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* Stress Signaling Unit, Laboratory of Cellular and Molecular Biology, National Institute on Aging, Intramural Research Program, National Institutes of Health, Baltimore, MD 21224; and
GlaxoSmithKline Pharmaceuticals, King of Prussia, PA 19406
Exposure of macrophages to LPS elicits the production of
proinflammatory cytokines, such as TNF-
, through complex signaling
mechanisms. Mitogen-activated protein (MAP) kinases play a critical
role in this process. In the present study, we have addressed the role
of MAP kinase phosphatase-1 (MKP-1) in regulating proinflammatory
cytokine production using RAW264.7 macrophages. Analysis of MAP kinase
activity revealed a transient activation of c-Jun N-terminal kinase
(JNK) and p38 after LPS stimulation. Interestingly, MKP-1 was induced
concurrently with the inactivation of JNK and p38, whereas blocking
MKP-1 induction by triptolide prevented this inactivation. Ectopic
expression of MKP-1 accelerated JNK and p38 inactivation and
substantially inhibited the production of TNF- and IL-6. Induction
of MKP-1 by LPS was found to be extracellular signal-regulated kinase
dependent and involved enhanced gene expression and increased protein
stability. Finally, MKP-1 expression was also induced by
glucocorticoids as well as cholera toxin B subunit, an agent capable of
preventing autoimmune diseases in animal models. These findings
highlight MKP-1 as a critical negative regulator of the macrophage
inflammatory response, underscoring its premise as a potential target
for developing novel anti-inflammatory
drugs.
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