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Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, MD 20814
In this study, the effect of in vitro endotoxin tolerance on
LPS-induced mitogen-activated protein kinase activation, transcription
factor induction, and cytokine, chemokine, and Toll-like receptor (TLR)
2 and 4 gene expression, as well as the involvement of TNF and IL-1
signaling pathways in tolerance, were examined. Pretreatment of mouse
macrophages with LPS inhibited phosphorylation of the extracellular
signal-regulated kinases, c-Jun NH2-terminal kinases, and
p38 kinase; degradation of I-
B
(inhibitory protein that
dissociates from NF-
B) and I-
Bß; and activation of the
transcription factors NF-
B and AP-1 in response to subsequent LPS
stimulation. These changes were accompanied by suppression of
LPS-induced expression of mRNA for GM-CSF, IFN-
-inducible
protein-10, KC, JE/monocyte chemoattractant protein-1,
macrophage-inflammatory protein-1ß, and macrophage-inflammatory
protein-2, with concurrent inhibition of chemokine secretion. In
contrast to control cells, endotoxin-tolerant macrophages exhibited an
increased basal level of TLR2 mRNA, and failed to increase levels of
TLR2 mRNA or to down-regulate TLR4 gene expression upon restimulation
with LPS. As judged by transcription factor activation, LPS and IL-1
were found to induce a state of cross-tolerance against each other,
while no such reciprocal effect was seen for LPS and TNF-
. In
addition, macrophages from TNFR I/II double knockout mice were LPS
tolerizable, and blocking of endogenous TNF-
with TNFR-Fc fusion
protein did not affect the capacity of LPS to tolerize macrophages.
These data extend our understanding of LPS-signaling mechanisms that
are inhibited in endotoxin-tolerized macrophages and suggest that
endotoxin tolerance might result from impaired expression and/or
functions of common signaling intermediates involved in LPS and IL-1
signaling.
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