Temporal regulation of non-transmembrane protein tyrosine kinase enzyme activity following T cell antigen receptor engagement
| Autor: | A L, Burkhardt, B, Stealey, R B, Rowley, S, Mahajan, M, Prendergast, J, Fargnoli, J B, Bolen |
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| Rok vydání: | 1994 |
| Předmět: |
Enzyme Precursors
ZAP-70 Protein-Tyrosine Kinase Molecular Sequence Data Intracellular Signaling Peptides and Proteins Receptors Antigen T-Cell In Vitro Techniques Protein-Tyrosine Kinases Proto-Oncogene Proteins c-fyn Cell Line Enzyme Activation Lymphocyte Specific Protein Tyrosine Kinase p56(lck) Proto-Oncogene Proteins Humans Syk Kinase Tyrosine Amino Acid Sequence Phosphotyrosine Signal Transduction |
| Zdroj: | The Journal of biological chemistry. 269(38) |
| ISSN: | 0021-9258 |
| Popis: | We evaluated in Jurkat T cells the time-dependent responses of Fyn, Lck, Syk, and Zap following antibody-mediated cross-linking of the T cell antigen receptor. Our results show that the protein kinase activities of Fyn and Lck were activated within seconds of receptor cross-linking. Fyn activity, as measured by autophosphorylation and tyrosine phosphorylation of an exogenous substrate, was maximal 5 s to 1 min following receptor cross-linking. Lck was also found to be activated within 5 s of antigen receptor cross-linking but differed from Fyn in that Lck activity was elevated for at least 30 min. Syk and Zap protein kinase activities were found to peak between 5 and 10 min following receptor cross-linking, returning to approximately basal activity levels by 60 min. The protein kinase activities of both Syk and Zap were found to parallel their reactivity in immunoblotting experiments with anti-phosphotyrosine antibodies. Both Syk and Zap were found to associate with the tyrosine-phosphorylated zeta subunit of the T cell antigen receptor. These observations imply that T cell antigen receptor signal transduction involves the activation of multiple members of at least two different families of non-transmembrane protein tyrosine kinases. |
| Databáze: | OpenAIRE |
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