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RI, on Human Mast Cells: Up-Regulation by IFN-1
Laboratory of Allergic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892
Biologically relevant activation of human mast cells through Fc
receptors is believed to occur primarily through the high-affinity IgE
receptor Fc
RI. However, the demonstration in animal models that
allergic reactions do not necessarily require Ag-specific IgE, nor the
presence of a functional IgE receptor, and the clinical occurrence of
some allergic reactions in situations where Ag-specific IgE appears to
be lacking, led us to examine the hypothesis that human mast cells
might express the high-affinity IgG receptor Fc
RI and in turn be
activated through aggregation of this receptor. We thus first
determined by RT-PCR that resting human mast cells exhibit minimal
message for FcRI. We next found that IFN- up-regulated the
expression of FcRI. This was confirmed by flow cytometry, where
FcRI expression on human mast cells was increased from 
2 to 44%
by IFN- exposure. FcRI, FcRII, and FcRIII expression was
not affected. Scatchard plots were consisted with these data where the
average binding sites for monomeric IgG1
(Ka = 4–5 x 108
M-1) increased from 2,400 to 12,100–17,300 per cell.
Aggregation of FcRI on human mast cells, and only after IFN-
exposure, led to significant degranulation as evidenced by histamine
release (24.5 ± 4.4%): and up-regulation of mRNA expression for
specific cytokines including TNF-
, GM-CSF, IL-3 and IL-13. These
findings thus suggest another mechanism by which human mast cells may
be recruited into the inflammatory processes associated with some
immunologic and infectious diseases.
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