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Butyrate inhibits interleukin-1-mediated nuclear factor-kappa B activation in human epithelial cells.

Authors
  • Lührs, H
  • Gerke, T
  • Boxberger, F
  • Backhaus, K
  • Melcher, R
  • Scheppach, W
  • Menzel, T
Type
Published Article
Journal
Digestive diseases and sciences
Publication Date
Sep 01, 2001
Volume
46
Issue
9
Pages
1968–1973
Identifiers
PMID: 11575451
Source
Medline
License
Unknown

Abstract

Nuclear factor-kappa B (NF-kappaB) is a critical transcription factor for the inducible expression of multiple genes involved in inflammation. NF-kappaB is sequestered in the cytoplasm by inhibitory IkappaB proteins. Extracellular stimuli, notably interleukin-1beta (IL-1beta) and tumor necrosis factor alpha (TNF-alpha) activate NF-kappaB nuclear translocation via IkappaB phosphorylation and degradation. Since previous reports suggest that the short chain fatty acid butyrate has antiinflammatory properties, the effects of butyrate on NF-kappaB nuclear translocation in human epithelial cells (HeLa229) were tested. In cells pretreated with butyrate, a time- and dose-dependent inhibition of IL-1beta-mediated NF-kappaB nuclear translocation was observed. However, IkappaB alpha phosphorylation and degradation occurred rapidly in both butyrate pretreated and nonpretreated cells, respectively. These data indicate that inhibition of IL-1beta-induced NF-kappaB activation by butyrate does not require an intact IkappaB alpha protein.

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