Modulation of the Activation of Extracellular Signal-Regulated Kinase (ERK) and the Production of Inflammatory Mediators by ADP-Ribosylation Inhibitors
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C. Le Page
Abstract
ADP-ribosylation is involved in nuclear factor κB (NF-κB)-dependent gene expression induced by lipopolysaccharide in murine macrophages. Here we have investigated the mechanism by which ADP-ribosylation inhibitors block signaling pathways induced in macrophages. In RAW264.7 macrophages the inducers of NF-κB activate the production of reactive oxygen species and three mitogenactivated protein kinases (MAPK), the extracellular signal regulated kinase (ERK), the c-jun N-terminal kinase/stress-activated protein kinase (JNK), and p38. We demonstrate that ADP-ribosylation inhibitors specifically inhibit ERK MAPK activation and reduce the release of inflammatory mediators such as tumor necrosis factor α (TNF-α), IL-6 and nitrite.
Copyright © 2003 by Walter de Gruyter GmbH & Co. KG
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- Mechanisms and Biological Consequences of Nitrosative Stress
- Regulation of the Expression of Inducible Nitric Oxide Synthase
- Nitrosative Stress and Transcription
- Nitric Oxide Signalling with a Special Focus on Lipid-Derived Mediators
- Potential of Embryonic and Adult Stem Cells in vitro
- Ribosomal Tolerance and Peptide Bond Formation
- Transcription of Cathepsin B in Glioma Cells: Regulation by an E-Box Adjacent to the Transcription Initiation Site
- The Catalytically Active Domain in the A Subunit of Calcineurin
- HIV TAT Basic Peptide Is Not a High-Affinity Ligand for VEGF Receptor 2
- Immunogenicity and Protectivity of Plasmodium falciparum EBA-175 Peptide and Its Analog Is Associated with α-Helical Region Shortening and Displacement
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