheumatoid arthritis-like disease in MRL/1 mice. J. Exp. Med. 1982; 155: 1690
  • Aho K., Wager O. Production of “anti-antibodies” in rabbits. Appearance in rabbit serum of “anti-antibodies” reacting with autogenous and isogenous antibody, following autostimulation with protein antigens. Ann. Med. Exp. Fenn. 1961; 39: 79
  • Van Snick J., Coulie P. Rheumatoid factors and secondary immune responses in the mouse. Eur. J. Immunol 1983; 13: 890
  • Coulie P., Van Snick J. Rheumatoid factors and secondary immune responses in the mouse. II. Incidence, kinetics and induction mechanisms. Eur. J. Immunol. 1983; 13: 895
  • Nemazee D. A., Sato V. L. Induction of rheumatoid antibodies in the mouse. Regulated production of autoantibody in the secondary humoral response. J. Exp. Med. 1983; 158: 529
  • Stanley S. I., Bishoff J., Davie J. M. Antigen induced rheumatoid factors: protein and carbohydrate antigens induce different rheumatoid factor responses. J. Immunol. 1987; 139: 2936
  • Stanley S. L., Jr., Li E., Davie J. M. Antigen induced rheumatoid factors: characteristics of monoclonal rheumatoid factors produced after protein and carbohydrate immunization. Mol. Immunol. 1988; 25: 285
  • Nemazee D. A. Immune complexes can trigger specific, T cell-dependent autoanti-IgG antibody production in mice. J. Exp. Med. 1985; 161: 242
  • Coulie P., Van Snick J. Rheumatoid factor (RF) production during anamnestic immune response in the mouse, in. Activation of RF precursor cells is induced by their interaction with immune complexes and carrier-specific helper T cells. J. Exp. Med. 1985; 161: 88
  • Holmdahl R., Klageskog L., Anderson M., Hansen C. High antibody response to autologous type II collagen is restricted to H-2q. Immunogenetics 1986; 24: 84
  • Casali P., Burastero S. E., Balow J. E., Notkins A. L. High affinity antibodies to ssDNA are produced by CD− B cells in systemic lupus erythematosus patients. J. Immunol. 1989; 143: 3476
  • Tarkowski A., Czerkinsky C., Nilsson L.-A. Detection of IgG rheumatoid factor secreting cells in autoimmune MRL/1 mice: a kinetic study. Clin. Exp. Immunol 1984; 58: 7
  • Izui S., Eisenberg R. A. Circulating anti-DNA-rheumatoid factor complexes in MRL/1 mice. Clin. Immunol. Immunopathol 1980; 15: 536
  • Fazekas Gy., Rajnavölgyi E., Kurucz I., Sintar E., Kiss K., Laszlo G., Gergely J. Isolation and characterization of IgG2a-reactive autoantibodies from influenza virus-infected BALB/c mice. Eur. J. Immunol 1990; 20: 2719
  • Paavonen T., Quartey-Papalio R., Delyes P. J., Mackenzie L., Lund T., Youinou P., Lydyard P. M. CD5 mRNA expression and autoantibodies in early human B cells immortalized by EBV. Scand. J. Immunol 1990; 31: 269
  • Taguchi H., Kanoh M., Takubo N., Kadota S., Kanazawa K., Hitsumoto V., Shirata T., Utsumi S. IgG isotype and isotype specificity of murine monoclonal IgG rheumatoid factors. Clin. Exp. Immunol 1990; 80: 136
  • Shlomshik M., Nemazee D., Van Snick J., Weigert M. Variable region sequence of murine IgM anti-IgG monoclonal autoantibodies (rheumatoid factors): II. Comparison of hybridomas derived by lipopolysaccharide stimulation and secondary protein immunization. J. Exp. Med. 1987; 165: 970
  • Shlomshik M. J., Marshak-Rothstein A., Wolfowicz C. B., Rothstein T. L., Weigert M. G. The role of clonal selection and somatic mutation in autoimmunity. Nature 1987; 328: 805
