Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1986 Oct;83(19):7282–7286. doi: 10.1073/pnas.83.19.7282

A cell surface desmosome-associated component: identification of tissue-specific cell adhesion molecule.

J C Jones, K M Yokoo, R D Goldman
PMCID: PMC386700  PMID: 3532108

Abstract

Autoantibodies in the serum of patients suffering the blistering skin disease pemphigus vulgaris recognize a 140-kDa glycoprotein (GP) present in enriched fractions of bovine tongue epidermal desmosomes. Immunofluorescence observations of cryostat sections of bovine tongue epidermis reveal that affinity-purified rabbit antibodies to the 140-kDa GP generate a punctate intercellular stain that is similar to that generated by antibodies directed against a desmosome plaque component (desmoplakin). In cultured mouse keratinocytes, the antibodies against 140-kDa GP recognize desmosomes along areas of cell-cell contact. Double immunofluorescence of cultured keratinocytes with these antibodies and a desmoplakin antiserum reveals that the antibodies against the 140-kDa GP stain a single fluorescent line along areas of cell-cell contact. This single fluorescent line lies between double fluorescent lines generated by the desmoplakin antiserum. Immunogold ultrastructural localization reveals that the 140-kDa antigen is localized not only along the intercellular area of the desmosome but also is found along the whole epidermal cell surface. The antibodies to the 140-kDa GP are able to induce a disruption of cell-cell contact in cultured keratinocytes that possess desmosomes. We propose that the 140-kDa GP is a cell adhesion molecule (CAM). Furthermore we discuss the heterogeneity of desmosomes in the light of our findings that antibodies against the 140-kDa GP recognize specific stratified squamous epithelial tissues.

Full text

PDF
7282

Images in this article

7283Image
on p.7283
7283Image
on p.7283
7283Image
on p.7283
7283Image
on p.7283
7283Image
on p.7283
7284Image
on p.7284
7284Image
on p.7284
7284Image
on p.7284
7285Image
on p.7285
7285Image
on p.7285
7286Image
on p.7286

