γD Immunoglobulin

  • Hans L. Spiegelberg
Chapter

Abstract

In the past 15 years, much has been learned about the structure and function of different classes of antibodies from studies of monoclonal immunoglobulins formed in patients with multiple myeloma and macroglobulinemia. This is particularly true for γD, the fourth class of human immunoglobulins. γD was discovered as the result of the study of an unusual human myeloma protein (Rowe and Fahey, 1965a), and all subsequent investigations of γD have depended in one or another phase on the availability of γD myeloma proteins. Two characteristics of γD often make it necessary to study γD myeloma proteins rather than normal γD. First, the concentration of γD in the serum is very low, an average of 30 µg/ml, and, second, γD is a labile immunoglobulin which has a great tendency to aggregate and to fragment into subunits during the isolation procedure. γD can therefore usually not be isolated in sufficient quantities from normal blood. Probably for this reason, progress in the evaluation of the role of γD in the immune mechanism of the body has been slow. Although the striking similarity of the structure of γD myeloma proteins to that of the other classes of immunoglobulins has always suggested that γD must represent a class of human antibodies, several years passed following its discovery before antibody activity in that class was reported; to date, all antibody activity has been demonstrated by indirect methods. Therefore, definite proof of antibody activity in isolated normal human γD still remains to be shown. Since γD does not share any of the biological activities of the other immunoglobulin classes, such as fixation of complement and induction of anaphylactic reactions in the skin, role evaluation remains difficult. It is the purpose of this chapter to review the present knowledge of human γD immunoglobulin and to stimulate new investigations which, it is hoped, will lead to discovery of the biological role of γD antibodies.