  • Jefferis R., Mageed R. A. The specificity and reactivity of rheumatoid factors with human IgG. Autoantibodies to Immunoglobulins, F. Shakib. Monogr. Allergy, S. Karger, Basel 1989; 26
  • Pisetsky D. S., Darwin B. S., Reich C. F. IgG binding of monoclonal anti-nuclear antibodies from MLR-1pr mice. Immunology 1990; 71: 586
  • Holmdahl R., Nordling C., Rubin K., Tarkowski A., Klareskog L. Generation of rheumatoid factors after immunization with collagen type II-anti-collagen II immune complexes. An anti-idiotypic antibody to anti-collagen II is also rheumatoid factor. Scand. J. Immunol. 1986; 24: 197
  • Bona C. A. Epibodies. A particular set of anti-idiotypes specific for autoantibodies. Clin. Immunol. Newsl. 1985; 6: 87
  • Chen P. P., Fong S., Houghten R. A., Carson D. A. Characterization of an epibody. An anti-idiotype that reacts with both the idiotype of rheumatoid factors (RF) and the antigen recognized by RF. J. Exp. Med. 1985; 161: 323
  • Johnson P. M., Phua K. K., Evans H. B. An idiotypic complementary between rheumatoid factor and antipeptidoglycan antibodies. Clin. Exp. Immunol. 1985; 61: 373
  • Nardella F. A., Teller D. C., Barber C. B., Mannik M. IgG rheumatoid factors and staphylococcal protein A bind to common molecular region on IgG. J. Exp. Med. 1985; 162: 1811
  • Nardella F. A., Schröder A. K., Svensson M.-L., Sjöquist J., Barber C., Christensen P. T15 group A streptococcal Fc receptor binds to the same location on IgG as staphylococcal protein A and IgG rheumatoid factors. J. Immunol. 1987; 140: 922
  • Sasso E. H., Barber C. V., Nardella F. A., Yount W. J., Mannik M. Antigenic specificities of human monoclonal and polyclonal IgM rheumatoid factors. J. Immunol. 1988; 140: 3098
  • Huck S., Fort P., Crawford D. H., Lefranc M.-P., Lefranc G. Sequence of a human immunoglobulin gamma 3 heavy chain constant region gene: comparison with the other human C genes. Nucl. Acids Res. 1986; 14: 1779
  • Artandi S. E., Canifieid S. M., Tao M.-H., Calame K. L., Morrison S. L., Bonagura V. R. Molecular analysis of IgM rheumatoid factor binding to chimeric IgG. J. Immunol 1991; 146: 603
  • Parekh R. B., Dwek R. A., Sutton B. J., Fernandes D. L., Leung A., Stanworth D. R., Rademacher T. W., Mizouchi T., Taniguchi T., Matsuta K., Takeuchi F., Nagano Y., Miyamoto T., Kobata A. Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG. Nature 1985; 316: 452
  • Axford J. S., Mackanzie L., Lydyard P. M., Hay F. C., Isenberg D. A., Roitt I. M. Reduced B cell galactosyltransferase activity in rheumatoid arthritis. J. Immunol. 1988; 140: 3098
  • Newkirk M. M., Lemmo A., Rauch J. Importance of the IgG isotype, not the state of glycosylation, in determining human rheumatoid factor binding. Arth. Rheum. 1990; 33: 800
  • Van Snick J., Stassin V., de Lestre B. Isotypic and allotypic specificity of mouse rheumatoid factors. J. Exp. Med. 1983; 157: 1006
  • Aguado M. T., Balderas R. S., Rubin R. L., Duchosal M. A., Kofler R., Birshtein B. K., Secher D. S., Dixon F. J., Theofilopoulos A. N. Specificity and molecular characteristics of monoclonal IgM rheumatoid factors from arthritic and non-arthritic mice. J. Immunol. 1987; 139: 1080
  • Stassin V., Coulie P., Birshtein B., Secher D., Van Snick J. Determinants recognized by murine rheumatoid factors: molecular localization using a panel of mouse myeloma variant immunoglobulins. J. Exp. Med. 1983; 158: 1763
