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RI/CD64) Gene and STAT Protein Binding to the IFN- Response Region (GRR) Are Regulated Differentially in Human Neutrophils and Monocytes by IL-101
Departments of
*
General Pathology and
Biochemistry, University of Verona, Verona, Italy
Since IL-10 has been shown to up-regulate the expression of the
high affinity receptor for IgG (Fc
RI/CD64) in human monocytes, we
examined whether the cytokine exerts a similar action toward
polymorphonuclear neutrophils (PMN). Unexpectedly, we found that in
neutrophils, IL-10 failed to induce either the mRNA accumulation or the
surface expression of FcRI. Consistent with these findings,
stimulation of PMN with IFN-, but not with IL-10, resulted in the
induction of specific DNA-binding activities to the IFN- response
region (GRR), a regulatory element located in the FcRI gene
promoter, required for transcriptional activation. In electrophoretic
mobility shift assays (EMSAs), we confirmed that in PBMC, IL-10 induces
the binding to the GRR of both STAT1 and STAT3, two members of the STAT
family. In neutrophils, however, these activators did not bind to the
GRR in response to IL-10, despite the fact that both STAT1 and STAT3
are expressed in these cells. On the other hand, IFN- was an
efficient inducer of STAT1 binding to the GRR in both PMN and PBMC. The
lack of inducible GRR-binding activity in IL-10-treated PMN could not
be ascribed to a lack of IL-10R, and did not appear to reflect an
inhibitory effect of the cytokine. Taken together, our data suggest
that IL-10 is unable to induce FcRI gene expression in neutrophils
because the intracellular signaling pathway triggered by the cytokine
is impaired at the level of, or upstream of, STAT1 and/or STAT3
activation.
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