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Vol. 282, Issue 1, 452-458, 1997
Department of Pharmacology, New York Medical College, Valhalla, New
York
Regulation of prostaglandin endoperoxide synthase-2 (PGHS-2) mRNA
levels by serine-threonine phosphatases was examined in murine
fibrosarcoma methylcholanthrene-101 cells. Okadaic acid (OA), a
serine-threonine phosphatase inhibitor, induced PGE2
production and a significant increase in PGHS-2 immunoreactive protein.
A specific PGHS-2 inhibitor, N-(2-cyclohexyloxy-4-nitrophenyl)
methanesulphonamide, completely abolished the OA-mediated increase in
PGE2 production, which suggests that the PGE2
formed in response to OA was derived from PGHS-2. OA-mediated PGHS-2
mRNA accumulation was observed at 1 hr, remained elevated for 24 hr and
was blocked by actinomycin D, which indicates that OA increases PGHS-2
gene transcription. A significant post-transcriptional mechanism also
contributed to the increased PGHS-2 mRNA accumulation, because the mRNA
half-life was approximately 4 to 5 h in OA-stimulated cells. Tumor
necrosis factor-
, but not OA, activated transcription factor nuclear
factor-
B in methylcholanthrene-101 cells, as demonstrated by
translocation of the nuclear factor-B complex to the nucleus and
disappearance of the cytoplasmic inhibitory protein, IB-. We
conclude that inhibition of serine-threonine phosphatases contributes
to the up-regulation of PGHS-2 expression in an NF-B-independent
manner.
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