Monoclonal IgM Rheumatoid Factors Generated from Synovial B Cells of Rheumatoid Arthritis Patients React with β₂-Microglobulin Monoclonal RF React with β₂m

References

• Waaler E. On occurrence of a factor in human serum activating the specific agglutination of sleep blood corpuscles. Acta Path Microbiol Scand 1940; 17: 172–188
   Google Scholar
• Schmid F. R., Roitt I. M., Rocha M. J. Complement fixation by a two-component antibody system: immunoglobulin G and immunoglobulin M antiglobulin (rheumatoid factor) paradoxical effect related to immunoglobulin G concentration. J Exp Med 1970; 132: 673–693
   PubMed Web of Science ®Google Scholar
• Zvaifler N. J. Rheumatoid factor and the fixation of complement. Part I.V., Possisble biological functions of rheumatoid factor in synovial space. Ann Ny Acad Sciences 1969; 168: 146–160
   PubMedGoogle Scholar
• Tanimoto K., Cooper N. R., Johnson J. S., Vaughn J. H. Complement fixation by rheumatoid factor. J Clin Invest 1975; 55: 437–455
   PubMed Web of Science ®Google Scholar
• Roosnek E., Lanzavecchia A. Efficient and selective presentation of antigen-antibody complexes by rheumatoid factor B cells. J Exp Med 1991; 173: 487–489
   PubMed Web of Science ®Google Scholar
• Tighe H., Chen P. P., Tucker R., Kipps T. J., Roudier J., Jirik F. R., Carson D. Function of B cells expressing a human immunoglobulin M rheumatoid factor autoantibody in transgenic mice. J Exp Med 1993; 177: 109–118
   PubMed Web of Science ®Google Scholar
• Messner R. P., Laxdal T., Quie P. G., Williams R. C., Jr. Serum opsonin, bacteria, and polymophonuclear leukocyte interactions in subacute bacterial endocarditis. Anti-γ-globulin factors and their interaction with specific opsonins. J Clin Invest 1968; 47: 1109–1120
   PubMedGoogle Scholar
• DeHoratius R. J., Williams R. C., Jr. Rheumatoid factor accentuation of pulmonary lesions associated with experimental diffuse proliferative lung disease. Arthritis Rheum 1972; 15: 293–301
   PubMedGoogle Scholar
• Clarkson A. B., Mellow G. H. Rheumatoid factor-like immunoglobulin M protects previously uninfected rat pups and dams from. Trypanosoma lewisi. Science 1981; 214: 186–188
   Google Scholar
• King R. A., Messner R. P., Williams R. C., Jr. Human lymphocyte transformation induced by anti-gamma globulin factors. Arthritis Rheum 1969; 12: 597–607
   PubMedGoogle Scholar
• Hobbs M. V., Morgan E. L., Baker N. L., Weigle W. O. Regulation of antibody responses by rheumatoid factor I polyclonal activation of human B cells by rheumatoid factor-containing preparations from seropositive plasma. J Immunol 1985; 134: 223–229
   PubMedGoogle Scholar
• Williams R. C., Jr, Malone C. C., Tsuchiya N. Rheumatoid factors from patients with rheumatoid arthritis react with β2 microglobulin. J Immunol 1992; 149: 1104–1113
   PubMed Web of Science ®Google Scholar
• Williams R. C., Jr, Malone C. C., Harley J. B. Rheumatoid factors from patients with rheumatoid arthritis react with tryptophane 60 and 95, Lysine 58 and arginine 97 on human β2 microglobulin. Arthritis & Rheum 1993; 36: 916–926
   PubMedGoogle Scholar
• Parker K. C., Wiley D. C. Over expression of native human β2-microglobulin in Escherichia coli and its purification. Gene 1989; 83: 117–124
   PubMedGoogle Scholar
• Robbins D. L., Kenny T. P., Larrick J. W., Wistar R., Jr. Production of human monocolonal rheumatoid factor secreting hybridomas derived from rheumatoid synovial cells. Med Sci Res 1989; 17: 157–158
   Google Scholar
