Nature Publishing Group, publisher of Nature, and other science journals and reference works
Nature
my account e-alerts subscribe register
SEARCH JOURNAL     advanced search
Journal Home
Current Issue
AOP
Archive
Download PDF
References
Export citation
Export references
Send to a friend
More articles like this

Letters to Nature
Nature 252, 602 - 604 (13 December 1974); doi:10.1038/252602a0

Immunoglobulin of T lymphoma cells is an integral membrane protein

DIETER HAUSTEIN, JOHN. J. MARCHALONIS & MICHAEL J. CRUMPTON*

The Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, Victoria 3050
The John Curtin School of Medical Research, Australian National University, Canberra, Australia
*Permanent address: National Institute of Medical Research, Mill Hill, London NW7, UK.

IMMUNOGLOBULINS, predominantly 7S IgM molecules (molecular weight approx 200,000), are associated with the plasma membranes of lymphocytes1−3 and considerable evidence suggests that these proteins function as receptors for antigen4−6. If these molecules are themselves integral parts of the lymphocyte membrane or are strongly associated with integral proteins they may transmit antigen-induced signals through the membrane and initiate cell activation. It has been proposed that the antigen-combining site of T cell IgM protrudes from the cell surface, but that the Fc portion bearing the characteristic antigenic determinants of the heavy chain is not accessible to large molecules in the solvent2,7. If these proposals are correct, then surface immunoglobulin of T cells might be considered an integral constituent of the plasma membrane8.

------------------

References
1. Vitetta, E. S., Baur, S., and Uhr, J. W., J. exp. Med., 134, 242–264 (1971).
2. Marchalonis, J. J., Cone, R. E., and Atwell, J. L., J. exp. Med., 135, 956–971 (1972).
3. Kennel, S. J., and Lerner, R. A., J. molec. Biol., 76, 485–502 (1973).
4. Greaves, M. F., Owen, J. J. T., and Raff, M. C., T and B Lymphocytes (Excerpta Medica, Amsterdam, 1973).
5. Marchalonis, J. J., and Cone, R. E., Transplant. Rev., 14, 3–49 (1973).
6. Warner, N. L., Adv. Immun., 19, 67–216 (1974).
7. Hogg, N. M., and Greaves, M. F., Immunology, 22, 967–980 (1972).
8. Singer, S. J., in Structure and Function of Biological Membranes (edit. by Rothfield, L. I.) 145 (Academic Press, New York, 1971).
9. Harris, A. W., Bankhurst, A. D., Mason, S., and Warner, N. L., J. Immun., 110, 431–438 (1973).
10. Stocker, J. W., Marchalonis, J. J., and Harris, A. W., J. exp. Med., 139, 785–790 (1974).
11. Crumpton, M. J., and Snary, D., in Contemporary Topics in Microbiology (edit by Ada, G. L.,) (Plenum Press, New York, in the press).
12. Haustein, D., J. Immun. Meth. (in the press).
13. Marchalonis, J. J., Cone, R. E., and Santer, V., Biochem. J., 124, 921–927 (1971).
14. Wright, B. M., Edwards, A. J., and Jones, V. E., J. Immun. Meth., 4, 281–296 (1974).
15. Hunter, W. M., and Greenwood, F. C., Nature, 194, 495–496 (1962).
16. Laemmli, U. K., Nature, 227, 680–685 (1970).
17. Basten, A., Miller, J. F. A. P., Sprent, J., and Pye, J. J., J. exp. Med., 135, 610–626 (1972).
18. Moroz, C., and Hahn, Y., Proc. natn. Acad. Sci. U.S.A., 70, 3716–3720 (1973).



© 1974 Nature Publishing Group
Privacy Policy