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. 1987 Mar 1;165(3):750–762. doi: 10.1084/jem.165.3.750

Lamin B autoantibodies in sera of certain patients with systemic lupus erythematosus

PMCID: PMC2188284  PMID: 3546581

Abstract

Sera from four patients with systemic lupus erythematosus containing antibodies that yield nuclear rim staining of HEp-2 cells by indirect immunofluorescence were identified and characterized. Each serum contained autoantibodies reacting strongly with lamin B on western blots. One of the four sera displayed weaker reactivity with lamins A and C, while the other three displayed only minimal reactivity with lamins A and C. Titers of antilamin antibodies ranged from 1:1,250 to 1:36,250. Two of the sera also reacted at a dilution of 1:20 with cytoplasmic filaments of PTK-2 cells, suggesting that a small fraction of the autoantibodies in these sera may bind to alpha-helical domains of the lamins that are homologous to those of intermediate filaments. The majority of the antilamin antibodies in these patients' sera are specific for portions of the lamin B molecule that are not homologous to lamins A and C, however. The findings suggest that autoantibodies to the nuclear lamina may, in some instances, be responsible for a rim pattern in the fluorescent antinuclear antibody assay. In addition, autoantibodies to the nuclear lamina in sera of certain patients with systemic lupus erythematosus may be useful for defining the molecular structure and biological functions of lamin B, as well as for studying mechanisms of autoimmunity.