Selected References

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

  1. Cohen S. M., Gorbsky G., Steinberg M. S. Immunochemical characterization of related families of glycoproteins in desmosomes. J Biol Chem. 1983 Feb 25;258(4):2621–2627. [PubMed] [Google Scholar]
  2. Cowin P., Mattey D., Garrod D. Identification of desmosomal surface components (desmocollins) and inhibition of desmosome formation by specific Fab'. J Cell Sci. 1984 Aug;70:41–60. doi: 10.1242/jcs.70.1.41. [DOI] [PubMed] [Google Scholar]
  3. Edelman G. M. Cell adhesion molecules. Science. 1983 Feb 4;219(4584):450–457. doi: 10.1126/science.6823544. [DOI] [PubMed] [Google Scholar]
  4. Franke W. W., Kapprell H. P., Mueller H. Isolation and symmetrical splitting of desmosomal structures in 9 M urea. Eur J Cell Biol. 1983 Nov;32(1):117–130. [PubMed] [Google Scholar]
  5. Franke W. W., Moll R., Mueller H., Schmid E., Kuhn C., Krepler R., Artlieb U., Denk H. Immunocytochemical identification of epithelium-derived human tumors with antibodies to desmosomal plaque proteins. Proc Natl Acad Sci U S A. 1983 Jan;80(2):543–547. doi: 10.1073/pnas.80.2.543. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gorbsky G., Steinberg M. S. Isolation of the intercellular glycoproteins of desmosomes. J Cell Biol. 1981 Jul;90(1):243–248. doi: 10.1083/jcb.90.1.243. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hennings H., Michael D., Cheng C., Steinert P., Holbrook K., Yuspa S. H. Calcium regulation of growth and differentiation of mouse epidermal cells in culture. Cell. 1980 Jan;19(1):245–254. doi: 10.1016/0092-8674(80)90406-7. [DOI] [PubMed] [Google Scholar]
  8. Hyafil F., Morello D., Babinet C., Jacob F. A cell surface glycoprotein involved in the compaction of embryonal carcinoma cells and cleavage stage embryos. Cell. 1980 Oct;21(3):927–934. doi: 10.1016/0092-8674(80)90456-0. [DOI] [PubMed] [Google Scholar]
  9. Jones J. C., Arnn J., Staehelin L. A., Goldman R. D. Human autoantibodies against desmosomes: possible causative factors in pemphigus. Proc Natl Acad Sci U S A. 1984 May;81(9):2781–2785. doi: 10.1073/pnas.81.9.2781. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Jones J. C., Goldman A. E., Steinert P. M., Yuspa S., Goldman R. D. Dynamic aspects of the supramolecular organization of intermediate filament networks in cultured epidermal cells. Cell Motil. 1982;2(3):197–213. doi: 10.1002/cm.970020302. [DOI] [PubMed] [Google Scholar]
  11. Jones J. C., Yokoo K. M., Goldman R. D. Further analysis of pemphigus autoantibodies and their use in studies on the heterogeneity, structure, and function of desmosomes. J Cell Biol. 1986 Mar;102(3):1109–1117. doi: 10.1083/jcb.102.3.1109. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Koulu L., Kusumi A., Steinberg M. S., Klaus-Kovtun V., Stanley J. R. Human autoantibodies against a desmosomal core protein in pemphigus foliaceus. J Exp Med. 1984 Nov 1;160(5):1509–1518. doi: 10.1084/jem.160.5.1509. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  14. Mueller H., Franke W. W. Biochemical and immunological characterization of desmoplakins I and II, the major polypeptides of the desmosomal plaque. J Mol Biol. 1983 Feb 5;163(4):647–671. doi: 10.1016/0022-2836(83)90116-x. [DOI] [PubMed] [Google Scholar]
  15. Olmsted J. B. Affinity purification of antibodies from diazotized paper blots of heterogeneous protein samples. J Biol Chem. 1981 Dec 10;256(23):11955–11957. [PubMed] [Google Scholar]
  16. Roth J., Bendayan M., Carlemalm E., Villiger W., Garavito M. Enhancement of structural preservation and immunocytochemical staining in low temperature embedded pancreatic tissue. J Histochem Cytochem. 1981 May;29(5):663–671. doi: 10.1177/29.5.6166664. [DOI] [PubMed] [Google Scholar]
  17. Schiltz J. R., Michel B. Production of epidermal acantholysis in normal human skin in vitro by the IgG fraction from pemphigus serum. J Invest Dermatol. 1976 Aug;67(2):254–260. doi: 10.1111/1523-1747.ep12513454. [DOI] [PubMed] [Google Scholar]
  18. Skerrow C. J., Matoltsy A. G. Isolation of epidermal desmosomes. J Cell Biol. 1974 Nov;63(2 Pt 1):515–523. doi: 10.1083/jcb.63.2.515. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Staehelin L. A. Structure and function of intercellular junctions. Int Rev Cytol. 1974;39:191–283. doi: 10.1016/s0074-7696(08)60940-7. [DOI] [PubMed] [Google Scholar]
  20. Stanley J. R., Yaar M., Hawley-Nelson P., Katz S. I. Pemphigus antibodies identify a cell surface glycoprotein synthesized by human and mouse keratinocytes. J Clin Invest. 1982 Aug;70(2):281–288. doi: 10.1172/JCI110615. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Steck T. L., Fairbanks G., Wallach D. F. Disposition of the major proteins in the isolated erythrocyte membrane. Proteolytic dissection. Biochemistry. 1971 Jun 22;10(13):2617–2624. doi: 10.1021/bi00789a031. [DOI] [PubMed] [Google Scholar]
  22. 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]
  23. Vestweber D., Kemler R. Rabbit antiserum against a purified surface glycoprotein decompacts mouse preimplantation embryos and reacts with specific adult tissues. Exp Cell Res. 1984 May;152(1):169–178. doi: 10.1016/0014-4827(84)90241-6. [DOI] [PubMed] [Google Scholar]
  24. Yoshida-Noro C., Suzuki N., Takeichi M. Molecular nature of the calcium-dependent cell-cell adhesion system in mouse teratocarcinoma and embryonic cells studied with a monoclonal antibody. Dev Biol. 1984 Jan;101(1):19–27. doi: 10.1016/0012-1606(84)90112-x. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES