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
. 1972 Aug;69(8):2295–2299. doi: 10.1073/pnas.69.8.2295

Cell-Bound Myeloma Proteins on the Surface of Myeloma Cells: Potential Targets for the Immune System

Kristian Hannestad 1,*, Ming-Shian Kao 1,, Herman N Eisen 1
PMCID: PMC426921  PMID: 4626403

Abstract

Rosette formation with 2,4,6-trinitrophenylated (Tnp)-sheep erythrocytes was used to demonstrate cell-bound myeloma proteins on cells from each of the eleven mouse plasmacytomas tested. Tnp-erythrocytes were bound directly by cells from two tumors (MOPC-315 and MOPC-460) that formed myeloma proteins with antihapten combining sites; rosette formation with cells from the other tumors required hybrid antibody fragments with one site specific for Tnp and the other specific for an appropriate immunoglobulin on the tumor cell surface. The cell-bound immunoglobulin of MOPC-315 and of MOPC-460 had the same heavy and light chains, idiotypic determinants, and ligand-binding specificities as the respective myeloma proteins secreted by these tumors. A variant tumor (MOC-315 NR) was grown from the small proportion of MOPC-315 cells (5-10%) that did not bind Tnp-erythrocytes directly: this tumor secreted only the light chain of protein 315, carried this chain on the cell surface, and resembled the variant tumors that arose, probably by immunoselection, in BALB/c mice challenged with MOPC-315 cells while making an immune response to the idiotype of protein 315.

