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A p38 MAP kinase inhibitor regulates stability of interleukin‐1‐induced cyclooxygenase‐2 mRNA
Author(s) -
Ridley Simon H.,
Dean Jonathon L.E.,
Sarsfield Simon J.,
Brook Matthew,
Clark Andrew R.,
Saklatvala Jeremy
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01342-8
Subject(s) - p38 mitogen activated protein kinases , microbiology and biotechnology , cyclooxygenase , messenger rna , protein kinase a , mapk/erk pathway , hela , chemistry , arachidonic acid , kinase , protein kinase c , biology , biochemistry , enzyme , gene , cell
The mechanism by which p38 mitogen‐activated protein kinase (MAPK) regulates the induction of cyclooxygenase (COX)‐2 by interleukin‐1 (IL‐1) has been investigated in HeLa cells. SB 203580, an inhibitor of p38 MAPK, in the range 0.1–1 μM inhibited IL‐1‐stimulated PGE 2 (but not arachidonic acid) release and this was associated with inhibition of induction of COX‐2 protein and mRNA. IL‐1 stimulated COX‐2 transcription in HeLa cells about 2‐fold as judged by both reporter gene and nuclear run‐on assays. The inhibitor had no significant effect on this. However, in cells previously stimulated with IL‐1 it caused rapid destabilisation of COX‐2 mRNA independently of on‐going transcription. The results suggest a novel function for p38 MAPK in the regulation of mRNA stability.