Immunogenetics

, Volume 16, Issue 5, pp 459–469 | Cite as

Human MHC class II molecules as differentiation markers

  • Veronica van Heyningen
  • Keith Guy
  • Roland Newman
  • C. Michael Steel
Article
Received:

Abstract

DA6.231 and DA6.164 are mouse monoclonal antibodies that immunoprecipitate HLA-DR-like p34,29 glycoprotein dimers from surface- and metabolically-labeled cells. On lymphoblastoid cell lines the distribution of the 231 epitope is completely nonpolymorphic, while the 164 epitope is present on all cells except on those that are DR7 homozygous. Binding-inhibition studies show that the 231 and 164 epitopes are spatially close to each other when present on the same molecule. The mutual inhibition pattern and the absence of the 164 epitope from the 231+ cells of a few leukemia patients suggest, however, that 231 and 164 epitopes are not invariably present together. Most DR-positive cells possess 231− 164+ and 231+ 164− class 11 molecules in approximately a 2:1 ratio. This has been confirmed by immune depletion studies. Thus DA6.231 appears to define a supralocus epitope. The 164 epitope may be a marker for a subset of class 11 molecules exhibiting differential expression on various cell types immortalized by malignant transformation.

Keywords

Monoclonal Antibody Leukemia Malignant Transformation Differentiation Marker Mouse Monoclonal Antibody 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References

