Abstract
Surface expression of TCR dimers by cells synthetizing three or four distinct types of receptor chains was analyzed. Cells containing intact γ, α, and β chains had only γδ dimers on the cell surface. In human PEER cells, addition of a functional α chain led to the loss of γδ dimer expression and expression of only αβ dimers. This result was not due to transcriptional down-regulation of the γ or δ loci. In murine cells expressing all four chains, both γδ and αβ dimers could be demonstrated on a single cell. No other chain combinations (αγ, αδ, βγ, βδ) were detected. Thus, there is stringent control of assembly and/or transport of TCR heterodimers, such that functional receptors consist only of αβ and γδ pairs, and no additional repertoire diversity is generated by cross pairing.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1003-1020 |
| Number of pages | 18 |
| Journal | Journal of Experimental Medicine |
| Volume | 168 |
| Issue number | 3 |
| DOIs | |
| State | Published - Sep 1 1988 |
ASJC Scopus subject areas
- Immunology and Allergy
- Immunology
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