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-Associated Protein-70 (ZAP-70) Tyrosine Kinase: Relevance for Invasion and Migration of a T Cell Hybridoma1
Division of Cell Biology, The Netherlands Cancer Institute, Amsterdam, The Netherlands
We previously showed that LFA-1-dependent in vitro invasion and in
vivo migration of a T cell hybridoma was blocked in cells
overexpressing a truncated dominant-negative 
-associated protein
(ZAP)-70. The truncated ZAP-70 also blocked LFA-1-dependent chemotaxis
through ICAM-1-coated filters induced by 1 ng/ml stromal cell-derived
factor-1, but not LFA-1-independent chemotaxis induced by 100 ng/ml
stromal cell-derived factor-1. This suggested that LFA-1 engagement
triggers a signal that amplifies a weak chemokine signal and that
dominant-negative ZAP-70 blocks this LFA-1 signal. Here we show that
cross-linking of part of the LFA-1 molecules with Abs causes activation
of free LFA-1 molecules (not occupied by the Ab) on the same cell,
which then bind to ICAM-2 on other cells. This causes cell aggregation
that was also blocked by dominant-negative ZAP-70. Thus, an LFA-1
signal involving ZAP-70 activates other LFA-1 molecules, suggesting
that the chemokine signal can be amplified by multiple cycles of LFA-1
activation. The chemokine and the LFA-1 signal were both blocked by a
phospholipase C inhibitor and a calpain inhibitor, suggesting that one
of the amplified signals is the phospholipase C-dependent activation of
calpain. Finally, we show that both Src-homology 2 domains are required
for inhibition of invasion, chemotaxis, and aggregation by the
truncated ZAP-70, suggesting that ZAP-70 interacts with a
phosphorylated immunoreceptor tyrosine-based activation motif (ITAM)
sequence. Remarkably, this is not an ITAM in the TCR/CD3 complex
because this is not expressed by this T cell
hybridoma.
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