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1 The Martin Boyer Laboratories, Inflammatory Bowel Disease Research Center, The University of Chicago, Chicago, IL, USA
* To whom correspondence should be addressed. E-mail: echang{at}medicine.bas.uchicago.edu.
Protection of colonic epithelial integrity and function is critical, as compromises in mucosal functions can lead to adverse and potentially life-threatening effects. The gut flora may contribute to this protection, in part through the sustained induction of cytoprotective heat shock proteins (Hsps) in surface colonocytes. In this study, we investigated whether E. coli lipopolysaccharide (LPS) mediates bacteria-induced Hsps using cultured young adult mouse colon (YAMC) cells, an in vitro model of the colonic epithelium. E. coli LPS led to an epithelial cell type-specific induction of Hsp25 in a time- and concentration-dependent manner, an effect which did not involve changes in Hsp72. YAMC cells expressed the toll like receptors (TLR) TLR2 and TLR4, but not the co-stimulatory CD14 molecule. While LPS stimulated both the p38 and extracellular signal regulated kinases (ERK)1/2, but not the stress activated protein kinase/c-jun N-terminal kinase (SAPK/JNK), signaling pathways in the YAMC cells, all three were stimulated in RAW macrophage cells (where no LPS-induced Hsp25 expression was observed). The p38 inhibitor SB203580 and the MEK-1 (MAP kinase kinase-1) inhibitor PD98059 inhibited Hsp25 induction by LPS. LPS treatment also conferred protection against actin depolymerization induced by the oxidant monochloramine. The Hsp25 dependence of the LPS protective effect was outlined in inhibitor studies and through adenovirus-mediated overexpression of Hsp25. In conclusion, LPS may be an important mediator of enteric bacteria-induced expression of intestinal epithelial Hsp25, an effect that may contribute to F-actin stabilization under physiological as well as pathophysiological conditions and thus protection of colonic epithelial integrity.
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