Skip to main content
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1987 Jan 1;104(1):1–7. doi: 10.1083/jcb.104.1.1

A monoclonal antibody against the nucleus reveals the presence of a common protein in the nuclear envelope, the perichromosomal region, and cytoplasmic vesicles

PMCID: PMC2117027  PMID: 3539946

Abstract

A monoclonal antibody that recognizes antigenic determinants on the nucleus of cultured mammalian cells was isolated. Immunofluorescence studies using this antibody showed that the recognized antigen was present not only on the nucleus but also in cytoplasmic vesicles of interphase cells and in the perichromosomal region of mitotic cells. Premature chromosome condensation analysis showed that the reactive site for this monoclonal antibody could be detected in the perichromosomal region during the G2 and M phases, but not during the G1 and S phases. Finally, immunoblot analysis showed that this monoclonal antibody prepared against the nucleus recognized a protein of approximately 40 kD both in the cytoplasm and in the perichromosomal regions.

Full Text

The Full Text of this article is available as a PDF (2.9 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Burnette W. N. "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate--polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal Biochem. 1981 Apr;112(2):195–203. doi: 10.1016/0003-2697(81)90281-5. [DOI] [PubMed] [Google Scholar]
  2. Chaly N., Bladon T., Setterfield G., Little J. E., Kaplan J. G., Brown D. L. Changes in distribution of nuclear matrix antigens during the mitotic cell cycle. J Cell Biol. 1984 Aug;99(2):661–671. doi: 10.1083/jcb.99.2.661. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Daskal Y., Mace M., Jr, Busch H. Demonstration of membranous patches on isolated chromosomes. Exp Cell Res. 1978 Feb;111(2):472–475. doi: 10.1016/0014-4827(78)90195-7. [DOI] [PubMed] [Google Scholar]
  4. 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]
  5. 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]
  6. 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]
  7. Ito S., Dan K., Goodenough D. Ultrastructure and 3H-thymidine incorporation by chromosome vesicles in sea urchin embryos. Chromosoma. 1981;83(4):441–453. doi: 10.1007/BF00328271. [DOI] [PubMed] [Google Scholar]
  8. Jost E., Johnson R. T. Nuclear lamina assembly, synthesis and disaggregation during the cell cycle in synchronized HeLa cells. J Cell Sci. 1981 Feb;47:25–53. doi: 10.1242/jcs.47.1.25. [DOI] [PubMed] [Google Scholar]
  9. Köhler G., Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature. 1975 Aug 7;256(5517):495–497. doi: 10.1038/256495a0. [DOI] [PubMed] [Google Scholar]
  10. Köhler G., Milstein C. Derivation of specific antibody-producing tissue culture and tumor lines by cell fusion. Eur J Immunol. 1976 Jul;6(7):511–519. doi: 10.1002/eji.1830060713. [DOI] [PubMed] [Google Scholar]
  11. Lohka M. J., Masui Y. Roles of cytosol and cytoplasmic particles in nuclear envelope assembly and sperm pronuclear formation in cell-free preparations from amphibian eggs. J Cell Biol. 1984 Apr;98(4):1222–1230. doi: 10.1083/jcb.98.4.1222. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. McKeon F. D., Tuffanelli D. L., Kobayashi S., Kirschner M. W. The redistribution of a conserved nuclear envelope protein during the cell cycle suggests a pathway for chromosome condensation. Cell. 1984 Jan;36(1):83–92. doi: 10.1016/0092-8674(84)90076-x. [DOI] [PubMed] [Google Scholar]
  13. Newport J. W., Kirschner M. W. Regulation of the cell cycle during early Xenopus development. Cell. 1984 Jul;37(3):731–742. doi: 10.1016/0092-8674(84)90409-4. [DOI] [PubMed] [Google Scholar]
  14. Sillar R., Young B. D. A new method for the preparation of metaphase chromosomes for flow analysis. J Histochem Cytochem. 1981 Jan;29(1):74–78. doi: 10.1177/29.1.6162882. [DOI] [PubMed] [Google Scholar]
  15. Sugawa H., Imamoto N., Wataya-Kaneda M., Uchida T. Foreign protein can be carried into the nucleus of mammalian cell by conjugation with nucleoplasmin. Exp Cell Res. 1985 Aug;159(2):419–429. doi: 10.1016/s0014-4827(85)80015-x. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES