Abstract
The antigen receptor on human T lymphocytes consists of two variable immunoglobulin-like glycoproteins, α and β, which occur in association with three invariable T3 membrane proteins1–3. In humans two of these proteins, T3-γ and T3-δ, are glycoproteins of relative molecular mass (Mr) 25,000 (25K) and 20,000 (20K), respectively, while the third, T3-ε, is a 20K non-glycosylated protein4–6. On the surface of murine T cells, a non-glycosylated protein dimer composed of 17K subunits (T3-ζ) is found associated with the T-cell receptor α and β chains and the three T3-like polypeptide chains7,8. It is generally accepted that major histocompatibility complex-restricted antigen recognition is a function of the α–β heterodimer. This has led to the postulation that the proteins of the T3 complex are involved in the signal transduction that immediately follows antigen recognition via the antigen receptor9. Events believed to be involved in early T-cell activation, such as rapid increases in phosphatidylinositol turnover and free intracellular calcium9,10, can be triggered by antibodies directed against either the T3 complex or the clonotypic receptor. We have previously reported our findings on the cloning of the complementary DNA and genomic structure encoding both the human and murine 20K glycoprotein, T3-δ (refs 11–13). We now present our results on the cloning of the cDNA encoding the human 20K non-glycosylated chain, T3-ε.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Oettgen, H. C., Kappler, J., Tax, W. J. P. & Terhorst, C. J. biol. Chem. 259, 12039–12048 (1984).
Meuer, S. C., Acuto, O., Hercend, T., Schlossman, S. F. & Reinherz, E. L. A. Rev. Immun. 2, 23–50 (1984).
Brenner, M. B., Trowbridge, I. S. & Strominger, J. L. Cell 40, 183–190 (1985).
Borst, J., Alexander, S., Elder, J. & Terhorst, C. J. biol. Chem. 258, 5135–5141 (1983).
Borst, J., Prendiville, M. A. & Terhorst, C. Eur. J. Immun. 13, 576–580 (1983).
Kanellopoulos, J. M., Wigglesworth, N. M., Owen, M. J. & Crumpton, M. J. EMBO J. 2, 1807–1814 (1983).
Samelson, L. E., Harford, J. B. & Klausner, R. D. Cell 43, 223–231 (1985).
Oettgen, H. C., Pettey, C., Maloy, W. L. & Terhorst, C. Nature 320, 272–275 (1986).
Oettgen, H. C., Terhorst, C., Cantley, L. C. & Rosoff, P. M. Cell 40, 583–590 (1985).
Imboden, J. B. & Stobo, D. J. J. exp. Med. 161, 446–456 (1985).
van den Elsen, P. et al. Nature 312, 413–418 (1985).
van den Elsen, P., Shepley, B.-A., Cho, M. & Terhorst, C. Nature 314, 542–544 (1985).
van den Elsen, P., Georgopoulos, K., Shepley, B.-A., Orkin, S. & Terhorst, C. Proc. natn. Acad. Sci. U.S.A. (in the press).
Pessano, S., Oettgen, H. C., Bhan, A. & Terhorst, C. EMBO J. 4, 337–344 (1985).
MacLeod, C. L., Minning, L., Gold, D. P., Terhorst, C. & Wilkinson, M. Proc. natn. Acad. Sci. U.S.A. (submitted).
Furley, A. J. et al. Cell (in the press).
Okayama, H. & Berg, P. Molec. cell. Biol. 2, 161–170 (1982).
Yokota, T. et al. Proc. natn. Acad. Sci. U.S.A. 81, 1070–1074 (1984).
von Heijne, G. J. molec. Biol. 184, 99–105 (1985).
Borst, J. et al. Nature 312, 455–458 (1984).
Hedrick, S. M., Cohen, D. I., Neilsen, E. A. & Davis, M. M. Nature 308, 149–153 (1984).
Yanagi, Y. et al. Nature 308, 145–148 (1984).
Chien, Y. et al. Nature 312, 31–35 (1984).
Saito, H. et al. Nature 312, 36–40 (1984).
Towbin, H., Staehelin, T. & Gordon, J. Proc. natn. Acad. Sci. U.S.A. 76, 4350–4354 (1979).
Puck, J. M. & Rich, R. R. J. Immun. 132, 1106–1112 (1984).
Woods, D., Crampton, J., Clark, B. & Williamson, R. Nucleic Acids Res. 8, 5157–5168 (1980).
Young, R. A. & Davis, R. W. Proc. natn. Acad. Sci. U.S.A. 80, 1194–1198 (1983).
Huynh, T. V., Young, R. A. & Davis, R. W. in Practical Approaches in Biochemistry (ed. Glover, D.) (IRL, Oxford, 1984).
Maniatis, T., Fritsch, E. F. & Sambrook, J. Molecular Cloning, A Laboratory Manual (Cold Spring Harbor Laboratory, New York, 1982).
Feinberg, A. P. & Vogelstein, B. Analyt. Biochem. 137, 266–267 (1984).
Sanger, F., Nicklen, S. & Coulson, A. R. Proc. natn. Acad. Sci. U.S.A. 74, 5463–5467 (1977).
Yanisch-Perron, C., Vieira, J. & Messing, J. Gene 33, 103–119 (1985).
Kyte, J. & Doolittle, R. F. J. molec. Biol. 157, 105–132 (1982).
Hunkapiller, M. W., Lujan, E., Ostrander, F. & Hood, L. E. Meth. Enzym. 91, 227–231 (1983).
Coligan, J. E., Gates, F. T., Kimball, E. S. & Maloy, W. L. Meth. Enzym. 91, 413–417 (1983).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Gold, D., Puck, J., Pettey, C. et al. Isolation of cDNA clones encoding the 20K non-glycosylated polypeptide chain of the human T-cell receptor/T3 complex. Nature 321, 431–434 (1986). https://doi.org/10.1038/321431a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/321431a0
This article is cited by
-
Association of proinflammatory cytokines and islet resident leucocytes with islet dysfunction in type 2 diabetes
Diabetologia (2014)
-
T lymphocyte apoptosis induced by CD8ε chimera
Chinese Science Bulletin (1997)
-
Independent mutations of the human CD3–ε gene resulting in a T cell receptor/CD3 complex immunodeficiency
Nature Genetics (1993)
-
T-Cell receptor and autoimmune disease
Immunologic Research (1990)
-
DNase hypersensitivity and methylation of the humanCD3G andD genes during T-cell development
Immunogenetics (1990)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.
