Abstract
The majority of human T cells express an antigen receptor consisting of a disulphide-linked heterodimer (Ti) of relative molecular mass 80,000–90,000 (Mr 80–90K) which is noncovalently associated with a set of at least three proteins of Mr 20–28K termed CD3 (Leu4, T3)1–3. Whereas both chains of Ti, an acidic α-chain of Afr 48–54K and a more basic β-chain of Mr 40–44 K, contain variable and constant region domains, the component peptides of CD3 are invariant4–8. Several laboratories have more recently reported the expression of CD3 in association with a novel protein9–12. On the surface of long-term T-cell lines and one thymocyte clone this novel structure consists of a 40K protein noncovalently linked to a 55 or 62K protein9,10 identified as the protein product of the Ti γ-chain gene, a T-cell specific gene which like the Ti α-and Ti β-chain genes undergoes rearrangement of variable (V) and joining (J) region gene segments13–16. On the human T-cell leukaemic line PEER we have detected only a single 55K gly-coprotein associated with CD311. We here demonstrate that an anti-Ti γ-peptide antiserum reacts with the 55K CD3-associated protein on PEER. Most previously described human Ti γ-chain complementary DNA clones encode the products of non-functional rearrangements17,18. One of the Ti γ cDNAs isolated from PEER, however, represents a functional rearrangement reported for the first time in a cell which expresses a Ti γ-chain protein product on the cell surface. Interestingly, a 48-base-pair (bp) sequence in the constant (C) region domain of this functional Ti γ-chain cDNA is triplicated in PEER and duplicated in other cDNAs isolated from PEER and other cell lines.
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
Meuer, S. C. et al. J. exp. Med. 157, 705–719 (1983).
Borst, J., Alexander, S., Elder, J. & Terhorst, C. J. biol. Chem. 258, 5135–5141 (1983).
Brenner, M. B., Trowbridge, I. S. & Strominger, J. L. Cell 40, 183–190 (1985).
Reinherz, E. L. et al. Proc. natn. Acad. Sci. U.S.A. 80, 4104–4108 (1983).
Kappler, J. et al. Cell 35, 295–302 (1983).
Borst, J., Prendiville, M. A. & Terhorst, C. J. Immun. 128, 1560–1565 (1982).
Weiss, A. & Stobo, J. D. J. exp. Med. 160, 1284–1299 (1984).
Ohashi, P. S. et al. Nature 316, 606–609 (1985).
Brenner, M. B. et al. Nature 322, 145–149 (1986).
Bank, I. et al. Nature 322, 179–181 (1986).
Weiss, A., Newton, M. & Crommie, D. Proc. natn. Acad. Sci. U.S.A. 83, 6998–7002 (1986).
Moingeon, P. et al. Nature 323, 638–640 (1986).
Saito, H. et al. Nature 309, 757–762 (1984).
Hayday, A. C. et al. Cell 40, 259–269 (1985).
Quertermous, T. et al. Science 231, 252–255 (1986).
LeFranc, M.-P., Forster, A., Baer, R., Stinson, M. A. & Rabbits, T. H. Cell 45, 237–246 (1986).
Quertermous, T. et al. Nature 322, 184–187 (1986).
Dialynas, D. P. et al. Proc. natn. Acad. Sci. U.S.A. 83, 2619–2623 (1986)
Raulet, D. H., Garman, R. D., Saito, H. & Tonegawa, S. Nature 314, 103–107 (1985).
Born, W., Rathbun, G., Tucker, P., Marrack, P. & Kappler, J. Science 234, 479–482 (1986).
Sangster, R. N., Minowada, J., Suciu-Foca, N., Minden, M. & Mak, T. W. J. exp. Med. 163, 1491–1508 (1986).
Pernis, B. & Axel, R. Cell 41, 13–16 (1985).
Wong, X.-F. & Calame, K. Cell 43, 659–665 (1985).
Garman, R. D., Doherty, P. J. & Raulet, D. H. Cell 45, 733–742 (1986).
Reth, M., Gehrmann, P., Petrac, E. & Wiese, P. Nature 322, 840–842 (1986).
Iwamoto, A. et al. J. exp. Med. 163, 1203–1212 (1986).
Lanier, L. et al. J. exp. Med. (in the press).
Sanger, F., Nicklen, S. & Coulson, A. Proc. natn. Acad. Sci. U.S.A. 74, 5463–5467 (1977).
Littman, D. R., Thomas, Y., Maddon, P. J., Chess, L. & Axel, R. Cell 40, 237–246 (1985).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Littman, D., Newton, M., Crommie, D. et al. Characterization of an expressed CDS-associated Ti γ-chain reveals Cγ domain polymorphism. Nature 326, 85–88 (1987). https://doi.org/10.1038/326085a0
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1038/326085a0
This article is cited by
-
Immunopathogenesis of juvenile rheumatoid arthritis: Role of T cells and MHC
Immunologic Research (1995)
-
T-cell antigen receptors in rheumatoid arthritis
Immunologic Research (1994)
-
Specific recognition of staphylococcal enterotoxin A by human T cells bearing receptors with the Vγ9 region
Nature (1990)
-
The role ofγδ T cells in the normal and disordered immune system
Klinische Wochenschrift (1990)
-
A human immunoglobulinIGHG3 allele (Gmb0, b1, c3, c5, u) with anIGHG4 converted region and three hinge exons
Immunogenetics (1989)
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.
