Characterization of an expressed CDS-associated Ti γ-chain reveals Cγ domain polymorphism

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.

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