Skip to main content
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
. 1981 Nov;78(11):7078–7082. doi: 10.1073/pnas.78.11.7078

Structural comparisons of TL antigens derived from normal and leukemia cells of Tl+ and TL- strains and relationship to genetically linked H-2 major histocompatibility complex products.

K Yokoyama, E Stockert, L J Old, S G Nathenson
PMCID: PMC349198  PMID: 6947273

Abstract

Comparative tryptic peptide analysis was used to probe the structure of the TL products coded for by normally expressed TL alleles (Tlaa and Tlac haplotypes) and the structure of the TL product on ERLD, a TL+ leukemia occurring in a strain that does not normally express TL antigens (Tlab haplotype). In mice that have the Tlaa haplotype, the peptide maps of TL glycoproteins from normal thymocytes and from TL+ leukemias were identical, a finding that is consistent with the indistinguishable serologically defined TL phenotype of these cells. Analysis of the TL product on ERLD leukemia cells (TL phenotype, TL.1,2,4) indicates a single TL glycoprotein species with the TL.4 determinant (restricted to leukemias of Tlab and Tlac haplotypes) coexisting on the same glycoprotein as the Tl.1 determinant (normally expressed by thymocytes of Tlaa haplotype). Comparison of the peptides of the TL product of ERLD and the products of the normally expressed Tlaa and Tlac loci showed a high degree of structural similarity (i.e., 70-80%) of shared peptides. In contrast, the products of the Tlaa, Tlab, and Tlac loci shared relatively few peptides with the products of the K, D, and L loci of the closely linked major histocompatibility complex (15-35%). The TL family, therefore, consists of alleles that are highly homologous. This contrasts with the marked diversity and polymorphism among the alleles of the K, D, and L loci.

Full text

PDF
7078

Selected References

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

  1. Anundi H., Rask L., Ostberg L., Peterson P. A. The subunit structure of thymus leukemia antigens. Biochemistry. 1975 Nov 18;14(23):5046–5054. doi: 10.1021/bi00694a003. [DOI] [PubMed] [Google Scholar]
  2. Boyse E. A., Old L. J. A comment on the genetic data relating to expression of TL antigens. Transplantation. 1971 Jun;11(6):561–562. [PubMed] [Google Scholar]
  3. Boyse E. A., Old L. J., Stockert E. An approach to the mapping of antigens on the cell surface. Proc Natl Acad Sci U S A. 1968 Jul;60(3):886–893. doi: 10.1073/pnas.60.3.886. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Boyse E. A., Stockert E., Old L. J. Modification of the antigenic structure of the cell membrane by thymus-leukemia (TL) antibody. Proc Natl Acad Sci U S A. 1967 Sep;58(3):954–957. doi: 10.1073/pnas.58.3.954. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Brown J. L., Kato K., Silver J., Nathenson S. G. Notable diversity in peptide composition of murine H-2K and H-2D alloantigens. Biochemistry. 1974 Jul 16;13(15):3174–3178. doi: 10.1021/bi00712a027. [DOI] [PubMed] [Google Scholar]
  6. Cullen S. E., Schwartz B. D. An improved method for isolation of H-2 and Ia alloantigens with immunoprecipitation induced by protein A-bearing staphylococci. J Immunol. 1976 Jul;117(1):136–142. [PubMed] [Google Scholar]
  7. Hayman M. J., Crumpton M. J. Isolation of glycoproteins from pig lymphocyte plasma membrane using Lens culinaris phytohemagglutinin. Biochem Biophys Res Commun. 1972 May 26;47(4):923–930. doi: 10.1016/0006-291x(72)90581-5. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. Lemke H., Hämmerling G. J., Hämmerling U. Fine specificity analysis with monoclonal antibodies of antigens controlled by the major histocompatibility complex and by the Qa/TL region in mice. Immunol Rev. 1979;47:175–206. doi: 10.1111/j.1600-065x.1979.tb00293.x. [DOI] [PubMed] [Google Scholar]
  10. McIntyre K. R., Vitetta E. S., Hämmerling U., Michaelson J., Flaherty L., Uhr J. W. Analysis of thymus-leukemia (TL) antigens with monoclonal antibodies. J Immunol. 1980 Aug;125(2):601–605. [PubMed] [Google Scholar]
  11. Nairn R., Nathenson S. G., Coligan J. E. Isolation, characterization and amino acid sequence studies of the cyanogen bromide fragments of the H-2Dd glycoprotein. Eur J Immunol. 1980 Jul;10(7):495–503. doi: 10.1002/eji.1830100703. [DOI] [PubMed] [Google Scholar]
  12. Nairn R., Yamaga K., Nathenson S. G. Biochemistry of the gene products from murine MHC mutants. Annu Rev Genet. 1980;14:241–277. doi: 10.1146/annurev.ge.14.120180.001325. [DOI] [PubMed] [Google Scholar]
  13. Nathenson S. G., Uehara H., Ewenstein B. M., Kindt T. J., Coligan J. E. Primary structural: analysis of the transplantation antigens of the murine H-2 major histocompatibility complex. Annu Rev Biochem. 1981;50:1025–1052. doi: 10.1146/annurev.bi.50.070181.005113. [DOI] [PubMed] [Google Scholar]
  14. OLD L. J., BOYSE E. A. ANTIGENIC PROPERTIES OF EXPERIMENTAL LEUKEMIAS. I. SEROLOGICAL STUDIES IN VITRO WITH SPONTANEOUS AND RADIATION-INDUCED LEUKEMIAS. J Natl Cancer Inst. 1963 Oct;31:977–995. [PubMed] [Google Scholar]
  15. Old L. J., Stockert E., Boyse E. A., Kim J. H. Antigenic modulation. Loss of TL antigen from cells exposed to TL antibody. Study of the phenomenon in vitro. J Exp Med. 1968 Mar 1;127(3):523–539. doi: 10.1084/jem.127.3.523. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Old L. J., Stockert E. Immunogenetics of cell surface antigens of mouse leukemia. Annu Rev Genet. 1977;11:127–160. doi: 10.1146/annurev.ge.11.120177.001015. [DOI] [PubMed] [Google Scholar]
  17. Pischel K. D., Little J. R. Further evidence for structural relatedness between murine MHC and thymus-leukemia antigens. Mol Immunol. 1980 May;17(5):681–685. doi: 10.1016/0161-5890(80)90167-4. [DOI] [PubMed] [Google Scholar]
  18. Sears D. W., Polizzi C. M. Biochemical evidence for a separate, MHC-linked locus encoding H-2.28 antigens. Immunogenetics. 1980;10(1):67–82. doi: 10.1007/BF01561553. [DOI] [PubMed] [Google Scholar]
  19. Vitetta E. S., Capra J. D. The protein products of the murine 17th chromosome: genetics and structure. Adv Immunol. 1978;26:147–193. doi: 10.1016/s0065-2776(08)60230-8. [DOI] [PubMed] [Google Scholar]
  20. Yokoyama K., Mashimo J., Kasai N., Terao T., Osawa T. Binding of bacterial lipopolysaccharide to histocompatibility-2-complex proteins of mouse lymphocytes. Hoppe Seylers Z Physiol Chem. 1979 Apr;360(4):587–595. doi: 10.1515/bchm2.1979.360.1.587. [DOI] [PubMed] [Google Scholar]
  21. Yokoyama K., Terao T., Osawa T. Isolation and characterization of membrane receptors for pokeweed mitogens from mouse lymphocytes. Biochem J. 1977 Sep 1;165(3):431–437. doi: 10.1042/bj1650431. [DOI] [PMC free article] [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