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RIIB1
Laboratoire d’Immunologie Cellulaire et Clinique, Institut National de la Santé et de la Recherche Médicale Unité 255, Institut Curie, Paris, France
Fc
RIIB are single-chain low-affinity receptors for IgG that bear
an immunoreceptor tyrosine-based inhibition motif in their
intracytoplasmic domain and that negatively regulate immunoreceptor
tyrosine-based activation motif-dependent cell activation. They are
widely expressed by cells of hematopoietic origin. We investigated here
whether FcRIIB could also negatively regulate protein tyrosine
kinase receptor (RTK)-dependent cell proliferation. As an experimental
model, we used growth factor-dependent mast cells that constitutively
express FcRIIB and c-kit, an RTK prototype. We
found that anti-c-kit Abs mimicked the effect of
stem cell factor and induced thymidine incorporation in
FcRIIB-/-, but not in wild-type (wt) mast cells unless
FcRIIB were blocked or anti-c-kit
F(ab')2 were used. When coaggregated with
c-kit by intact Abs in wt mast cells, FcRIIB
inhibited thymidine incorporation, as well as cell proliferation, and
inhibition was correlated with an arrest of cells in G1 during the cell
cycle. The coaggregation of c-kit with FcRIIB did not
affect ligand-induced c-kit phosphorylation and induced
the tyrosyl-phosphorylation of FcRIIB, which selectively recruited
the Src homology 2 domain-bearing inositol 5-phosphatase SHIP. Our
results indicate that IgG Abs to growth factors or growth factor
receptors may control RTK-dependent proliferation of a variety of cells
that express FcRIIB.
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