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Am J Physiol Gastrointest Liver Physiol 281: G890-G898, 2001;
0193-1857/01 $5.00
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Vol. 281, Issue 4, G890-G898, October 2001

EPEC-activated ERK1/2 participate in inflammatory response but not tight junction barrier disruption

Suzana D. Savkovic, Akila Ramaswamy, Athanasia Koutsouris, and Gail Hecht

Department of Medicine, Section of Digestive and Liver Diseases, University of Illinois, West Side Veterans Affairs Medical Center, Chicago, Illinois 60612

Enteropathogenic Escherichia coli (EPEC) alters many functions of the host intestinal epithelia. Inflammation is initiated by activation of nuclear factor (NF)-kappa B, and paracellular permeability is enhanced via a Ca2+- and myosin light-chain kinase (MLCK)-dependent pathway. The aims of this study were to identify signaling pathways by which EPEC triggers inflammation and to determine whether these pathways parallel or diverge from those that alter permeability. EPEC-induced phosphorylation and degradation of the primary inhibitor of NF-kappa B (Ikappa Balpha ) were tumor necrosis factor (TNF)-alpha and interleukin (IL)-1beta independent. In contrast to Salmonella typhimurium, EPEC-stimulated Ikappa Balpha degradation and IL-8 expression did not require Ca2+. Instead, extracellular signal-regulated kinase (ERK)-1/2 was significantly and rapidly activated. ERK1/2 inhibitors attenuated Ikappa Balpha degradation and IL-8 expression. Although ERK1/2 can activate MLCK, its inhibition had no impact on EPEC disruption of the tight junction barrier. In conclusion, EPEC-induced inflammation 1) is TNF-alpha and IL-1beta receptor independent, 2) utilizes pathways differently from S. typhimurium, 3) requires ERK1/2, and 4) employs signals that are distinct from those that alter permeability. This is the first time that EPEC-activated signaling cascades have been linked to independent functional consequences.

permeability; nuclear factor-kappa B; primary inhibitor of nuclear factor-kappa B; interleukin-8; enteric pathogens; enteropathogenic Escherichia coli; extracellular signal-regulated kinase-1/2


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