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RI on Mast Cells Is Induced by IgE Binding Through Stabilization and Accumulation of FcRI on the Cell Surface1
,
,¶
Departments of
*
Laboratory Animal Science and
Immunology, Tokyo Metropolitan Organization for Medical Science, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan;
Japan Science and Technology Corporation, Tokyo, Japan;
Department of Experimental Immunology, Institute of Development, Aging and Cancer, Tohoku University, Sendai, Japan; and
¶ Department of Immune Regulation, Tokyo Medical and Dental University, Graduate School, Tokyo, Japan
It has been shown that IgE binding to Fc
RI on mast cells results
in increased FcRI expression, which in turn enhances IgE-dependent
chemical mediator release from mast cells. Therefore, prevention of the
IgE-mediated FcRI up-regulation would be a promising strategy for
management of allergic disorders. However, the mechanism of
IgE-mediated FcRI up-regulation has not been fully elucidated. In
this study, we analyzed kinetics of FcRI on peritoneal mast cells
and bone marrow-derived mast cells. In the presence of brefeldin A,
which prevented transport of new FcRI molecules to the cell surface,
levels of IgE-free FcRI on mast cells decreased drastically during
culture, whereas those of IgE-bound FcRI were stable. In contrast,
levels of Fc
RIII on the same cells were stable even in the absence
of its ligand, indicating that FcRI 
-chain, but not 
- and
-chains, was responsible for the instability of IgE-free FcRI. As
far as we analyzed, there was no evidence to support the idea that IgE
binding to FcRI facilitated synthesis and/or transport of FcRI to
the cell surface. Therefore, the stabilization and accumulation of
FcRI on the cell surface through IgE binding appears to be the major
mechanism of IgE-mediated FcRI up-regulation.
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