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Physical and Functional Association of Fc R With Protein Tyrosine
Kinase Lyn
Heinz Gulle,
Aysen Samstag,
Martha M. Eibl, and
Hermann M. Wolf
From the Institute of Immunology, University of Vienna, Vienna,
Austria; and Immuno AG, Vienna, Austria.
In this report, we show that the Src family nonreceptor protein
tyrosine kinase (PTK) Lyn associates with aggregated IgA Fc receptor
(Fc R) in the monocytic cell line THP-1. Receptor aggregation and
subsequent immunoprecipitation of receptor complexes with huIgA
adsorbed to nitrocellulose particles shows that Lyn associates with
FcR by a mechanism sensitive to short treatment with the Src
family-selective inhibitor PP1. However, interaction of Lyn with IgG Fc
receptor (Fc R) in THP-1 cells was unaffected by short treatment with
the PTK inhibitor. Cross-linking of FcR induced tyrosine
phosphorylation of several cellular proteins, including p72Syk, which appears to be a major target of early PTK
activity. Unexpectedly, in vitro kinase assays showed that FcR
aggregation-induced tyrosine phosphorylation of Syk did not result in
upregulation of Syk activity. Despite the lack of enhanced Syk kinase
activity, downstream signaling after FcR cross-linking was
functional and induced the release of significant amounts of
interleukin-1 receptor antagonist and interleukin-8. The induction of
cytokine release was completely blocked by PP1, thus confirming the
biological significance of the association of Lyn with aggregated
FcR. Our data show that early signal transduction after FcR
cross-linking as well as FcR-mediated activation of cellular
effector functions depends on Src family kinase activity. The
Src-family PTK involved in FcR-mediated tyrosine phosphorylation
appears to be Lyn, which coprecipitated with aggregated FcR
complexes.
Blood, Vol. 91 No. 2 (January 15), 1998:
pp. 383-391
© 1998 by The American Society of Hematology.
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