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Division of Cell Biology, The Netherlands Cancer Institute, Amsterdam, The Netherlands
Dissemination of T cell hybridomas in mice, a model for in vivo
migration of memory T cells and for T lymphoma metastasis, depends on
the chemokine stromal cell-derived factor-1 (SDF-1) and the integrin
LFA-1 and correlates well with invasion into fibroblast cultures. In
addition to the known role of the pertussis toxin-sensitive
heterotrimeric GTPase Gi, we show that also the pertussis
toxin-insensitive GTPase Gq/11 is required for
dissemination and invasion. Furthermore, we show that the small
GTPases, Cdc42 and RhoA, are involved, and that invasion is blocked
by inhibitors of actinomyosin contraction. Gq/11, RhoA, and
contraction are specifically required for LFA-1 activation, since 1)
they are essential for LFA-1-dependent migration toward low SDF-1
concentrations through ICAM-1-coated filters, but not for migration
toward high SDF-1 levels, which is LFA-1 independent; 2) G protein
(AlF4-)-induced adhesion to ICAM-1 requires
RhoA and contraction; 3) constitutively active Gq induces
aggregation, mediated by LFA-1. We previously reported that binding of
this activated LFA-1 to ICAM-1 triggers a signal, transduced by the
-associated protein 70 tyrosine kinase, that activates additional
LFA-1 molecules. This amplification of LFA-1 activation is essential
for invasion. We show here that -associated protein 70-induced LFA-1
activation requires neither Cdc42 and RhoA nor contraction and is thus
quite different from that induced by SDF-1. We conclude that two modes
of LFA-1 activation, with distinct underlying mechanisms, are required
for the in vivo migration of T cell hybridomas.
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