Role of the ceramide signalling pathway in cytokine responses to P fimbriated Escherichia coli.
(1996) In Journal of Experimental Medicine 183(3). p.1037-1044- Abstract
- Escherichia coli express fimbriae-associated adhesins through which they attach to mucosal cells and activate a cytokine response. The receptors for E. coli P fimbriae are the globoseries of glycosphingolipids; Gal alpha 1-->4Gal beta-containing oligosaccharides bound to ceramide in the outer leaflet of the lipid bilayer. The receptors for type 1 fimbriae are mannosylated glycoproteins rather than glycolipids. This study tested the hypothesis that P-fimbriated E. coli elicit a cytokine response through the release of ceramide in the receptor-bearing cell. We used the A498 human kidney cell line, which expressed functional receptors for P and type 1 fimbriae and secreted higher levels of interleukin (IL)-6 when exposed to the fimbriated... (More)
- Escherichia coli express fimbriae-associated adhesins through which they attach to mucosal cells and activate a cytokine response. The receptors for E. coli P fimbriae are the globoseries of glycosphingolipids; Gal alpha 1-->4Gal beta-containing oligosaccharides bound to ceramide in the outer leaflet of the lipid bilayer. The receptors for type 1 fimbriae are mannosylated glycoproteins rather than glycolipids. This study tested the hypothesis that P-fimbriated E. coli elicit a cytokine response through the release of ceramide in the receptor-bearing cell. We used the A498 human kidney cell line, which expressed functional receptors for P and type 1 fimbriae and secreted higher levels of interleukin (IL)-6 when exposed to the fimbriated strains than to isogenic nonfimbriated controls. P-fimbriated E. coli caused the release of ceramide and increased the phosphorylation of ceramide to ceramide 1-phosphate. The IL-6 response to P-fimbriated E. coli was reduced by inhibitors of serine/threonine kinases but not by other protein kinase inhibitors. In contrast, ceramide levels were not influenced by type 1-fimbriated E. coli, and the IL-6 response was insensitive to the serine/threonine kinase inhibitors. These results demonstrate that the ceramide-signaling pathway is activated by P-fimbriated E. coli, and that the receptor specificity of the P fimbriae influences this process. We propose that this activation pathway contributes to the cytokine induction by P-fimbriated E. coli in epithelial cells. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/f4c92884-e7c0-4b3d-a2fb-4cf6d829ed09
- author
- Hedlund, Maria LU ; Svensson, Majlis LU ; Nilsson, Åke LU ; Duan, Rui-Dong LU and Svanborg, Catharina LU
- organization
- publishing date
- 1996
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Experimental Medicine
- volume
- 183
- issue
- 3
- pages
- 1037 - 1044
- publisher
- Rockefeller University Press
- external identifiers
-
- pmid:PMC2192311
- scopus:0030006201
- ISSN
- 1540-9538
- DOI
- 10.1084/jem.183.3.1037
- language
- English
- LU publication?
- yes
- id
- f4c92884-e7c0-4b3d-a2fb-4cf6d829ed09
- date added to LUP
- 2019-02-03 11:08:34
- date last changed
- 2024-02-14 16:56:56
@article{f4c92884-e7c0-4b3d-a2fb-4cf6d829ed09,
abstract = {{Escherichia coli express fimbriae-associated adhesins through which they attach to mucosal cells and activate a cytokine response. The receptors for E. coli P fimbriae are the globoseries of glycosphingolipids; Gal alpha 1-->4Gal beta-containing oligosaccharides bound to ceramide in the outer leaflet of the lipid bilayer. The receptors for type 1 fimbriae are mannosylated glycoproteins rather than glycolipids. This study tested the hypothesis that P-fimbriated E. coli elicit a cytokine response through the release of ceramide in the receptor-bearing cell. We used the A498 human kidney cell line, which expressed functional receptors for P and type 1 fimbriae and secreted higher levels of interleukin (IL)-6 when exposed to the fimbriated strains than to isogenic nonfimbriated controls. P-fimbriated E. coli caused the release of ceramide and increased the phosphorylation of ceramide to ceramide 1-phosphate. The IL-6 response to P-fimbriated E. coli was reduced by inhibitors of serine/threonine kinases but not by other protein kinase inhibitors. In contrast, ceramide levels were not influenced by type 1-fimbriated E. coli, and the IL-6 response was insensitive to the serine/threonine kinase inhibitors. These results demonstrate that the ceramide-signaling pathway is activated by P-fimbriated E. coli, and that the receptor specificity of the P fimbriae influences this process. We propose that this activation pathway contributes to the cytokine induction by P-fimbriated E. coli in epithelial cells.}},
author = {{Hedlund, Maria and Svensson, Majlis and Nilsson, Åke and Duan, Rui-Dong and Svanborg, Catharina}},
issn = {{1540-9538}},
language = {{eng}},
number = {{3}},
pages = {{1037--1044}},
publisher = {{Rockefeller University Press}},
series = {{Journal of Experimental Medicine}},
title = {{Role of the ceramide signalling pathway in cytokine responses to P fimbriated Escherichia coli.}},
url = {{http://dx.doi.org/10.1084/jem.183.3.1037}},
doi = {{10.1084/jem.183.3.1037}},
volume = {{183}},
year = {{1996}},
}