• Burastero S. E., Casali P., Wilder R. L., 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: 1979–1992
   PubMed Web of Science ®Google Scholar
• Williams R. C., Jr., Malone C. C., Casali P. Heteroclitic polyclonal and monoclonal anti-Gm(a) and anti-Gm(g) human rheumatoid factors react with epitopes induced in Gm(a-), Gm(g-) IgG by interaction with antigen or by nonspecific aggregation. A possible mechanism for the in vivo generation of rheumatoid factors. J Immunol 1992; 149: 1817–1824
   PubMedGoogle Scholar
• Geysen H. M., Rodda S. J., Mason T. J., Tribbick G., Schoofs P. G. Strategies for epitope analysis using peptide synthesis. J Immunol Methods 1987; 102: 259–274
   PubMed Web of Science ®Google Scholar
• Getzoff E. D., Geysen H. M., Rodda S. J., Alexander H., Tainer J. A., Lerner R. A. Mechanisms of antibody binding to protein. Science 1987; 235: 1191–1196
   PubMed Web of Science ®Google Scholar
• Williams R. C., Jr., Kievit E., Tsuchiya N., Malone C. C., Hutt-Fletcher L. Differential mapping of Fcγ-binding and monoclonal-antibody-reactive epitopes on gE, the Feγ-binding glycoprotein of herpes simplex virus type 1. J Immunol 1992; 149: 2415–2427
   PubMed Web of Science ®Google Scholar
• Spangler B. D. Binding to native proteins by antipeptide monoclonal antibodies. J Immunol 1991; 146: 1591–1595
   PubMed Web of Science ®Google Scholar
• Laver W. G., Air G. M., Webster R. G., Smith-Gill S. J. Epitopes on protein antigens: misconceptions and realities. Cell 1990; 61: 553–556
   PubMed Web of Science ®Google Scholar
• Bjorkman P. J., Saper M. A., Samraoui B., Bennett W. S., Strominger J. L., Wiley D. C. Structure of the human class I histocompatibility antigen, HLA-A2. Nature 1987; 328: 506–512
   Google Scholar
• Bjorkman P. J., Saper M. A., Samraoui B., Bennett W. S., Strominger J. L., Wiley D. C. The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens. Nature 1987; 329: 512–518
   PubMed Web of Science ®Google Scholar
• Saper M. A., Bjorkman P. J., Wiley D. C. Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 ÅA resolution. J Mol Biol 1991; 219: 277–319
   PubMed Web of Science ®Google Scholar
• Stage D. E., Mannik M. Rheumatoid factors in rheumatoid arthritis. Bull Rheum Dis 1972; 23: 720–725
   PubMedGoogle Scholar
• Williams R. C., Jr. Rheumatoid factors. Human Pathol 1983; 14: 386–391
   PubMedGoogle Scholar
• Carson D. A., Chen P. P., Kipps T. J. New roles for rheumatoid factor. J Clin Invest 1991; 87: 379–383
   PubMed Web of Science ®Google Scholar
• Harboe M. Relation between Gm types and hemagglutinating substance in rheumatoid sera. Acta Path Microbiol Scand 1960; 50: 89–105
   PubMedGoogle Scholar
• Fudenberg H. H., Kunkel H. G. Specificity of the reaction between rheumatoid factors and gamma globulin. J Exp Med 1961; 114: 257–278
   PubMedGoogle Scholar
• Osterland C. K., Harboe M., Kunkel H. G. Anti-γ-globulin factors in human sera revealed by enzyme splitting of anti-Rh antibodies. Vox Sang 1963; 8: 133–152
   PubMedGoogle Scholar
• Harboe M., Rau B., Aho K. Properties of various anti-γ-globulin factors in human sera. J Exp Med 1965; 121: 503–519
   PubMed Web of Science ®Google Scholar
• Williams R. C., Jr. Heterogeneity of L-chain sites on Bence-Jones proteins reacting with anti-gamma-globulin factors. Proc Natl Acad Sci 1964; 52: 60–64
   PubMedGoogle Scholar
• Robbins D. L., Skilling J., Benisek W. F., Wistar R., Jr. Estimation of the relative avidity of 19S IgM rheumatoid factor secreted by rheumatoid synovial cells for human IgG subclasses. Arthritis Rheum 1986; 29: 722–729