  • Izui S., Eisenberg R. A., Dixon F. J. IgM rheumatoid factors in mice injected with bacterial lipopolysaccharides. J. Immunol. 1979; 122: 2096
  • Tarkowski A., Holmdahl R., Klageskog L. Rheumatoid factors in mice. Autoantibodies to Immunoglobulins, F. Shakib. Monogr. Allergy, S. Karger, Basel 1989; 26
  • Coutelier J.-P., Van der Logt J. T. M., Hessen F. W. A., Vink A., Warnier G., Van Snick J. IgG2a restriction of murine antibodies elicited by viral infections. J. Exp. Med. 1987; 165: 64
  • Coutelier J.-P., Van der Logt J. T. M., Hessen F. W. A., Vink A., Van Snick J. Virally induced modulation of murine IgG subclasses. J. Exp. Med. 1988; 168: 2373
  • Rajnavölgyi E., Fazekas Gy., Daeron M., Teillaud J.-L., Fridman W. H., Jefferis R., Gergely J. Fine specificity and functional properties of rheumatoid factor-like autoantibodies isolated from influenza virus infected Ba1b/c mice, unpublished manuscript
  • Nardella F. A., Teller D. C., Mannik M. Studies on the antigenic determinants in the self-association of IgG rheumatoid factor. J. Exp. Med. 1981; 154: 112
  • Robbins D. L., Skilling J., Benisek W. F., Wistar R. Estimation of the relative avidity of 19S IgM rheumatoid factor secreted by rheumatic synovial cells for human IgG subclasses. Arth. Rheum. 1986; 29: 722
  • Easterbrook-Smith S. B., Vandenberg R. J., Alden J. R. The role of Fc:Fc interactions in insoluble immune complex formation and complement activation. Mol. Immunol 1988; 25: 1331
  • Klaasen R. J. L., Goldschmeding R., Tetteroo P. A. T., von dem Borne A. E. G. K. The Fc valency of an immune complex is the decisive factor for binding to low-affinity Fc receptors. Eur. J. Immunol 1988; 18: 1373
  • Jungi T. W., Lerch P. G., Cachelin A. B., Morell A. Monomelic and dimeric IgG1 as probes for assessing high-affinity and low-affinity receptors for IgG on human monocyte derived macrophages and on activated macrophages. Mol. Immunol 1985; 55: 555
  • Doekes G., Schouten J., Cats A., Dana M. R. Reduction of the complement activation capacity of soluble IgG aggregates and immune complexes by IgM-rheumatoid factor. Immunology 1985; 55: 555
  • Doekes G., Hiemstra P. S. Rheumatoid factor and complement activation. Autoantibodies to Immunoglobulins, F. Shakib. Monogr. Allergy, S. Karger, Basel 1989; 26
  • Rajnavölgyi E., Reth M., Uher F., Miklos K., Gergely J., Rajewsky K. Fc-dependent effector functions of idiotype-anti-idiotype immune complexes. Mol. Immunol. 1984; 21: 127
  • Tesar J. T., Schmid F. R. Conversion of soluble immune complexes into complement-fixing aggregates by IgM-rheumatoid factor. J. Immunol. 1970; 105: 1206
  • Tanimoto K., Cooper N. R., Johnson J. S., Vaughan J. H. Complement fixation by rheumatoid factor. J. Clin. Invest. 1975; 55: 437
  • Doekes G., Van Es L. A., Daha M. R. Activation of C1q by soluble IgG aggregates as detected by a novel one-step hemolytic assay that specifically measures proenzyme form of C1s. J. Immunol. 1983; 131: 1924
  • Feinstein A., Richardson N. E., Gorick B. D., Hugh-Jones N. C. Immunoglobulin M conformational change is a signal for complement activation. Protein Conformation as an Immunological Signal, F. Celada, V. N. Schumaker, E. E. Sercarz. Plenum Press, New York 1983; 47
  • Chestnut R. W., Colon S. M., Grey H. M. Requirements for the processing of antigens by antigen-presenting B cells. I. Functional comparison of B cell tumors and macrophages. J. Immunol. 1982; 129: 2382