Keywords: plasmacytomas, tumor variants, idiotypes, rosettes

Full text

PDF
2295

Images in this article

Selected References

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

  1. BOYSE E. A., OLD L. J., STOCKERT E. Some further data on cytotoxic isoantibodies in the mouse. Ann N Y Acad Sci. 1962 Oct 24;99:574–587. doi: 10.1111/j.1749-6632.1962.tb45339.x. [DOI] [PubMed] [Google Scholar]
  2. Bach J. F., Muller J. Y., Dardenne M. In vivo specific antigen recognition by rosette forming cells. Nature. 1970 Sep 19;227(5264):1251–1252. doi: 10.1038/2271251a0. [DOI] [PubMed] [Google Scholar]
  3. Baur S., Schenkein I., Uhr J. W. Cell surface immunoglobulin. I. Isolation and characterization of immunoglobulin from murine myeloma cells. J Immunol. 1972 Mar;108(3):748–754. [PubMed] [Google Scholar]
  4. Byrt P., Ada G. L. An in vitro reaction between labelled flagellin or haemocyanin and lymphocyte-like cells from normal animals. Immunology. 1969 Oct;17(4):503–516. [PMC free article] [PubMed] [Google Scholar]
  5. Coffino P., Scharff M. D. Rate of somatic mutation in immunoglobulin production by mouse myeloma cells. Proc Natl Acad Sci U S A. 1971 Jan;68(1):219–223. doi: 10.1073/pnas.68.1.219. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cuatrecasas P. Protein purification by affinity chromatography. Derivatizations of agarose and polyacrylamide beads. J Biol Chem. 1970 Jun;245(12):3059–3065. [PubMed] [Google Scholar]
  7. Eisen H. N., Simms E. S., Potter M. Mouse myeloma proteins with antihapten antibody acitivity. The protein produced by plasma cell tumor MOPC-315. Biochemistry. 1968 Nov;7(11):4126–4134. doi: 10.1021/bi00851a048. [DOI] [PubMed] [Google Scholar]
  8. Goetzl E. J., Metzger H. Affinity labeling of a mouse myeloma protein which binds nitrophenyl ligands. Kinetics of labeling and isolation of a labeled peptide. Biochemistry. 1970 Mar 3;9(5):1267–1278. doi: 10.1021/bi00807a031. [DOI] [PubMed] [Google Scholar]
  9. HELMREICH E., KERN M., EISEN H. N. The secretion of antibody by isolated lymph node cells. J Biol Chem. 1961 Feb;236:464–473. [PubMed] [Google Scholar]
  10. Hart D. A., Wang A. L., Pawlak L. L., Nisonoff A. Suppression of idiotypic specificities in adult mice by administration of antiidiotypic antibody. J Exp Med. 1972 Jun 1;135(6):1293–1300. doi: 10.1084/jem.135.6.1293. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hämmerling U., Aoki T., de Harven E., Boyse E. A., Old L. J. Use of hybrid antibody with anti-gamma-G and anti-ferritin specificities in locating cell surface antigens by electron microscopy. J Exp Med. 1968 Dec 1;128(6):1461–1473. doi: 10.1084/jem.128.6.1461. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Jaffe B. M., Simms E. S., Eisen H. N. Specificity and structure of the myeloma protein produced by mouse plasmacytoma MOPC-460. Biochemistry. 1971 Apr 27;10(9):1693–1699. doi: 10.1021/bi00785a029. [DOI] [PubMed] [Google Scholar]
  13. Kincade P. W., Lawton A. R., Bockman D. E., Cooper M. D. Suppression of immunoglobulin G synthesis as a result of antibody-mediated suppression of immunoglobulin M synthesis in chickens. Proc Natl Acad Sci U S A. 1970 Dec;67(4):1918–1925. doi: 10.1073/pnas.67.4.1918. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Lynch R. G., Graff R. J., Sirisinha S., Simms E. S., Eisen H. N. Myeloma proteins as tumor-specific transplantation antigens. Proc Natl Acad Sci U S A. 1972 Jun;69(6):1540–1544. doi: 10.1073/pnas.69.6.1540. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. McConnell I., Munro A., Gurner B. W., Coombs R. R. Studies on actively allergized cells. I. The cyto-dynamics and morphology of rosete-forming lymph node cells in mice and inhibition of rosette-formation with antibody to mouse immunoglobulins. Int Arch Allergy Appl Immunol. 1969;35(3):209–227. [PubMed] [Google Scholar]
  16. NISONOFF A., RIVERS M. M. Recombination of a mixture of univalent antibody fragments of different specificity. Arch Biochem Biophys. 1961 May;93:460–462. doi: 10.1016/0003-9861(61)90296-x. [DOI] [PubMed] [Google Scholar]
  17. 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]
  18. Paraskevas F., Lee S. T., Israels L. G. Absence of gamma-globulin receptors on mouse plasmacytoma cells. Nature. 1970 Jul 25;227(5256):395–397. doi: 10.1038/227395a0. [DOI] [PubMed] [Google Scholar]
  19. Rittenberg M. B., Pratt K. L. Antitrinitrophenyl (TNP) plaque assay. Primary response of Balb/c mice to soluble and particulate immunogen. Proc Soc Exp Biol Med. 1969 Nov;132(2):575–581. doi: 10.3181/00379727-132-34264. [DOI] [PubMed] [Google Scholar]
  20. Schulenburg E. P., Simms E. S., Lynch R. G., Bradshaw R. A., Eisen H. N. Amino acid sequence of the light chain from a mouse myeloma protein with anti-hapten activity: evidence for a third type of light chain. Proc Natl Acad Sci U S A. 1971 Nov;68(11):2623–2626. doi: 10.1073/pnas.68.11.2623. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Sirisinha S., Eisen H. N. Autoimmune-like antibodies to the ligand-binding sites of myeloma proteins. Proc Natl Acad Sci U S A. 1971 Dec;68(12):3130–3135. doi: 10.1073/pnas.68.12.3130. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Takahashi T., Old L. J., McIntire K. R., Boyse E. A. Immunoglobulin and other surface antigens of cells of the immune system. J Exp Med. 1971 Oct 1;134(4):815–832. doi: 10.1084/jem.134.4.815. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Underdown B. J., Simms E. S., Eisen H. N. Subunit structure and number of combining sites of the immunoglobulin A myeloma protein produced by mouse plasmacytoma MOPC-315. Biochemistry. 1971 Nov 23;10(24):4359–4368. doi: 10.1021/bi00800a002. [DOI] [PubMed] [Google Scholar]
  24. Yakulis V., Bhoopalam N., Schade S., Heller P. Surface immunoglobulins of circulating lymphocytes in mouse plasmacytoma. I. Characteristics of lymphocyte surface immunoglobulins. Blood. 1972 Apr;39(4):453–464. [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