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A diarrheal pathogen, enteropathogenic Escherichia coli (EPEC), triggers a flux of inositol phosphates in infected epithelial cells

Enteropathogenic Escherichia coli (EPEC) is a bacterial pathogen that causes diarrhea in infants by adhering to intestinal epithelial cells. EPEC induces host cell protein phosphorylation and increases intracellular calcium levels that may function to initiate cytoskeletal rearrangement. We found th...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1994
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2191415/
https://www.ncbi.nlm.nih.gov/pubmed/8113690
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collection PubMed
description Enteropathogenic Escherichia coli (EPEC) is a bacterial pathogen that causes diarrhea in infants by adhering to intestinal epithelial cells. EPEC induces host cell protein phosphorylation and increases intracellular calcium levels that may function to initiate cytoskeletal rearrangement. We found that EPEC triggers the release of inositol phosphates (IPs) after adherence of bacteria to cultured epithelial cells. We also demonstrated that the EPEC-induced flux of IPs precedes actin rearrangement and bacterial invasion. EPEC mutants and tyrosine protein kinase inhibitors were used to establish that formation of IPs is dependent on tyrosine phosphorylation of a 90-kD HeLa protein. Collectively these results suggest that EPEC-induced tyrosine phosphorylation of a host cell substrate(s) leads to release of IPs, which may then trigger cytoskeletal rearrangement.
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spelling pubmed-21914152008-04-16 A diarrheal pathogen, enteropathogenic Escherichia coli (EPEC), triggers a flux of inositol phosphates in infected epithelial cells J Exp Med Articles Enteropathogenic Escherichia coli (EPEC) is a bacterial pathogen that causes diarrhea in infants by adhering to intestinal epithelial cells. EPEC induces host cell protein phosphorylation and increases intracellular calcium levels that may function to initiate cytoskeletal rearrangement. We found that EPEC triggers the release of inositol phosphates (IPs) after adherence of bacteria to cultured epithelial cells. We also demonstrated that the EPEC-induced flux of IPs precedes actin rearrangement and bacterial invasion. EPEC mutants and tyrosine protein kinase inhibitors were used to establish that formation of IPs is dependent on tyrosine phosphorylation of a 90-kD HeLa protein. Collectively these results suggest that EPEC-induced tyrosine phosphorylation of a host cell substrate(s) leads to release of IPs, which may then trigger cytoskeletal rearrangement. The Rockefeller University Press 1994-03-01 /pmc/articles/PMC2191415/ /pubmed/8113690 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
A diarrheal pathogen, enteropathogenic Escherichia coli (EPEC), triggers a flux of inositol phosphates in infected epithelial cells
title A diarrheal pathogen, enteropathogenic Escherichia coli (EPEC), triggers a flux of inositol phosphates in infected epithelial cells
title_full A diarrheal pathogen, enteropathogenic Escherichia coli (EPEC), triggers a flux of inositol phosphates in infected epithelial cells
title_fullStr A diarrheal pathogen, enteropathogenic Escherichia coli (EPEC), triggers a flux of inositol phosphates in infected epithelial cells
title_full_unstemmed A diarrheal pathogen, enteropathogenic Escherichia coli (EPEC), triggers a flux of inositol phosphates in infected epithelial cells
title_short A diarrheal pathogen, enteropathogenic Escherichia coli (EPEC), triggers a flux of inositol phosphates in infected epithelial cells
title_sort diarrheal pathogen, enteropathogenic escherichia coli (epec), triggers a flux of inositol phosphates in infected epithelial cells
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2191415/
https://www.ncbi.nlm.nih.gov/pubmed/8113690