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Differential activation of the tyrosine kinases ZAP-70 and Syk after Fc
gamma RI stimulation
N Taylor, T Jahn, S Smith, T Lamkin, L Uribe, Y Liu, DL Durden and K Weinberg
Division of Research Immunology, Childrens Hospital Los Angeles, CA, USA.
Engagement of the high-affinity IgG Fc receptor (Fc gamma RI) activates a
signal transduction pathway involving tyrosine phosphorylation of
associated kinases. We compared the activation of the related protein
tyrosine kinases (PTKs), Syk and ZAP-70, in Fc gamma RI-mediated signaling.
Cross-linking of the Fc gamma RI multimeric receptor in monocytic cells
results in tyrosine phosphorylation of the Fc epsilon RI gamma subunit and
association of Syk with this complex. We stably introduced ZAP-70 via a
retroviral vector into two monocytic cell lines, U937 and THP-1, which
normally do not express ZAP-70. Neither Syk nor MAP kinase activation was
affected by the presence of ZAP-70. Although transduced ZAP-70 had in vitro
kinase activity and associated with Fc epsilon RI gamma after receptor
aggregation, it was not tyrosine phosphorylated. In contrast, both ZAP-70
and Syk were phosphorylated in a T-cell line in which their respective
levels of expression were similar to those detected in U937/ZAP-70 cells.
Therefore, these results suggest that requirements for Syk and ZAP-70
phosphorylation are distinct in a monocytic cell context.
Volume 89,
Issue 2,
pp. 388-396,
01/15/1997
Copyright © 1997 by The American Society of Hematology
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