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Am J Physiol Cell Physiol 283: C31-C41, 2002. First published February 6, 2002; doi:10.1152/ajpcell.00113.2001
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Vol. 283, Issue 1, C31-C41, July 2002

MAP kinases contribute to IL-8 secretion by intestinal epithelial cells via a posttranscriptional mechanism

Humberto B. Jijon1, William J. Panenka1, Karen L. Madsen2, and Howard G. Parsons1

1 Gastrointestinal Research Group, University of Calgary, Calgary T2N 4N1; and 2 Division of Gastroenterology, University of Alberta, Edmonton, Alberta, Canada T6G 2C2

The intracellular pathways that regulate intestinal epithelial gene expression are poorly understood. In this study we examined the roles of extracellular signal-regulated kinase (ERK) and p38 in the expression of interleukin-8 (IL-8) and intercellular adhesion molecule-1 (ICAM-1) using the human intestinal cell line HT-29. HT-29 cells were treated with tumor necrosis factor-alpha (TNF-alpha ) in the presence or absence of ERK and p38 pathway inhibitors. TNF-alpha treatment resulted in increased IL-8 and ICAM-1 protein and mRNA synthesis, increased ERK and p38 activity, and activation of the transcription factors activator protein-1 (AP-1) and nuclear factor-kappa B (NF-kappa B). Inhibition of the ERK and p38 pathways attenuated IL-8 secretion but did not alter ICAM-1 expression. Furthermore, AP-1 and NF-kappa B DNA binding was not affected by ERK and p38 inhibition. In contrast, ERK and p38 inhibition resulted in the accelerated degradation of the IL-8 mRNA, suggesting that in HT-29 cells, p38 and ERK contribute to TNF-alpha -stimulated IL-8 secretion by intestinal epithelial cells via a posttranscriptional mechanism that involves stabilization of the IL-8 transcript.

enterocyte; intestinal inflammation; signal transduction; mRNA stability


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