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Sphingomyelin, glycosphingolipids, and ceramide signalling in cells exposed to p-fimbriated Escherichia coli

Hedlund, Maria LU ; Duan, Rui-Dong LU ; Nilsson, Åke LU and Svanborg, Catharina LU (1998) In Molecular Microbiology 29(5). p.1297-1306
Abstract
Uropathogenic Escherichia coli attach to epithelial cells through P fimbriae that bind Galα1‐4Galβ‐oligosaccharide sequences in cell surface glycosphingolipids. The binding of P‐fimbriated E. coli to uroepithelial cells causes the release of ceramide, activation of the ceramide signalling pathway and a cytokine response in the epithelial cells. The present study examined the molecular source of ceramide in human kidney A498 cells exposed to P‐fimbriated E. coli. Agonists such as TNF‐α and IL‐1β released ceramide from sphingomyelin by the activation of endogenous sphingomyelinases and hydrolysis of sphingomyelin, and triggered an IL‐6 response. P‐fimbriated E. coli caused a slight increase in endogenous sphingomyelinase activity, but there... (More)
Uropathogenic Escherichia coli attach to epithelial cells through P fimbriae that bind Galα1‐4Galβ‐oligosaccharide sequences in cell surface glycosphingolipids. The binding of P‐fimbriated E. coli to uroepithelial cells causes the release of ceramide, activation of the ceramide signalling pathway and a cytokine response in the epithelial cells. The present study examined the molecular source of ceramide in human kidney A498 cells exposed to P‐fimbriated E. coli. Agonists such as TNF‐α and IL‐1β released ceramide from sphingomyelin by the activation of endogenous sphingomyelinases and hydrolysis of sphingomyelin, and triggered an IL‐6 response. P‐fimbriated E. coli caused a slight increase in endogenous sphingomyelinase activity, but there was no associated sphingomyelin hydrolysis. Instead, the concentration of galactose‐containing glycolipids decreased. We propose that P‐fimbriated E. coli differ from other activators of the ceramide pathway, in that release of ceramide is from receptor glycolipids and not from sphingomyelin. Receptor breakdown may be an efficient host defence strategy, as it reduces the concentration of cell surface receptors, releases soluble receptor analogues and activates an inflammatory response. (Less)
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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Molecular Microbiology
volume
29
issue
5
pages
10 pages
publisher
Wiley-Blackwell
external identifiers
  • scopus:0031659853
ISSN
1365-2958
DOI
10.1046/j.1365-2958.1998.01017.x
language
English
LU publication?
yes
id
dd1e3c79-01ef-42e9-a042-526387caf63d
date added to LUP
2019-02-03 16:21:54
date last changed
2022-01-31 17:21:53
@article{dd1e3c79-01ef-42e9-a042-526387caf63d,
  abstract     = {{Uropathogenic Escherichia coli attach to epithelial cells through P fimbriae that bind Galα1‐4Galβ‐oligosaccharide sequences in cell surface glycosphingolipids. The binding of P‐fimbriated E. coli to uroepithelial cells causes the release of ceramide, activation of the ceramide signalling pathway and a cytokine response in the epithelial cells. The present study examined the molecular source of ceramide in human kidney A498 cells exposed to P‐fimbriated E. coli. Agonists such as TNF‐α and IL‐1β released ceramide from sphingomyelin by the activation of endogenous sphingomyelinases and hydrolysis of sphingomyelin, and triggered an IL‐6 response. P‐fimbriated E. coli caused a slight increase in endogenous sphingomyelinase activity, but there was no associated sphingomyelin hydrolysis. Instead, the concentration of galactose‐containing glycolipids decreased. We propose that P‐fimbriated E. coli differ from other activators of the ceramide pathway, in that release of ceramide is from receptor glycolipids and not from sphingomyelin. Receptor breakdown may be an efficient host defence strategy, as it reduces the concentration of cell surface receptors, releases soluble receptor analogues and activates an inflammatory response.}},
  author       = {{Hedlund, Maria and Duan, Rui-Dong and Nilsson, Åke and Svanborg, Catharina}},
  issn         = {{1365-2958}},
  language     = {{eng}},
  number       = {{5}},
  pages        = {{1297--1306}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{Molecular Microbiology}},
  title        = {{Sphingomyelin, glycosphingolipids, and ceramide signalling in cells exposed to p-fimbriated Escherichia coli}},
  url          = {{http://dx.doi.org/10.1046/j.1365-2958.1998.01017.x}},
  doi          = {{10.1046/j.1365-2958.1998.01017.x}},
  volume       = {{29}},
  year         = {{1998}},
}