Keywords

Multiple Myeloma Light Chain Disulfide Bond Amino Sugar Antibody Activity 
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. Abel, C. A., and Grey, H. M. (1967). Science 156: 1609.Google Scholar
  2. Alkjaersig, N., Fletscher, A. P., and Sheiry, S. (1959). J. Biol. Chem. 234: 832.PubMedGoogle Scholar
  3. Avrameas, S., and Ternynck, T. (1967). J. Biol. Chem. 242: 1651.PubMedGoogle Scholar
  4. Cuatrecasas, P., Wilchek, M., and Anfinsen, C. B. (1968). Proc. Natl. Acad. Sci. 61: 636.PubMedCrossRefGoogle Scholar
  5. Cunningham, B. A., Pflumm, M. N., Rutishauser, U., and Edelman, G. M. (1969). Proc. Natl. Acad. Sci. 64: 997.PubMedCrossRefGoogle Scholar
  6. Devey, M., Sanderson, C. J., Carter, D., and Coombs, R. R. A. (1970). Lancet 2: 1280.Google Scholar
  7. Fahey, J. L, Carbone, P. P., Rowe, D. S., and Bachmann, R. (1970). Am. J. Med. 45: 373.CrossRefGoogle Scholar
  8. Fishkin, B. G., Glassy, F. J., Hattersley, P. G., Hirose, F. M., and Spiegelberg, H. L. (1970). Am. J. Clin. Pathol. 53: 209.PubMedGoogle Scholar
  9. Gleich, G. J., Bieger, R. C., and Stankievic, R. (1969). Science 165: 606.PubMedCrossRefGoogle Scholar
  10. Hanson, U. B., Laurell, C. A., and Bachmann, R. (1966). Acta Med. Scand.Suppl. 445: 89.Google Scholar
  11. Heiner, D. C., and Rose, B. (1970). J. Immunol. 104: 691.PubMedGoogle Scholar
  12. Heiner, D. C., Saha, A., and Rose, B. (1968). Fed. Proc. 27: 489.Google Scholar
  13. Henney, C. S., Welscher, H. D., Terry, W. D., and Rowe, D. S. (1969). Immunochemistry 6: 445.PubMedCrossRefGoogle Scholar
  14. Henson, P., Bell, H. J., and Spiegelberg, H. L. (1972). Clin. Exp. Immunol. (in preparation).Google Scholar
  15. Hobbs, J. R., and Corbett, A. A. (1969). Brit. Med. J. 1: 412.PubMedCrossRefGoogle Scholar
  16. Ishizaka, K. (1970). Ann. Rev. Med. 21: 187.PubMedCrossRefGoogle Scholar
  17. Kantor, G. L., van Herle, A. J., and Barnett, E. V. (1970). Clin. Exptl. Immunol. 69: 951.Google Scholar
  18. Ko, A., Clamp, L. R., Dawson, G., and Cebra, J. (1967). Biochem. J. 105: 35 P.Google Scholar
  19. Kunkel, H. G. (1954). Meth. Biochem. Anal. 1: 140.Google Scholar
  20. Kunkel, H. G., Joslin, F. G., Penn, G. M., and Natvig, J. B. (1970). J. Exptl. Med. 132: 508.CrossRefGoogle Scholar
  21. Müller-Eberhard, H. J. (1960). Scand. J. Clin. Lab. Invest. 12: 33.PubMedCrossRefGoogle Scholar
  22. Ovary, Z. (1969). J. Immunol. 102: 790.PubMedGoogle Scholar
  23. Palmer, J. L., and Nisonoff, A. (1964). Biochemistry 3: 863.PubMedCrossRefGoogle Scholar
  24. Pernis, B., Chiappino, G., and Rowe, D. S. (1966). Nature 211: 424.PubMedCrossRefGoogle Scholar
  25. Perry, M. B., and Milstein, C. (1970). Nature 228: 934.PubMedCrossRefGoogle Scholar
  26. Ritchie, R. F. (1968). Rheumatism 11: 506.Google Scholar
  27. Robbins, J. B., Haimovich, J., and Sela, M. (1967). Immunochemistry 4: 11.PubMedCrossRefGoogle Scholar
  28. Rogentine, G. N., Rowe, D. S., Bradley, J., Waldmann, T. A., and Fahey, J. L. (1966). J. Clin. Invest. 45: 1467.Google Scholar
  29. Rowe, D. S., and Fahey, J. L. (1965a). J. Exptl. Med. 121: 171.CrossRefGoogle Scholar
  30. Rowe, D. S., and Fahey, J. L. (1965b). J. Exptl. Med. 121: 185.CrossRefGoogle Scholar
  31. Rowe, D. S., Boyle, J. A., and Buchanan, W. W. (1968a). Clin. Exptl. Immunol. 3: 233.Google Scholar
  32. Rowe, D. S., Crabbe, P. A., and Turner, M. W. (1968b). Clin. Exptl. Immunol. 3: 477.Google Scholar
  33. Rowe, D. S., McGregor, I. A., Smith, S. J., Hall, P., and Williams, K. (1968c). Clin. Exptl. Immunol. 3: 63.Google Scholar
  34. Rowe, D. S., Dolder, F., and Welscher, H. D. (1969). Immunochemistry 6: 437.PubMedCrossRefGoogle Scholar
  35. Rutishauser, U., Cunningham, B. A., Bennet, C., Konigsberg, W. H., and Edelman, G. M. (1968). Proc. Natl. Acad. Sci. 61: 1414.Google Scholar
  36. Saha, A., Chowdhury, P., Sambury, S., Behelak, Y., Heiner, D. C., and Rose, B. (1970). J. Immunol. 105: 238.PubMedGoogle Scholar
  37. Sanford, A., and Osler, A. (1971). Complement Workshop, Baltimore.Google Scholar
  38. Smyth, D. G., and Utsumi, S. (1967). Nature 216: 332.PubMedCrossRefGoogle Scholar
  39. Spiegelberg, H. L., Abel, C. A., Fishkin, B. G., and Grey, H. M. (1970a). Biochemistry 9: 4217.PubMedCrossRefGoogle Scholar
  40. Spiegelberg, H. L., Prahl, J. W., and Grey, H. M. (1970b). Biochemistry 9: 2115.Google Scholar
  41. Spiegelberg, H. L., Gotze, O., and Muller-Eberhard, H. J. (1972). Fed. Proc. (in press).Google Scholar
  42. Watson, I., Heiner, D., Rose, B., and Bootello, A. (1969). Clin. Res. 17: 362.Google Scholar
  43. Yphantis, D. A. (1964). Biochemistry 3: 297.PubMedCrossRefGoogle Scholar
  44. Zawadzki, Z. A., and Edwards, G. A. (1967). J. Clin. Pathol. 48: 418.Google Scholar

Copyright information

© Springer Science+Business Media New York 1972

Authors and Affiliations

  • Hans L. Spiegelberg
    • 1
  1. 1.Department of Experimental PathologyScripps Clinic and Research FoundationCaliforniaUSA

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