   PubMedGoogle Scholar
• Robbins D. L., Wistar R., Jr. Comparative specificities of serum and synovial cell 19S IgM rheumatoid factors in rheumatoid arthritis. J Rheumatology 1985; 12: 437–443
   PubMedGoogle Scholar
• Hoffman W. L., Goldberg M. S., Smiley J. D. Immunoglobulin G3 subclass production by rheumatoid synovial tissue cultures. J Clin Invest 1982; 69: 136–144
   PubMedGoogle Scholar
• Allen J. C., Kunkel H. G. Hidden rheumatoid factors with specificity for native γ-globulins. Arthritis Rheum 1966; 9: 758–768
   PubMed Web of Science ®Google Scholar
• Gaarder P. I., Natvig J. B. Hidden rheumatoid factors reaching with “non a” and other antigens of native autologous IgG. J Immunol 1970; 105: 928–937
   PubMedGoogle Scholar
• Sasso E. H., Barber C. V., Nardella F. A., Yount W. J., Mannik M. Antigenic specificities of human monoclonal and polyclonal IgM rheumatoid factors. The Cγ2-Oγ3 interface region contains the major determinants. J Immunol 1988; 140: 3098–3107
   PubMed Web of Science ®Google Scholar
• Ledford D. K., Goni F., Pizzolato M., Franklin E. C., Solomon A., Frangione F. Preferential association of KIIIb light chains with monoclonal human IgM autoantibodies. J Immunol 1983; 131: 1322–1325
   PubMedGoogle Scholar
• Radoux V., Chen P. P., Sorge J. A., Carson D. A. A conserved human Vk gene directly encodes rheumatoid factor light chains. J Exp Med 1986; 164: 2119–2124
   PubMed Web of Science ®Google Scholar
• Chen P. P., Albrandt K., Kipps T. J., Radoux V., Liu F. T., Carson D. A. Isolation and characterization of human VK III germ-line genes. Implications for the molecular basis of human VK III light chain diversity. J Immunol 1987; 139: 1727–1733
   PubMedGoogle Scholar
• Chen P. P., Liu M. F., Glass C. A., Sinha S., Kipps T. J., Carson D. A. Characterization of two immunoglobulin VH genes that are homologous to human rheumatoid factors. Arthritis Rheum 1989; 32: 72–76
   PubMedGoogle Scholar
• Victor K. D., Randen I., Thomspon K., Forre O., Natvig J. B., Fu S. M., Capra J. D. Rheumatoid factors isolated from patients with autoimmune disorders are derived from germline genes distinct from those encoding the Wa, Po, and Bla cross-reactive idiotypes. J Clin Invet 1991; 87: 1603–1613
   PubMed Web of Science ®Google Scholar
• Weisbart R. H., Wong A. L., Noritake D., Kalena A., Chan G., Ruland C., Chin E., Chin I. S.Y., Rosenblatt J. D. The rheumatoid factor reactivity of a human IgG monoclonal autoantibody is encoded by a variant VK II L chain gene. J Immunol 1991; 147: 2795–2801
   PubMedGoogle Scholar
• Aman P., Ehlin-Henriksson B., Klein G. Epstein-Barr virus susceptibility of normal human B lymphocyte populations. J Exp Med 1984; 159: 208–220
   PubMed Web of Science ®Google Scholar
• Tosato G., Blaese R. M., Yarchoan R. Relationship between immunoglobulin production and immortalization by Epstein Barr virus. J Immunol 1985; 135: 959–964
   PubMed Web of Science ®Google Scholar
• Bardwick P. A., Bluestein H. G., Zvaifler N. J., Depper J. M., Seegmiller J. E. Altered regulation of Epstein-Barr virus induced lymphoblast proliferation in rheumatoid arthritis lymphoid cells. Arthritis Rheum 1980; 23: 626–632
   PubMed Web of Science ®Google Scholar
• Williams R. C., Malone C. Antigenic epitopes on β2m reacting with monoclonal antibodies. J Lab & Clin Med 1993; 121: 805–820, In press
   PubMedGoogle Scholar