This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Musch, M. W.
Right arrow Articles by Chang, E. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Musch, M. W.
Right arrow Articles by Chang, E. B.
Right arrowPubmed/NCBI databases
*Gene*GEO Profiles
*HomoloGene*UniGene
*Substance via MeSH

 Previous Article  |  Next Article 

Infection and Immunity, June 2004, p. 3187-3194, Vol. 72, No. 6
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.6.3187-3194.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Bacterial Superantigen-Treated Intestinal Epithelial Cells Upregulate Heat Shock Proteins 25 and 72 and Are Resistant to Oxidant Cytotoxicity

Mark W. Musch,1 Elaine O. Petrof,2 Keishi Kojima,1 Hongyu Ren,1 Derek M. McKay,3 and Eugene B. Chang1*

The Martin Boyer Laboratories, Inflammatory Bowel Disease Research Center,1 Section of Infectious Diseases, Department of Medicine, The University of Chicago, Chicago, Illinois 60637,2 Intestinal Disease Research Programme, McMaster University, Hamilton, Ontario, Canada L8N 3Z53

Received 13 November 2003/ Returned for modification 31 December 2003/ Accepted 19 February 2004

While the pathological events evoked by infection are commonly described, effective host responses to bacteria and their products should primarily be protective. Heat shock protein (Hsp) expression is upregulated by many stimuli and serves to maintain intracellular protein integrity. The ability of the prototypic superantigen, Staphylococcus aureus enterotoxin B (SEB) to induce Hsps was investigated with BALB/c mice and by in vitro addition to the murine small intestinal epithelial cell line MSIE. SEB-treated (5 or 100 µg intraperitoneally) mice revealed increased Hsp25 and Hsp72, but not Hsc73, in jejunal lymphocytes and epithelial cells. A similar Hsp response to SEB occurred in MSIE cells and was preceded by activation of the ERK1/2 and p38 mitogen-activated protein kinases but not the SAPK/JNK pathway; pharmacological inhibition of ERK1/2, but not p38, significantly reduced SEB-induced Hsps. Moreover, SEB-treated MSIE cells were protected against oxidant-induced cytotoxicity (measured by 51Cr release) and F-actin depolymerization. Thus, SEB exposure results in a rapid induction of the Hsp25 and Hsp72 in intestinal epithelial cells, both directly and through lymphocyte activation, and we suggest that this event is important in protecting the gut from damage by Staphylococcus infection or in the reparatory process and may be a generalized response to lumen-derived bacterial toxins.

* Corresponding author. Mailing address: The IBD Research Center, Department of Medicine (MC6084), The University of Chicago, 5841 South Maryland Ave., Chicago, IL 60637. Phone: (773) 702-6458. Fax: (773) 702-2281. E-mail: echang{at}medicine.bsd.uchicago.edu.

Editor: J. B. Bliska

Infection and Immunity, June 2004, p. 3187-3194, Vol. 72, No. 6
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.6.3187-3194.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Petrof, E. O., Musch, M. W., Ciancio, M., Sun, J., Hobert, M. E., Claud, E. C., Gewirtz, A., Chang, E. B. (2008). Flagellin is required for salmonella-induced expression of heat shock protein Hsp25 in intestinal epithelium. Am. J. Physiol. Gastrointest. Liver Physiol. 294: G808-G818 [Abstract] [Full Text]  
  • Kammanadiminti, S. J., Chadee, K. (2006). Suppression of NF-{kappa}B Activation by Entamoeba histolytica in Intestinal Epithelial Cells Is Mediated by Heat Shock Protein 27. J. Biol. Chem. 281: 26112-26120 [Abstract] [Full Text]  
  • Henderson, B., Allan, E., Coates, A. R. M. (2006). Stress Wars: the Direct Role of Host and Bacterial Molecular Chaperones in Bacterial Infection. Infect. Immun. 74: 3693-3706 [Full Text]  
  • Enoh, V. T., Lin, C. Y., Varma, T. K., Sherwood, E. R. (2006). Differential effect of imipenem treatment on injury caused by cecal ligation and puncture in wild-type and NK cell-deficient {beta}2-microgloblin knockout mice. Am. J. Physiol. Gastrointest. Liver Physiol. 290: G277-G284 [Abstract] [Full Text]  
  • Arvans, D. L., Vavricka, S. R., Ren, H., Musch, M. W., Kang, L., Rocha, F. G., Lucioni, A., Turner, J. R., Alverdy, J., Chang, E. B. (2005). Luminal bacterial flora determines physiological expression of intestinal epithelial cytoprotective heat shock proteins 25 and 72. Am. J. Physiol. Gastrointest. Liver Physiol. 288: G696-G704 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»