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J Biol Chem, Vol. 274, Issue 45, 31868-31874, November 5, 1999
B Kinase Activity
and Nuclear Factor B DNA Binding
§,,§, and§¶
From the The transcription factor nuclear factor Lineberger Comprehensive Cancer Center,
¶ Department of Biology, and § Center for
Gastrointestinal Biology and Disease, University of North Carolina,
Chapel Hill, North Carolina 27599-7295
B
(NF-B) coordinates the activation of numerous genes in response to
pathogens and proinflammatory cytokines and is, therefore, pivotal in
the development of acute and chronic inflammatory diseases. In its
inactive state, NF-B is constitutively present in the cytoplasm as a
p50-p65 heterodimer bound to its inhibitory protein IB.
Proinflammatory cytokines, such as tumor necrosis factor (TNF),
activate NF-B by stimulating the activity of the IB kinases
(IKKs) which phosphorylate IB
on serine residues 32 and 36, targeting it for rapid degradation by the 26 S proteasome. This enables
the release and nuclear translocation of the NF-B complex and
activation of gene transcription. Interleukin-10 (IL-10) is a
pleiotropic cytokine that controls inflammatory processes by
suppressing the production of proinflammatory cytokines which are known
to be transcriptionally controlled by NF-B. Conflicting data exists
on the effects of IL-10 on TNF- and LPS-induced NF-B activity in
human monocytes and the molecular mechanisms involved have not been
elucidated. In this study, we show that IL-10 functions to block
NF-B activity at two levels: 1) through the suppression of IKK
activity and 2) through the inhibition of NF-B DNA binding activity.
This is the first evidence of an anti-inflammatory protein inhibiting
IKK activity and demonstrates that IKK is a logical target for blocking
inflammatory diseases.
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