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Selected References

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  1. Aaronson R. P., Blobel G. Isolation of nuclear pore complexes in association with a lamina. Proc Natl Acad Sci U S A. 1975 Mar;72(3):1007–1011. doi: 10.1073/pnas.72.3.1007. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Blobel G. Gene gating: a hypothesis. Proc Natl Acad Sci U S A. 1985 Dec;82(24):8527–8529. doi: 10.1073/pnas.82.24.8527. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Blobel G., Potter V. R. Nuclei from rat liver: isolation method that combines purity with high yield. Science. 1966 Dec 30;154(3757):1662–1665. doi: 10.1126/science.154.3757.1662. [DOI] [PubMed] [Google Scholar]
  4. Burke B., Tooze J., Warren G. A monoclonal antibody which recognises each of the nuclear lamin polypeptides in mammalian cells. EMBO J. 1983;2(3):361–367. doi: 10.1002/j.1460-2075.1983.tb01431.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Conner G. E., Nelson D., Wisniewolski R., Lahita R. G., Blobel G., Kunkel H. G. Protein antigens of the RNA-protein complexes detected by anti-SM and anti-RNP antibodies found in serum of patients with systemic lupus erythematosus and related disorders. J Exp Med. 1982 Nov 1;156(5):1475–1485. doi: 10.1084/jem.156.5.1475. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Davis L. I., Blobel G. Identification and characterization of a nuclear pore complex protein. Cell. 1986 Jun 6;45(5):699–709. doi: 10.1016/0092-8674(86)90784-1. [DOI] [PubMed] [Google Scholar]
  7. Dwyer N., Blobel G. A modified procedure for the isolation of a pore complex-lamina fraction from rat liver nuclei. J Cell Biol. 1976 Sep;70(3):581–591. doi: 10.1083/jcb.70.3.581. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Fisher D. Z., Chaudhary N., Blobel G. cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins. Proc Natl Acad Sci U S A. 1986 Sep;83(17):6450–6454. doi: 10.1073/pnas.83.17.6450. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Franke W. W. Structure, biochemistry, and functions of the nuclear envelope. Int Rev Cytol. 1974;Suppl 4:71–236. [PubMed] [Google Scholar]
  10. Friou G. J. Antinuclear antibodies: diagnostic significance and methods. Arthritis Rheum. 1967 Apr;10(2):151–159. doi: 10.1002/art.1780100210. [DOI] [PubMed] [Google Scholar]
  11. Gerace L., Blobel G. Nuclear lamina and the structural organization of the nuclear envelope. Cold Spring Harb Symp Quant Biol. 1982;46(Pt 2):967–978. doi: 10.1101/sqb.1982.046.01.090. [DOI] [PubMed] [Google Scholar]
  12. Gerace L., Blobel G. The nuclear envelope lamina is reversibly depolymerized during mitosis. Cell. 1980 Jan;19(1):277–287. doi: 10.1016/0092-8674(80)90409-2. [DOI] [PubMed] [Google Scholar]
  13. Gerace L., Blum A., Blobel G. Immunocytochemical localization of the major polypeptides of the nuclear pore complex-lamina fraction. Interphase and mitotic distribution. J Cell Biol. 1978 Nov;79(2 Pt 1):546–566. doi: 10.1083/jcb.79.2.546. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Gonzalez E. N., Rothfield N. F. Immunoglobulin class and pattern of nuclear fluorescence in systemic lupus erythematosus. N Engl J Med. 1966 Jun 16;274(24):1333–1338. doi: 10.1056/NEJM196606162742401. [DOI] [PubMed] [Google Scholar]
  15. Henderson D., Weber K. Immuno-electron microscopical identification of the two types of intermediate filaments in established epithelial cells. Exp Cell Res. 1981 Apr;132(2):297–311. doi: 10.1016/0014-4827(81)90106-3. [DOI] [PubMed] [Google Scholar]
  16. Hunkapiller M. W., Lujan E., Ostrander F., Hood L. E. Isolation of microgram quantities of proteins from polyacrylamide gels for amino acid sequence analysis. Methods Enzymol. 1983;91:227–236. doi: 10.1016/s0076-6879(83)91019-4. [DOI] [PubMed] [Google Scholar]
  17. Kay R. R., Johnston I. R. The nuclear envelope: current problems of structure and of function. Subcell Biochem. 1973;2(2):127–167. [PubMed] [Google Scholar]
  18. Krohne G., Benavente R. The nuclear lamins. A multigene family of proteins in evolution and differentiation. Exp Cell Res. 1986 Jan;162(1):1–10. doi: 10.1016/0014-4827(86)90421-0. [DOI] [PubMed] [Google Scholar]
  19. Krohne G., Debus E., Osborn M., Weber K., Franke W. W. A monoclonal antibody against nuclear lamina proteins reveals cell type-specificity in Xenopus laevis. Exp Cell Res. 1984 Jan;150(1):47–59. doi: 10.1016/0014-4827(84)90700-6. [DOI] [PubMed] [Google Scholar]
  20. Lehner C. F., Fürstenberger G., Eppenberger H. M., Nigg E. A. Biogenesis of the nuclear lamina: in vivo synthesis and processing of nuclear protein precursors. Proc Natl Acad Sci U S A. 1986 Apr;83(7):2096–2099. doi: 10.1073/pnas.83.7.2096. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Lerner M. R., Steitz J. A. Antibodies to small nuclear RNAs complexed with proteins are produced by patients with systemic lupus erythematosus. Proc Natl Acad Sci U S A. 1979 Nov;76(11):5495–5499. doi: 10.1073/pnas.76.11.5495. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Maul G. G., Baglia F. A., Newmeyer D. D., Ohlsson-Wilhelm B. M. The major 67 000 molecular weight protein of the clam oocyte nuclear envelope is lamin-like. J Cell Sci. 1984 Apr;67:69–85. doi: 10.1242/jcs.67.1.69. [DOI] [PubMed] [Google Scholar]
  23. McKeon F. D., Kirschner M. W., Caput D. Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature. 1986 Feb 6;319(6053):463–468. doi: 10.1038/319463a0. [DOI] [PubMed] [Google Scholar]
  24. McKeon F. D., Tuffanelli D. L., Fukuyama K., Kirschner M. W. Autoimmune response directed against conserved determinants of nuclear envelope proteins in a patient with linear scleroderma. Proc Natl Acad Sci U S A. 1983 Jul;80(14):4374–4378. doi: 10.1073/pnas.80.14.4374. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Miake-Lye R., Kirschner M. W. Induction of early mitotic events in a cell-free system. Cell. 1985 May;41(1):165–175. doi: 10.1016/0092-8674(85)90071-6. [DOI] [PubMed] [Google Scholar]
  26. Ottaviano Y., Gerace L. Phosphorylation of the nuclear lamins during interphase and mitosis. J Biol Chem. 1985 Jan 10;260(1):624–632. [PubMed] [Google Scholar]
  27. Reeves W. H. Use of monoclonal antibodies for the characterization of novel DNA-binding proteins recognized by human autoimmune sera. J Exp Med. 1985 Jan 1;161(1):18–39. doi: 10.1084/jem.161.1.18. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Senecal J. L., Rothfield N. F., Oliver J. M. Immunoglobulin M autoantibody to vimentin intermediate filaments. J Clin Invest. 1982 Mar;69(3):716–721. doi: 10.1172/JCI110500. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Staufenbiel M., Deppert W. Different structural systems of the nucleus are targets for SV40 large T antigen. Cell. 1983 May;33(1):173–181. doi: 10.1016/0092-8674(83)90346-x. [DOI] [PubMed] [Google Scholar]
  30. Tan E. M. Autoantibodies to nuclear antigens (ANA): their immunobiology and medicine. Adv Immunol. 1982;33:167–240. doi: 10.1016/s0065-2776(08)60836-6. [DOI] [PubMed] [Google Scholar]
  31. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Wedrychowski A., Ward W. S., Schmidt W. N., Hnilica L. S. Chromium-induced cross-linking of nuclear proteins and DNA. J Biol Chem. 1985 Jun 10;260(11):7150–7155. [PubMed] [Google Scholar]
  33. Wolin S. L., Steitz J. A. The Ro small cytoplasmic ribonucleoproteins: identification of the antigenic protein and its binding site on the Ro RNAs. Proc Natl Acad Sci U S A. 1984 Apr;81(7):1996–2000. doi: 10.1073/pnas.81.7.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]

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