  1. Barnstable, C. J., Bodmer, W. F., Brown, G., Galfre, G., Milstein, C., Williams, A. F., and Ziegler, A.: Production of monoclonal antibodies to group A erythrocytes, HLA and other human cell surface antigens — new tools for genetic analysis. Cell 14: 9–20, 1978Google Scholar
  2. Benacerraf, B: Genetic control of the specificity of T lymphocytes and their regulatory products. In M. Fougereau and J. Dausset (eds.): Fourth International Congress of Immunology: Immunology 80: pp. 419–431 Acad. Press, London 1980Google Scholar
  3. Bodmer, W. F., Batchelor, J. R., Bodmer, J. G., Festenstein, H., and Morris, P. J. (eds.): Histocompatibility Testing 1977: Report of the 7th International Histocompatibility Workshop and Conference. Munksgaard, Copenhagen, 1978Google Scholar
  4. Corte, G., Calabi, F., Damiani, G., Bargellesi, A., Tosi, R., and Sorrentino, R.: Human Ia molecules carrying DC1 determinants differ in both α- and β-subunits from Ia molecules carrying DR determinants. Nature 292: 357–360, 1981Google Scholar
  5. de Kretser, T. A., Crumpton, M. J., Bodmer, J. G., and Bodmer, W. F.: Demonstration of two distinct light chains in HLA-DR-associated antigens by two dimensional gel electrophoresis. Eur. J. Immunol. 12: 214–221, 1982Google Scholar
  6. Duquesnoy, R. J., Marrari, M., and Armen, K.: Identification of an HLA-DR-associated system of B-cell alloantigens. Transplant. Proc. 11: 1757–1760, 1979Google Scholar
  7. Goyert, S. M. and Silver, J.: Isolation of I-A subregion-like molecules from subhuman primates and man. Nature 294: 266–268, 1981Google Scholar
  8. Guy, K., van Heyningen, V., Cohen, B. B., Deane, D. L., Crichton, D., and Steel, C. M.: Subsets of human D-locus products identified by a series of monoclonal antibodies. In H. Peeters (ed): Protides of the Biological Fluids 29th Colloquium, 1981, pp. 729–734, Pergamon Press, Oxford, 1982aGoogle Scholar
  9. Guy, D., van Heyningen, V., Cohen, B. B., Deane, D. L., and Steel, C. M.: Differential expression and serologically distinct subpopulations of the human Ia antigens detected with monoclonal antibodies to Ia alpha and beta chains. Eur. J. Immunol., in press, 1982bGoogle Scholar
  10. Jones, P. P., Murphy, D. B., and McDevitt, H. O.: Two-gene control of the expression of a marine Ia antigen. J. Exp. Med. 148: 925–939, 1978Google Scholar
  11. Koch, N. and Hämmerling, G. J.: Ia antigens contain two distinct forms of β chain. Immunogenetics 14: 437–444, 1981Google Scholar
  12. Kratzin, H., Yang, C., Gotz, H., Pauly, E., Kolbel, S., Egert, G., Thrones, F. P., Wernet, P., Altervogt, P., and Hilschmann, N.: Primary structure of class If human histocompatibility antigens: l. Amino acid sequence of the N-terminal 198 residues of the β chain of a HLA DW2,2,DR2,2 alloantigen. Hoppe Seylers Z. Physiol. Chem. 362: 1665–1669, 1981Google Scholar
  13. Lampson, L. A. and Levy, R.: Two populations of la-like molecules on a human B cell line. J. Immunol. 125: 293–299, 1980Google Scholar
  14. Letarte, M. and Falk, J.: Biochemical and immunologic heterogeneity of Ia glycoproteins isolated from a chronic lymphocytic leukaemia. J. Immunol. 128: 217–223, 1982Google Scholar
  15. Lloyd, K. O., Ng, J., and Dippold, W. G.: Analysis of the biosynthesis of HLA-DR glycoproteins in human malignant melanoma cell lines. J. Immunol. 126: 2408–2413, 1981Google Scholar
  16. McDevitt, H. O.: The role of H-2 I region genes in regulation of the immune response. In M. Fougereau and J. Dausset (eds.): Fourth International Congress of Immunology: Immunology 80, pp. 503–512 Acad. Press, London, 1980Google Scholar
  17. Markert, M. L. and Cresswell, P.: Polymorphism of human B-cell alloantigens: Evidence for three loci within the HLA system. Proc. Natl. Acad. Sci. U.S.A., 77: 6101–6104, 1980Google Scholar
  18. Nadler, L. M., Stashenko, P., Hardy, R., Tomaselli, K. J., Yunis, E. J., Schlossman, S. F. and Pesando, J. M.: Monoclonal antibody identifies a new la-like (p.29, 34) polymorphic system linked to the HLA-D/DR region. Nature 290: 591–593, 1981Google Scholar
  19. Quaranta, V., Pellegrino, M. A., and Ferrone, S.: Serologic and immunochemical characterization of the specificity of four monoclonal antibodies to distinct antigenic determinants expressed on subpopulations of human la-like antigens. J. Immunol. 126: 548–552, 1981Google Scholar
  20. Robinson, J., Sieff, C., Delia, D., Edwards, P. A. W., and Greaves, M.: Expression of cell-surface HLADR, HLA-ABC and glycophorin during erythroid differentiation. Nature 289: 68–71, 1981Google Scholar
  21. Shackelford, D. A., Mann, D. L., van Rood, J. J., Ferrara, G. B., and Strominger, J. L.: Human B-cell alloantigens DCl, MT 1 and LB 12 are identical to each other but distinct from the HLA-DR antigen. Proc. Natl. Acad. Sci. U.S.A., 78: 4566–4570, 1981Google Scholar
  22. Shaw, S., Johnson, A. H., and Shearer, G. M.: Evidence for a new segregant series of B cell antigens that are encoded in the HLA-D region and that stimulate secondary allogeneic proliferative and cytotoxic responses. J. Exp. Med. 152: 555–580, 1980Google Scholar
  23. Tosi, R., Tanigaki, N., Centis, D., Ferrara, G. B., and Pressman, D.: Immunological dissection of human Ia molecules. J. Exp. Med. 148: 1592–1611, 1978Google Scholar
  24. van Heyningen, V., Barron, L., Brock, D. J. H., Crichton, D., and Lawrie, S.: Monoclonal antibodies to human a-fetoproteim analysis of the behaviour of three different antibodies. J. Immunol. Methods, 50: 123–131, 1982Google Scholar
  25. Winchester, R. J.: Aspects of surface membrane differentiation during maturation of human hematopoietic and tumor cells: the Ia system. Curr. Top. Dev. Biol. 14: 115–125, 1980Google Scholar
  26. Winchester, R. J. and Kunkel, H. G.: The human Ia system. Adv. Immunol. 28: 221–292, 1979Google Scholar

Copyright information

© Springer-Verlag 1982

Authors and Affiliations

  • Veronica van Heyningen
    • 1
  • Keith Guy
    • 1
  • Roland Newman
    • 2
  • C. Michael Steel
    • 1
  1. 1.MRC Clinical & Population Cytogenetics UnitWestern General HospitalEdinburghUnited Kingdom
  2. 2.Imperial Cancer Research FundLincoln's Inn FieldsLondonUnited Kingdom

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