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J Biol Chem, Vol. 274, Issue 1, 264-269, January 1, 1999
From the Kennedy Institute of Rheumatology, 1 Aspenlea Road,
Hammersmith, London W6 8LH, United Kingdom
p38 mitogen-activated protein kinase (MAPK) is
activated by inflammatory stimuli such as bacterial lipopolysaccharide
(LPS), interleukin-1, and tumor necrosis factor. We have previously
shown that the pyridinyl imidazole SB 203580, which inhibits it, blocks the interleukin-1 induction of cyclooxygenase-2 (COX-2) and matrix metalloproteinase 1 and 3 mRNAs in fibroblasts. Here we explore the
role of p38 MAPK in the response of human monocytes to LPS. 0.1 µM SB 203580 significantly inhibited the LPS induction of COX-2 and tumor necrosis factor protein and mRNAs. The activity of
MAPK-activated protein kinase-2 (a substrate of p38 MAPK) in the cells
was commensurately reduced. Some isoforms of c-jun
N-terminal kinase (which is also activated by LPS) are sensitive to SB
203580; the inhibitor had little effect on monocyte c-jun
N-terminal kinases up to 2 µM. We investigated the
mechanism of inhibition of COX-2 induction. Transcription (measured by
a nuclear run-on assay) was 60% inhibited by SB 203580 (2 µM). Importantly, we found that p38 MAPK was essential
for stabilizing COX-2 mRNA: when cells stimulated for 4 h with
LPS were treated with actinomycin D, COX-2 mRNA decayed slowly.
Treatment of stimulated cells with 2 µM SB 203580 caused
a rapid disappearance of COX-2 mRNA, even with actinomycin D
present. We conclude p38 MAPK plays a role in the transcription and
stabilization of COX-2 mRNA.
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