  • Lanzavecchia A. Antigen uptake and accumulation in antigen-specific B cells. Immunol. Rev. 1987; 99: 39
  • DeFranco A. L., Gold M. R., Jakway J. P. B-lymphocyte signal transduction in response to anti-immunoglobulin and bacterial lipopolysaccharide. Immunol. Rev. 1987; 95: 161
  • Cambier J. C., Ransom J. T. Molecular mechanisms of transmembrane signalling in B lymphocytes. Annu. Rev. Immunol. 1987; 5: 175
  • Klaus G. G. B., Bijsterbosch M. K., O'Garra A., Harnett M. H., Rigley K. P. Receptor signalling and crosstalk in B lymphocytes. Immunol. Rev. 1987; 99: 19
  • McDougall S. L., Grinstein S., Gelfand E. W. Activation of Ca++ dependent K+ channels in human B lymphocytes by anti-immunoglobulins. J. Clin. Invest. 1988; 81: 449
  • Ransom J. T., Cambier J. C. The dynamics of K+ efflux and Ca2+ influx in B lymphocytes following antigen receptor crosslinking. Proc. Soc. Gen. Physiol., in press
  • Amigorena S., Choquet D., Teillaud J.-L., Korn H., Fridman W. H. Ion channels and B cell mitogenesis. Mol. Immunol 1990; 27: 1259
  • Ingles J., Engel P., De La Calle O., Gallart T. Differential responsiveness of human B lymphocytes to phorbol ester and calcium ionophore based on their state of activation. Immunology 1989; 67: 359
  • Lenhardt W., Karasuyama H., Rolink A., Melchers F. Control of the cycle of murine B 11 of α- and β-growth factors and of B cell maturation factors. Immunol. Rev. 1987; 99: 241
  • Melchers F., Lenhardt W. Three restriction points in the cell cycle of activated murine B lymphocytes. Proc. Natl. Acad. Sci. U.S.A. 1985; 82: 7681
  • Janeway C. A., Jr., Bottomly K., Babich J., Conrad P., Conzen S., Jones B., Kaye J., Katz M., McVay L., Murphy D. B., Tite J. Quantitative variation in la antigen expression plays a central role in immune regulation. Immunol. Today 1984; 5: 99
  • Melchers F., Erdei A., Schultz T., Dierich M. P. Growth control of activated, synchronized murine B cells by the C3d fragment of human complement. Nature (London) 1985; 317: 264
  • Howard M., Paul W. E. Regulation of B cell growth and differentiation by soluble factors. Ann. Rev. Immunol. 1983; 1: 307
  • Barrett T. B., Shu G. L., Draves K. E., Pezutto A., Clark E. A. Signaling through CD19, Fc receptors or transforming growth factor-β: each inhibits the activation of resting human B cells differently. Eur. J. Immunol. 1990; 20: 1053
  • Pezzutto A., Dörken B., Rabinovich P. S., Ledbetter J. A., Moldenhauer G., Clark E. A. CD19 monoclonal antibody HD37 inhibits anti-immunoglobulin induced B cell activation and proliferation. J. Immunol. 1987; 138: 2793
  • Sinclair N. R. S., Chan P. L. Regulation of the immune response. IV. The role of the Fc-fragment in feedback inhibition by antibody. Adv. Exp. Biol. 1971; 12: 609
  • Uhr J. W., Möller G. Regulatory effect of antibody on the immune response. Adv. Immunol. 1968; 8: 81
  • Abrahams S., Phillips R. S., Miner R. A. Inhibition of the immune response by tS antibody. Mechanism and site of action. J. Exp. Med. 1973; 137: 870
  • Ryan J. L., Henkart P. A. Fc receptor mediated inhibition of murine B lymphocyte activation. J. Exp. Med. 1976; 144: 768
  • Kölsch E., Oberbarnscheidt J., Bruner K., Heuer J. The Fc-receptor: its role in the transmission of differentiation signals. Immunol. Rev. 1980; 49: 61
