Abstract
In human T lymphocytes the antigen receptor (Ti) is associated non-covalently on the cell surface with the invariant T3 antigen which comprises 3 chains: two glycosylated polypeptides of relative molecular mass 26,000 (Mr26K) and 21K (γ and δ) and one non-N-glycosylated polypeptide of Mr 19K (ε)1–7. The proposed function of T3 is to transduce the activation signals delivered via the antigen receptor8–13. Recently we have shown that phorbol esters, which stimulate protein kinase C, can induce phosphorylation of the γ subunit of the T3 antigen14,15. But the critical question is whether T3 phosphorylation occurs as a normal consequence of immune activation of T lymphocytes. In this respect, it has been shown that immune stimulation of murine T cells results in phosphorylation of Ti-associated polypeptides that may be the functional analogues of the human T3 antigen16,17. We have therefore monitored T3 phosphorylation after exposure of human T cells to antigen or phytohaemagglutinin (PHA). The data show that both stimuli initiate phosphorylation of the γ subunit of the T3 antigen which indicates that T3 phosphorylation is a physiological response to immune activation.
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Cantrell, D., Davies, A., Londei, M. et al. Association of phosphorylation of the T3 antigen with immune activation of T lymphocytes. Nature 325, 540–542 (1987). https://doi.org/10.1038/325540a0
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DOI: https://doi.org/10.1038/325540a0
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