Skip to main content
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1974 Oct 1;140(4):939–953. doi: 10.1084/jem.140.4.939

ANTIGENIC MODULATION IN VITRO

I. Fate of Thymus-Leukemia (TL) Antigen-Antibody Complexes Following Modulation of TL Antigenicity from the Surfaces of Mouse Leukemia Cells and Thymocytes

Christopher W Stackpole 1, Janet B Jacobson 1, Michael P Lardis 1
PMCID: PMC2139632  PMID: 4610077

Abstract

The modulation or loss of thymus-leukemia (TL) antigenicity from the surfaces of mouse RADA1 leukemia cells and normal thymocytes during incubation with TL antibody in vitro at 37°C was investigated by cytotoxicity, immunofluorescence, and immunoelectron microscopy. The fate of bivalent and monovalent antibody during modulation was visualized by fluorescence microscopy. Considerable antibody remained bound to the cell surface after modulation, bivalent antibody being displaced topographically into "patches" and "caps" while monovalent antibody was only slightly aggregated on the cell surface. Some antibody was internalized, presumably by pinocytosis, and was sequestered into the Golgi region of the cell. Capping usually occurred over the pole of the cell opposite from the Golgi region, which may explain the lack of extensive pinocytosis of modulating bivalent antibody. Since modulation with monovalent antibody occurs without patch or cap formation, gross topographical redistribution of TL antigen-antibody complexes is not required for modulation, although more subtle displacement of these complexes may be involved. Modulation was demonstrable by cytotoxicity with guinea pig C' but not with absorbed rabbit C', indicating that modulated TL antigens remain bound to the cell surface. A heat-labile factor in TL antiserum and in mouse serum in general is responsible for "blocking" the cytolytic interaction of guinea pig C' with modulated TL antigen-antibody complexes.

Full Text

The Full Text of this article is available as a PDF (1.0 MB).

Selected References

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

  1. Boyse E. A., Flaherty L., Stockert E., Old L. J. Histoincompatibility attributable to genes near H-2 that are not revealed by hemagglutination or cytotoxicity tests. Transplantation. 1972 Apr;13(4):431–432. doi: 10.1097/00007890-197204000-00013. [DOI] [PubMed] [Google Scholar]
  2. Boyse E. A., Hubbard L., Stockert E., Lamm M. E. Improved complementation in the cytotoxic test. Transplantation. 1970 Nov;10(5):446–449. doi: 10.1097/00007890-197011000-00019. [DOI] [PubMed] [Google Scholar]
  3. 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]
  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. Cebra J. J., Goldstein G. Chromatographic purification of tetramethylrhodamine-immune globulin conjugates and their use in the cellular localization of rabbit gamma-globulin polypeptide chains. J Immunol. 1965 Aug;95(2):230–245. [PubMed] [Google Scholar]
  6. Gingell D. Membrane permeability change by aggregation of mobile glycoprotein units. J Theor Biol. 1973 Mar;38(3):677–679. doi: 10.1016/0022-5193(73)90266-x. [DOI] [PubMed] [Google Scholar]
  7. Hämmerling U., Aoki T., Wood H. A., Old L. J., Boyse E. A., de Harvin E. New visual markers of antibody for electron microscopy. Nature. 1969 Sep 13;223(5211):1158–1159. doi: 10.1038/2231158a0. [DOI] [PubMed] [Google Scholar]
  8. Hämmerling U., Chin A. F., Arny M. Fluorescence labeling of mouse alloantibodies. Eur J Immunol. 1974 Apr;4(4):314–317. doi: 10.1002/eji.1830040416. [DOI] [PubMed] [Google Scholar]
  9. Hämmerling U., Rajewsky K. Evidence for surface-associated immunoglobulin on T and B lymphocytes. Eur J Immunol. 1971 Dec;1(6):447–452. doi: 10.1002/eji.1830010608. [DOI] [PubMed] [Google Scholar]
  10. Lamm M. E., Boyse E. A., Old L. J., Lisowska-Bernstein B., Stockert E. Modulation of TL (thymus-leukemia) antigens by Fab-fragments of TL antibody. J Immunol. 1968 Jul;101(1):99–103. [PubMed] [Google Scholar]
  11. 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]
  12. Stackpole C. W., DeMilio L. T., Jacobson J. B., Hämmerling U., Lardis M. P. A comparison of ligand-induced redistribution of surface immunoglobulins, alloantigens, and concanavalin A receptors on mouse lymphoid cells. J Cell Physiol. 1974 Jun;83(3):441–447. doi: 10.1002/jcp.1040830315. [DOI] [PubMed] [Google Scholar]
  13. Stackpole C. W., Jacobson J. B., Lardis M. P. Two distinct types of capping of surface receptors on mouse lymphoid cells. Nature. 1974 Mar 15;248(445):232–234. doi: 10.1038/248232a0. [DOI] [PubMed] [Google Scholar]
  14. Yu A., Cohen E. P. Studies on the effect of specific antisera on the metabolism of cellular antigens. I. Isolation of thymus leukemia antigens. J Immunol. 1974 Apr;112(4):1285–1295. [PubMed] [Google Scholar]
  15. Yu A., Cohen E. P. Studies on the effect of specific antisera on the metabolism of cellular antigens. II. The synthesis and degradation of TL antigens of mouse cells in the presence of TL antiserum. J Immunol. 1974 Apr;112(4):1296–1307. [PubMed] [Google Scholar]

Articles from The Journal of Experimental Medicine are provided here courtesy of The Rockefeller University Press

RESOURCES