Sphingomyelin, glycosphingolipids, and ceramide signalling in cells exposed to p-fimbriated Escherichia coli
(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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https://lup.lub.lu.se/record/dd1e3c79-01ef-42e9-a042-526387caf63d
- author
- Hedlund, Maria LU ; Duan, Rui-Dong LU ; Nilsson, Åke LU and Svanborg, Catharina LU
- organization
- publishing date
- 1998
- 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}}, }