Protein tyrosine kinase p59 super(fyn) is associated with the T cell receptor-CD3 complex in functional human lymphocytes
The binding of antigen to the multicomponent T cell antigen receptor (TcR)-CD3 complex leads to the activation of several signal transduction pathways which results in T lymphocyte proliferation and lymphokine secretion by molecular mechanisms and catalytic molecules as yet poorly defined. One of th...
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Veröffentlicht in: | European journal of immunology 1992-01, Vol.22 (1), p.283-286 |
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Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Online-Zugang: | Volltext |
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Zusammenfassung: | The binding of antigen to the multicomponent T cell antigen receptor (TcR)-CD3 complex leads to the activation of several signal transduction pathways which results in T lymphocyte proliferation and lymphokine secretion by molecular mechanisms and catalytic molecules as yet poorly defined. One of the earliest events that follows the triggering of the antigen-specific TcR-CD3 complex is a rapid tyrosine phosphorylation of several intracellular substrates suggesting stimulation of at least one protein tyrosine kinase (PTK). The findings provide direct evidence for a significant association of p59 super(fyn) with the TcR-CD3 complex under physiologically relevant conditions in functional T lymphocytes. They suggest that p59 super(fyn) is a crucial component of the TcR signal transduction machinery and that one of the earliest consequences of antigen recombination by the TcR is p59 super(fyn)-mediated phosphorylation of intracellular substrates on tyrosine residues. |
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ISSN: | 0014-2980 |