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p38 mitogen-activated protein kinase (MAPK) stabilises pro-inflammatory mediator mRNAs by inhibiting AU-rich element (ARE)-mediated decay. We show that in bone-marrow derived murine macrophages tristetraprolin (TTP) is necessary for the p38 MAPK-sensitive decay of several pro-inflammatory mRNAs, including cyclooxygenase-2 and the novel targets interleukin (IL)-6, and IL-1alpha. TTP(-/-) macrophages also strongly overexpress IL-10, an anti-inflammatory cytokine that constrains the production of the IL-6 despite its disregulation at the post-transcriptional level. TTP directly controls IL-10 mRNA stability, which is increased and insensitive to inhibition of p38 MAPK in TTP(-/-) macrophages. Furthermore, TTP enhances deadenylation of an IL-10 3'-untranslated region RNA in vitro.

Original publication

DOI

10.1016/j.febslet.2009.04.039

Type

Journal article

Journal

FEBS Lett

Publication Date

18/06/2009

Volume

583

Pages

1933 - 1938

Keywords

Animals, Base Sequence, In Vitro Techniques, Inflammation Mediators, Interleukin-10, Interleukin-12 Subunit p40, Interleukin-6, MAP Kinase Signaling System, Macrophages, Mice, Mice, Inbred C57BL, Mice, Knockout, RNA Stability, RNA, Messenger, Tristetraprolin, p38 Mitogen-Activated Protein Kinases