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B
Through Preventing IB Kinase Activation in Respiratory Epithelial Cells1
,
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*
Department of Internal Medicine, Seoul National University College of Medicine, Seoul, Korea;
Clinical Research Institute, Seoul National University Hospital, Seoul, Korea; and
Lung Institute, Seoul National University Medical Research Center, Seoul, Korea
Heat shock protein (HSP) induction confers protection against
diverse forms of cellular and tissue injury. However, the mechanism by
which HSP exerts cytoprotective effects is unclear. Because HSP
induction inhibits genetic expression of pro-inflammatory cytokines,
the transcription of which is dependent on NF-
B activation, we
explored the relationship between the anti-inflammatory effect of
HSP induction and the NF-B/IB
pathway. Both HS and sodium
arsenite treatment increased HSP70 expression time dependently at mRNA
and protein levels. Prior induction of HSP suppressed cytokine-induced
IL-8 and TNF- expression at both mRNA and protein levels. Although
HSP induction did not affect total cellular expression of NF-B,
TNF--induced increase in NF-B-DNA binding activity and nuclear
translocation of the p65 subunit of NF-B were inhibited by prior HSP
induction, suggesting that activation of NF-B was blocked.
Cytokine-induced IB phosphorylation and its degradation were
blocked in HSP-induced cells. Immune complex kinase assays demonstrated
that TNF- induced increase in IB kinase activity was suppressed
by prior HSP induction. These results suggest that the
anti-inflammatory effect of HSP induction in respiratory epithelial
cells is related to stabilization of IB, possibly through the
prevention of IB kinase activation, which thereby inhibits
activation of NF-B.
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