Nature 312, 455 - 458 (29 November 1984); doi:10.1038/312455a0

The - and -chains of the human T3/T-cell receptor complex are distinct polypeptides

Jannie Borst, John E. Coligan^*, Hans Oettgen, Silvana Pessano, Robert Malin & Cox Terhorst

Laboratory of Molecular Immunology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, USA
^*Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20205, USA

The T3/T-cell receptor complex on the surface of human thymus-derived lymphocytes consists of four glycoproteins: the -chain of relative molecular mass (M _r) 40,000−50,000 (40−50K), the -chain (37−45K); the -chain (25K) and the -chain (20K)¹⁻³. The T3 - and -chains have been identified as clonotypic T-cell receptors³⁻⁷, but functionally the T3/T-cell receptor chains seem to form a single complex: monoclonal antibodies directed at the 20K T3 components are mitogenic for normal human T lymphocytes^8,9 and, at higher concentrations, anti-clonotypic and anti-20K reagents block T-cell function^4,10. Recently, Zanders et al. ¹¹ showed that incubation of human T-helper clones with high concentrations of antigen abolishes antigen-specific proliferation and induces disappearance of T3 from the cell surface. Thus, the T3/T-cell receptor complex consists of two variable subunits, the T3 - and -chains, which interact with antigen and the monomorphic 20K/25K T3 chains. Recently, the existence of a fifth polypeptide chain, the unglycosylated T3 -chain, has been postulated^12,13. Here we confirm that a 20K -chain does exist. The T3 -chain differs from the T3 -chain in primary structure as judged by N-terminal amino acid sequencing, peptide mapping and immuno-blotting with anti-T3- and anti-T3- antibodies. Treatment with endoglycosidase F revealed two nonglycosylated T3 polypeptide backbone chains (16K and 14K) with identical amino termini. Together with previous pulse-chase experiments² this observation suggests that the 14K T3 polypeptide is derived from the 16K T3 precursor by proteolytic processing near the C-terminus of the molecule.

References

1.	Borst, J., Prendiville, M. A. & Terhorst, C. J. Immun. 128, 1560−1565 (1982). | PubMed | ISI | ChemPort |
2.	Borst, J., Alexander, S., Elder, J. & Terhorst, C. J. biol. Chem. 258, 5135−5141 (1983). | PubMed | ISI | ChemPort |
3.	Reinherz, E. L. et al. Proc. natn. Acad. Sci. U.S.A. 80, 4104−4110 (1983). | ChemPort |
4.	Reinherz, E. L., Meuer, S. C. & Schlossman, S. F. Immun. Rev. 74, 83−112 (1983). | PubMed | ISI | ChemPort |
5.	Allison, J. P., McIntyre, B. W. & Bloch, D. J. Immun. 129, 2293−2299 (1982). | PubMed | ISI | ChemPort |
6.	Haskins, K. et al. J. exp. Med. 157, 1149−1157 (1983). | Article | PubMed | ISI | ChemPort |
7.	Oettgen, H., Kappler, J., Tax, W. & Terhorst, C. J. biol. Chem. 259, 12039−12048 (1984). | PubMed | ChemPort |
8.	van Wauwe, de Mey, J. R. & Goossens, J. G. J. Immun. 124, 2708−2714 (1980). | PubMed | ChemPort |
9.	Tax, W. J. M., Willems, H. W., Reekers, P. P. M., Capel, P. J. A. & Koene, R. A. P. Nature 304, 445−447 (1983). | PubMed | ISI | ChemPort |
10.	Spits, H., Borst, J., Terhorst, C. & de Vries, J. E. J. Immun. 129, 1563−1569 (1982). | PubMed | ISI | ChemPort |
11.	Zanders, E. D., Lamb, J. R., Feldmann, M., Green, N. & Beverley, P. C. L. Nature 303, 625−627 (1983). | PubMed | ISI | ChemPort |
12.	Borst, J., Prendiville, M. A. & Terhorst, C. Eur. J. Immun. 13, 576−580 (1983). | ISI | ChemPort |
13.	Kanellopoulos, J. M., Wigglesowrth, N. M., Owen, M. J. & Crumpton, M. J. EMBO J. 2, 1807−1814 (1983). | PubMed | ISI | ChemPort |
14.	Van den Elsen, P. et al. Nature 212, 413−418 (1984).
15.	Kabat, E. A., Wu, T. T., Bilofsky, H., Reid-Miller, M. & Perry, H. Sequences of Proteins of Immunological Interest (U. S. Department of Health, Education and Welfare, 1983).
16.	Yanagi, Y. et al. Nature 308, 145−148 (1984). | PubMed | ISI | ChemPort |
17.	Hedrick, S. M., Cohen, D. I., Nielsen, E. A. & Davis, M. M. Nature 308, 149−153 (1984). | PubMed | ISI | ChemPort |
18.	Hedrick, S. M., Nielsen, E. A., Kavaler, J., Cohen, D. I. & Davis, M. M. Nature 308, 153−157 (1984). | PubMed | ISI | ChemPort |
19.	Saito, H. et al. Nature 309, 757−762 (1984). | PubMed | ISI | ChemPort |
20.	Snow, P., Keizer, G., Coligan, J. E. & Terhorst, C. J. Immun. 133, 2058−2066 (1984). | PubMed | ISI | ChemPort |
21.	Williams, A. F. & Gagnon, J. Science 216, 696−702 (1982). | PubMed | ISI | ChemPort |
22.	Oettgen, H. C., Terhorst, C., Cantley, L. C. & Rosoff, P. Cell (submitted).
23.	Terhorst, C. et al. Cell 23, 771−780 (1981). | Article | PubMed | ISI | ChemPort |
24.	Terhorst, C., LeClair, K., Ma, A. & Slayter, H. Molec. Immun. 18, 520−529 (1980).
25.	Schneider, C., Newman, R. A., Asser, U., Sutherland, D. R. & Greaves, M. F. J. biol. Chem. 257, 10766−10772 (1982). | PubMed | ChemPort |
26.	Hunkapiller, M. W., Lujan, E., Ostrander, F. & Hood, L. E. Meth. Enzym. 91, 227−231 (1983). | Article | PubMed | ISI | ChemPort |
27.	Adair, S. Analyt. Biochem. 126, 299−306 (1982).
28.	Coligan, J. E., Gates, F. T., Kimball, E. S. & Maloy, W. L. Meth. Enzym. 91, 413−417 (1983). | Article | PubMed | ISI | ChemPort |
29.	Towbin, J., Staehelin, T. & Gordon, J. Biochemistry 76, 4350−4355 (1979).
30.	Green, N. et al. Cell 28, 477−487 (1982). | Article | PubMed | ISI | ChemPort |