p59fyn tyrosine kinase regulates p56lck tyrosine kinase activity and early TCR-mediated signaling |
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Authors: | Lee, Sang-Kyou Shaw, Andrey Maher, Stephen E. Bothwell, Alfred L. M. |
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Affiliation: | Section of Immunobiology and Department of Biology, Yale University School of Medicine New Haven, CT 06520–8011, USA 1 Department of Pathology, Washington University School of Medicine St Louis, MO 63110–1093, USA |
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Abstract: | To study the role of p59fyn in T cell activation, we used antisenseRNA to inhibit p59fyn expression in a T cell clone. Transfectantswith reduced levels of p59fyn were functionally impaired intheir responses to antigen, Con A + recombinant IL-1 and cross-linkingwith anti-TCR mAb. Induction of tyrosine phosphorylation onmost intracellular substrates was greatly reduced. We also notedthat the Ick kinase activity was greatly reduced even thoughthe amount of Ick protein was equivalent to that present inparental D10 cells. Our results suggest that the protein tyrosinekinase p59fyn is critical in TCR-mediated signaling and alsosuggests that p59fyn may regulate p56fyn tyrosine kinase activity. |
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Keywords: | antisense transfectants fyn tyrosine kinase Ick tyrosine kinase T cell activation T cell clone |
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