  • Uher F., Dickler H. B. Independent ligand occupancy and cross-linking of surface Ig and Fc receptors downregulates B-lymphocyte function. Evaluation in various B-lymphocyte populations. Mol. Immunol 1985; 23: 1177
  • Waldschmidt T. J., Vitetta E. S. Fc receptors on B cells mediate down regulation of antibody secretion. Ann. Immunol. 1985
  • Phillips N. E., Parker D. C. Crosslinking of B lymphocytes, Fcγ receptors and membrane immunoglobulin inhibits anti-immunoglobulin-induced blastogenesis. J. Immunol. 1984; 132: 627
  • Bijsterbosch M. K., Klaus G. G. Crosslinking of surface immunoglobulin and Fc receptors on B lymphocytes inhibits stimulation of inositol phospholipid breakdown via the antigen receptors. J. Exp. Med. 1985; 162: 1825
  • Rigley K. P., Harnett M. M., Klaus G. G. B. Co-cross-linking of surface immunoglobulin Fcγ receptors on B lymphocytes uncouples the antigen receptors from their associated G protein. Eur. J. Immunol. 1989; 19: 481
  • Tsokos G. C., Kinoshita T., Thyphronitis G., Patel A. D., Didder H. B., Finkelman F. D. J. Immunol. 1990; 144: 239
  • Carter R. H., Spycher M. O., Yin C. N. G., Hoffman R., Fearon D. T. Synergistic interaction between complement receptors type 2 and membrane IgM on B lymphocytes. J. Immunol. 1988; 141: 457
  • Wiersma E. J., Coulie P. G., Heyman B. Dual immunoregulatory effects of monoclonal IgG-antibodies: suppression and enhancement of the antibody response. Scand. J. Immunol 1989; 29: 439
  • Heyman B. Fc-dependent IgG-mediated suppression of the antibody response: fact or artifact. Immunol. Today 1990; 11: 310
  • Marcelletti J. F., Katz D. H. FcR+ lymphocytes and the regulation of the IgE antibody system. I. A new class of molecules termed IgE-induced regulants (EIR) which modulate FcR expression by lymphocytes. J. Immunol 1984; 133: 2821
  • Bonnefoy J. Y., Defrance T., Peronne C., Menetrier C., Pene J., de Vries J.-E., Bancherau J. Human recombinant interleukin 4 induces normal B cells to produce soluble CD23/IgR binding factor analogous to that spontaneously released by lymphoblastoid B cell lines. Eur. J. Immunol 1988; 18: 117
  • Delespesse G. M., Sarfati M., Hofstetter H. Human IgE-binding factors. Immunol. Today 1989; 10: 159
  • Gordon J., Flores-Romo L., Cairns J. A., Millsum M. J., Lane P. J., Johnson G. D., McClennan I. C. M. CD23: a multifunctional receptor/lymphokine. Immunol. Today 1989; 10: 153
  • Amin A. R., Coico R. F., Finkelman F., Siskind G. W., Thorbecke G. J. Release of IgD-binding factor by T cells under the influence of interleukin 2, interleukin 4, or cross-linked IgD. Proc. Natl. Acad. Sci. U.S.A. 1988; 85: 9179
  • Fridman W. H., Gresser I., Bandu M. T., Aguet M., Neauport-Sautes C. Interferon enhances the expression of Fcγ receptors. J. Immunol 1980; 124: 2436
  • Daeron M., Yodoi J., Neauport-Sautes C., Moncuit J., Fridman W. H. Receptors for immunoglobulin isotypes (FcR) on murine T cells. I. Multiple FcR expression on T lymphocytes and hybridoma T cell clones. Eur. J. Immunol. 1985; 15: 662
  • Hoover R. G., Dieckgraefe B. H., Lynch R. G. T cells with Fc receptors for IgA: induction of T cells in vivo by purified IgA. J. Immunol 1981; 127: 1560
  • Mathur A., Lynch R. G. Increased Tγ and Tμ, cells in Ba1b/c mice with IgG and IgM plasmacytomas and hybridomas. J. Immunol 1986; 136: 521
