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*
Department of Pathology, General Pathology Unit, University of Verona, Verona, Italy; and
DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, CA 94304
We have recently shown that IL-10 fails to trigger Stat3 and Stat1
tyrosine phosphorylation in freshly isolated human neutrophils. In this
study, we report that IL-10 can nonetheless induce Stat3 tyrosine
phosphorylation and the binding of Stat1 and Stat3 to the
IFN-
response region or the high-affinity synthetic derivative of
the c-sis-inducible element in neutrophils that have been
cultured for at least 3 h with LPS. Similarly, the ability of
IL-10 to up-regulate suppressor of cytokine signaling (SOCS)-3 mRNA was
dramatically enhanced in cultured neutrophils and, as a result,
translated into the SOCS-3 protein. Since neutrophils’ acquisition of
responsiveness to IL-10 required de novo protein synthesis, we assessed
whether expression of IL-10R1 or IL-10R2 was modulated in cultured
neutrophils. We detected constitutive IL-10R1 mRNA and protein
expression in circulating neutrophils, at levels which were much lower
than those observed in autologous monocytes or lymphocytes. In
contrast, IL-10R2 expression was comparable in both cell types.
However, IL-10R1 (but not IL-10R2) mRNA and protein expression was
substantially increased in neutrophils stimulated by LPS. The ability
of IL-10 to activate Stat3 tyrosine phosphorylation and SOCS-3
synthesis and to regulate IL-1 receptor antagonist and
macrophage-inflammatory protein 1
release in LPS-treated neutrophils
correlated with this increased IL-10R1 expression, and was abolished by
neutralizing anti-IL-10R1 and anti-IL-10R2 Abs. Our results
demonstrate that the capacity of neutrophils to respond to IL-10, as
assessed by Stat3 tyrosine phosphorylation, SOCS-3 expression, and
modulation of cytokine production, is very dependent on the level of
expression of IL-10R1.
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