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J Biol Chem, Vol. 274, Issue 37, 26448-26453, September 10, 1999

Inhibition of Interleukin-1-stimulated NF-kappa B RelA/p65 Phosphorylation by Mesalamine Is Accompanied by Decreased Transcriptional Activity

Laurence J. EganDagger §, Dennis C. Mays§, Catherine J. Huntoonparallel , Michael P. Bellparallel , M. Gennett Pike§, William J. SandbornDagger , James J. Lipsky§, and David J. McKeanparallel

From the Dagger  Division of Gastroenterology and Hepatology, the § Clinical Pharmacology Unit, and the parallel  Department of Immunology, Mayo Clinic, Rochester, Minnesota 55905

Nuclear factor kappa B (NF-kappa B) is an inducible transcription factor that regulates genes important in immunity and inflammation. The activity of NF-kappa B is highly regulated: transcriptionally active NF-kappa B proteins are sequestered in the cytoplasm by inhibitory proteins, Ikappa B. A variety of extracellular signals, including interleukin-1 (IL-1), activate NF-kappa B by inducing phosphorylation and degradation of Ikappa B, allowing nuclear translocation and DNA binding of NF-kappa B. Many of the stimuli that activate NF-kappa B by inducing Ikappa B degradation also cause phosphorylation of the NF-kappa B RelA (p65) polypeptide. The transactivating capacity of RelA is positively regulated by phosphorylation, suggesting that in addition to cytosolic sequestration by Ikappa B, phosphorylation represents another mechanism for control of NF-kappa B activity. In this report, we demonstrate that mesalamine, an anti-inflammatory aminosalicylate, dose-dependently inhibits IL-1-stimulated NF-kappa B-dependent transcription without preventing Ikappa B degradation or nuclear translocation and DNA binding of the transcriptionally active NF-kappa B proteins, RelA, c-Rel, or RelB. Mesalamine was found to inhibit IL-1-stimulated RelA phosphorylation. These data suggest that pharmacologic modulation of the phosphorylation status of RelA regulates the transcriptional activity of NF-kappa B, independent of nuclear translocation and DNA binding. These findings highlight the importance of inducible phosphorylation of RelA in the control of NF-kappa B activity.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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