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Departments of Immunology and Internal Medicine, Mayo Clinic and Mayo Foundation, Rochester, MN 55905
Human eosinophils have been reported to express both the mRNA and
protein for the high affinity IgE receptor (Fc
RI); it is speculated
that this receptor plays a role in eosinophil mediator release in
allergic diseases. However, questions still remain. How much of the
Fc
RI protein is actually expressed on the cell surface of the
eosinophil? If they are present, are these IgE receptors associated
with effector functions of eosinophils? To address these issues, we
studied blood eosinophils from patients with ragweed hay fever. A high
level of low affinity IgG receptor (Fc
RII, CD32), but no expression
of Fc
RI, was detectable on the eosinophil surface by standard FACS
analysis. However, after in vitro sensitization with biotinylated
chimeric IgE (cIgE), cell-bound cIgE was detected by PE-conjugated
streptavidin. This cIgE binding was partially inhibited by
anti-Fc
RI mAb, suggesting that eosinophils do express minimal
amounts of Fc
RI detectable only by a sensitive method. Indeed, FACS
analysis of whole blood showed that eosinophils express
0.5% of the
Fc
RI that basophils express. When stimulated with human IgE or
anti-human IgE, these eosinophils did not exert effector functions;
there was neither production of leukotriene C4 or
superoxide anion nor any detectable degranulation response. In
contrast, eosinophils possessed membrane-bound human IgG and showed
functional responses when stimulated with human IgG or anti-human
IgG. Thus, IgG and/or cytokines, such as IL-5, appear to be more
important for eosinophil activation in allergic diseases than
IgE.
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