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ß Mediates the Lipopolysaccharide-Induced Activation of Transcription Factor Stat1 in Mouse Macrophages: Pivotal Role of Stat1 in Induction of the Inducible Nitric Oxide Synthase Gene1
*
Wilkinson Laboratory of the Kansas Cancer Institute and Department of Pathology and Laboratory Medicine, University of Kansas Medical Center, Kansas City, KS 66160; and
Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, MD 20814
We have examined the role of Stat1
in the induction by LPS of
the mouse inducible nitric oxide synthase (EC 1.14.13.39) gene. LPS
induced both the tyrosine phosphorylation of Stat1 and the
production of nitric oxide in a time- and dose-dependent manner. The
phosphorylation of Stat1 elicited by LPS differed from that observed
using IFN-
or IFN-ß, in that LPS induced less phosphorylated
protein and the time course of induction was much delayed (2–4 h
compared with 30 min). Cycloheximide inhibited LPS-mediated Stat1
phosphorylation. In addition, cell culture supernatants derived from
macrophages treated with LPS for 4 h could be transferred to naive
macrophage cultures resulting in rapid (30 min), rather than delayed (4
h), phosphorylation of Stat1. Together, these results implicated an
autocrine/paracrine effector protein(s) in the phosphorylation process.
LPS stimulated phosphorylation of Stat1 in peritoneal macrophages
derived from IFN--knockout mice, negating any possibility that
IFN- was the mediator. By contrast, neutralizing Ig raised against
mouse IFN-ß inhibited both the delayed LPS-mediated
phosphorylation of Stat1 and the rapid induction of phosphorylation
induced by supernatants from LPS-stimulated cultures. Collectively,
these results show that LPS-induced IFN-ß production, Stat1
activation, and nitrite accumulation closely parallel one another,
suggesting that indirect activation of transcription factor Stat1 by
IFN-ß is a critical determinant of LPS-mediated inducible nitric
oxide synthase gene expression.
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