Interaction of antibodies against nuclear envelope-associated proteins from rat liver nuclei with rodent and human cells

Ely, Susan; D’Arcy, Allan; Jost, Erich

doi:10.1016/0014-4827(78)90455-x

Cited by 64 publications

(16 citation statements)

References 13 publications

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“…The immunofluorescence results above are similar to those of previous reports that used antibodies to nuclear lamins derived from heterologous immunization (6,17,18). To test the possibility that the target of these autoantibodies was the nuclear lamins, we isolated a crude preparation of nuclear matrices that could be prepared rapidly by a solid-phase extraction of CHO cells attached to plastic dishes.…”

Section: Immunocytochemicalsupporting

confidence: 81%

Autoimmune response directed against conserved determinants of nuclear envelope proteins in a patient with linear scleroderma.

McKeon¹,

Tuffanelli²,

Fukuyama³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

113

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We have studied the autoantibodies in the serum of a patient with linear scleroderma that specifically recognize the nuclear envelope of cultured cells. These antibodies bind to conserved determinants of nuclear lamins, the predominant mammalian nuclear envelope proteins. Of the three mammalian nuclear lamin proteins (P70, P68, and P60), only P70 and P60 bind the autoantibodies. In addition, two proteins of the Drosophila embryonic nuclear matrix, P70 and P68, bind these autoantibodies. We have used nuclear matrices to isolate the autoantibodies from the patient's serum that react to the nuclear lamins. At least three different IgG heavy chains were found to be involved in this autoimmune response to nuclear lamins, indicating that this response is not due to the expansion of a single B-cell clone.A strong correlation exists between systemic rheumatic diseases and the presence of circulating autoantibodies to proteinnucleic acid complexes (1). The targets of these autoantibodies include nuclear ribonucleoprotein particles (2), nucleosomes (3), nucleoli (4), kinetochores (5), and others. The range of targets for particular disease syndromes are often limited; for example, systemic lupus erythematosis is often associated with autoantibodies to nuclear ribonucleoprotein particles (2), whereas most scleroderma CREST patients produce autoantibodies to centromeric regions of chromosomes (kinetochores; ref. 5). Surprisingly, little is known of the autoimmune responses or their targets on a molecular level.In an attempt to associate the immunofluorescence pattern of sera from patients with specific autoimmune diseases, we discovered a high-titer serum directed against the nuclear envelope in a patient with linear scleroderma. We designate this serum as LS-1. We have chosen here to characterize this autoimmune response more precisely by identifying the antigens recognized by this serum and by determining the nature and complexity of the antibody response. We have found that this autoimmune response is polyclonal and directed against two of the three predominant polypeptides of the nuclear envelope, known as nuclear lamins (6).Using immunofluorescence and immunotransfers of NaDodSO4 gels, we also have detected nuclear lamins in Drosophila melanogaster embryonic nuclear matrices. This demonstrates that nuclear lamins are present in invertebrates and that these autoantibodies from LS-1 serum must be directed against highly conserved determinants. at 26°C in Echalier's medium (7).Immunofluorescence Microscopy. CHO and Kc cells were grown on glass coverslips (12-mm diameter, Corning), fixed in 1% formaldehyde in phosphate-buffered saline (Pi/NaCl) for 5 min at 22°C, and made permeable to antibodies by washing in 0.1% Triton X-100 (Sigma) in Pi/NaCl. The cells were first exposed to LS-1 serum diluted 1:200 and subsequently to a rhodamine-conjugated goat anti-human IgG (Cappel Laboratories, Cochranville, PA). Cells were photographed with a Zeiss photomicroscope with a X 100 planapo objective.Immunohistochemical Microsc...

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Section: Immunocytochemicalsupporting

confidence: 81%

Autoimmune response directed against conserved determinants of nuclear envelope proteins in a patient with linear scleroderma.

McKeon¹,

Tuffanelli²,

Fukuyama³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

113

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“…First, structural proteins at the nuclear periphery, most probably the lamins, may determine the structure of interphase chromatin because they interact with DNA (15,20,32). Second, the dissociation of the lamins correlates with chromosome condensation at the onset of mitosis and meiosis, and the lamins reassociate before reconstruction of the nuclear envelope and the reestablishment of the interphase organizational state of the chromatin (9,16,28,42). Third, specific loci of Drosophila polytene chromosomes have been found to be associated with the nuclear envelope in vivo at discrete points (34).…”

Section: Kmentioning

confidence: 99%

Nuclear envelope localization of an adenovirus tumor antigen maintains the integrity of cellular DNA.

White¹,

Blose²,

Stillman³

1984

Mol. Cell. Biol.

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The adenovirus early-region lB 19,000-molecular-weight tumor antigen is required for oncogenic transformation of cells by adenovirus. We have demonstrated that this tumor antigen is located in the nuclear envelope of infected and transformed cells and that a fraction of the protein within the nuclear envelope is associated with the nuclear lamina. During cell division in the transformed cells, the nuclear envelope containing the tumor antigen dissociates at metaphase and then reforms around the separated daughter chromosomes at telophase. Adenovirus mutants carrying lesions in the gene encoding this tumor antigen cause degradation of host cell chromosomal DNA, and in these mutants, the intracellular localization of the 19,000-dalton protein is altered. These results demonstrate that components of the nuclear envelope function in the organization of chromatin in infected and transformed cells and that a virus-encoded protein plays a critical role in this process.

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“…Ely et al, 1978) have indicated that the three lamins are distributed evenly upon the inner face of the nuclear envelope. Bar = 20 1tim.…”

Section: Immunofluorescence Microscopymentioning

confidence: 99%

A monoclonal antibody which recognises each of the nuclear lamin polypeptides in mammalian cells.

Burke¹,

Tooze²,

Warren³

1983

The EMBO Journal

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A monoclonal IgM has been characterised which recognises the nuclear lamins in all mammalian cells tested. In immunoblotting experiments using both one‐ and two‐dimensional gels it recognises lamins A, B and C. The common antigenic determinant lies on a proteolytic fragment of 46,000 daltons which can be generated from each lamin polypeptide by treatment with chymotrypsin. In immunofluorescence experiments on whole cells and thin frozen sections, the antibody labelled only the nuclear envelope and not the nuclear interior. During mitosis, labelling was found dispersed throughout the cell cytoplasm. By immunoelectron microscopy using the antibody and protein A‐gold, only the nucleoplasmic side of the nuclear envelope (the nuclear lamina) was labelled, but there was no labelling of the nuclear pores.

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Interaction of antibodies against nuclear envelope-associated proteins from rat liver nuclei with rodent and human cells

Cited by 64 publications

References 13 publications

Autoimmune response directed against conserved determinants of nuclear envelope proteins in a patient with linear scleroderma.

Autoimmune response directed against conserved determinants of nuclear envelope proteins in a patient with linear scleroderma.

Nuclear envelope localization of an adenovirus tumor antigen maintains the integrity of cellular DNA.

A monoclonal antibody which recognises each of the nuclear lamin polypeptides in mammalian cells.

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