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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




Journal article


Febs letters

Publication Date





1933 - 1938


Kennedy Institute of Rheumatology Division, Imperial College London, London, United Kingdom.


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