  • Daeron M., Bonnerot C., Sandor M., Varin N., Hogarth P. M., Even J., Fridman W. H. Molecular mechanisms regulating the expression of murine T cell Fcγ receptor II. Mol. Immunol. 1988; 25: 1143
  • Brunati S., Moncuit J., Fridman W. H., Teillaud J.-L. Regulation of IgG production by suppressor FcγRII+ T hybridomas. Eur. J. Immunol 1990; 20: 55
  • Varin N., Sautes C., Galinha A., Even J., Hogarth P. M., Fridman W. H. Recombinant soluble receptors for the Fcγ portion inhibit antibody productio. in vitro, Eur. J. Immunol 1989; 19: 2263
  • Bonnerot C., Daeron M., Varin N., Amigorena S., Hogarth P. M., Even J., Fridman W. H. Methylation in the 5′ region of the murine βFcγR gene regulates the expression of the Fcγ receptor II. J. Immunol 1988; 141: 1026
  • Daeron M., Bonnerot C., Latour S., Benhamou M., Fridman W. H. The murine αFeγR gene product: identification, expression, and regulation. Mol. Immunol 1990; 27: 1181
  • Weinshank R. L., Luster A. D., Ravetch J. V. Function and regulation of a murine macrophage-specific IgG Fc receptor, FcγR-α. J. Exp. Med. 1988; 167: 1909
  • Yokota A., Kikutani H., Tanaka T., Sato R., Barsumian E. L., Suemura M., Kishimoto T. Two species of human FcR H (FcRII/CD23): tissue specific and interleukin-4 specific regulation of the gene expression. Cell 1988; 55: 611
  • Laszlo G., Dickler H. B. IL-4 induces loss of B lymphocyte FcγRII ligand binding capacity. J. Immunol 1988; 141: 3416
  • O'Garra A., Rigley K. P., Holman M., McLaughlin J. B., Klaus G. G. B cell stimulatory factor 1 reverses Fc receptor-mediated inhibition of B lymphocyte activation. Proc. Natl. Acad. Sci. U.S.A. 1987; 84: 6254
  • Amigorena S., Bonnerot C., Choquet D., Fridman W. H., Teillaud J.-L. FcγRII expression in resting and activated B lymphocytes. Eur. J. Immunol 1989; 19: 1379
  • Gordon J., Flores-Romo L., Cairns J. A., Millsum M. J., Lane P. J., Johanson G. D., McClennan I. C. CD23: a multifunctional receptor/lymphokine. Immunol. Today 1989; 10: 153
  • Gordon J., Webb A., Walker L., Guy G. R., Rowe M. Evidence for an association between CD23 and the low molecular weight B cell growth factor. Eur. J. Immunol. 1986; 16: 1627
  • Hivroz C., Valle A., Brouet J. C., Banchereau J., Grillot-Courvalin C. Regulation by inter-leukin-2 of CD23 expression of leukemic and normal B cells: comparison with interleukin-4. Eur. J. Immunol. 1989; 19: 1025
  • Letellier M., Sarfati M., Delespesse G. Mechanisms of formation of IgE-binding factors (soluble CD23). I. FcRII bearing B cells generate IgE-binding factors of different molecular weights. Mol. Immunol. 1989; 26: 1105
  • Monestier M., Bellon B., Manheimer A. J., Bona C. A. Rheumatoid factors. Immunochemical, molecular and regulatory properties. Ann. N. Y. Acad. Sci. 1986; 475: 106
  • Grabar P. Autoantibodies and physiological role of immunoglobulins. Immunol. Today 1983; 14: 337
  • Manheimer A., Bona C. Age-dependent isotype variation during secondary immune response in MRL-1pr mice producing auto-anti-γ-globulin. J. Exp. Med. 1985; 103: 105
  • St. Sinclair N. R. C., Panoskaltsis A. Rheumatoid factor and Fc signaling: a tale of two Cinderellas. Clin. Immunol. Immunopathol. 1989; 52: 133
  • Rajnavölgyi E., Kurucz I., Fazakas G Y., Sintar E., Laszlo G., Gergely J. In vivo manipulation of IgG2a production by isotype specific autoantibodies. Mol. Immunol. 1990; 27: 1241

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