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Department of Nutrition, School of Medicine, University of Tokushima, Tokushima, Japan
Treatment of murine resident peritoneal macrophages with
macrophage-CSF (M-CSF) up-regulated the synthesis of a discrete set of
proteins, including a 26-kDa protein (p26). The sequence of 20
NH2-terminal amino acids of the purified p26 was identical
with the mouse homolog of a human IgE-dependent histamine-releasing
factor (HRF). Among macrophage activators tested (M-CSF,
granulocyte-macrophage-CSF, IL-3, TNF-
, IFN-
, and LPS), only
M-CSF could up-regulate the p26 HRF synthesis by cultured macrophages.
M-CSF not only increased the levels of p26 HRF mRNA and protein, but
also stimulated the secretion of an N-glycosylated p26 HRF
with a m.w. of 30 kDa. Repeated injections of M-CSF into mouse
peritoneal cavity for 4 days elicited macrophages expressing abundant
p26 HRF. A single i.p. injection of M-CSF failed to increase the p26
HRF level in peritoneal macrophages of thioglycollate-, LPS-, or
adjuvant-treated mice, while M-CSF challenge to OVA-immunized mice
caused macrophage infiltration and overproduction of p26 HRF, similarly
as did OVA challenge. The Ag-specific priming for enhanced synthesis
and secretion of p26 HRF by M-CSF was also demonstrated in cultured
macrophages prepared from OVA-immunized mice. An i.p. injection of
M-CSF or recombinant p26 HRF triggered eosinophil recruitment, even in
the absence of the Ag, in the sensitized mice, but not in normal mice.
Furthermore, recombinant p26 HRF could induce eosinophilia without
marked macrophage and lymphocyte infiltrations. Our results suggest
that p26 HRF secreted by M-CSF-stimulated macrophages may be an
important mediator for the late phase allergic
inflammation.
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