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• W4313333781 endingPage "5616" @default.
• W4313333781 startingPage "5608" @default.
• W4313333781 abstract "Abstract Sodium salicylate (NaSal) and other nonsteroidal anti-inflammatory drugs (NSAIDs) coordinately inhibit the activity of NF-κB, activate heat shock transcription factor 1 and suppress cytokine gene expression in activated monocytes and macrophages. Because our preliminary studies indicated that these effects could be mimicked by inhibitors of signal transduction, we have studied the effects of NSAIDs on signaling molecules potentially downstream of LPS receptors in activated macrophages. Our findings indicate that ribosomal S6 kinase 2 (RSK2), a 90-kDa ribosomal S6 kinase with a critical role as an effector of the RAS-mitogen-activated protein kinase pathway and a regulator of immediate early gene transcription is a target for inhibition by the NSAIDs. NSAIDs inhibited the activity of purified RSK2 kinase in vitro and of RSK2 in mammalian cells and suppressed the phosphorylation of RSK2 substrates cAMP response element binding protein (CREB) and I-κBα in vivo. Additionally, NaSal inhibited the phosphorylation by RSK2 of CREB and I-κBα on residues crucial for their transcriptional activity in vivo and thus repressed CREB and NF-κB-dependent transcription. These experiments suggest that RSK2 is a target for NSAIDs in the inhibition of monocyte-specific gene expression and indicate the importance of RSK2 and related kinases in cell regulation, indicating a new area for anti-inflammatory drug discovery." @default.
• W4313333781 created "2023-01-06" @default.
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• W4313333781 date "1999-11-15" @default.
• W4313333781 modified "2023-10-11" @default.
• W4313333781 title "Salicylic Acid and Aspirin Inhibit the Activity of RSK2 Kinase and Repress RSK2-Dependent Transcription of Cyclic AMP Response Element Binding Protein- and NF-κB-Responsive Genes" @default.
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• W4313333781 doi "https://doi.org/10.4049/jimmunol.163.10.5608" @default.
• W4313333781 hasPublicationYear "1999" @default.
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