Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Role of N-linked glycosylation in expression of E-selectin on human endothelial cells.
Jönköping University, School of Health Science, HHJ, Dep. of Natural Science and Biomedicine. Jönköping University, School of Health Science, HHJ. Ageing - living conditions and health. Jönköping University, School of Health Science, HHJ. Biomedical Platform.
1995 (English)In: European Journal of Immunology, ISSN 0014-2980, Vol. 25, no 9, 2452-2459 p.Article in journal (Refereed) Published
Abstract [en]

E-selectin is a cytokine-inducible membrane glycoprotein capable of mediating adhesion of leukocytes to endothelial cells. It is highly glycosylated, containing 11 sites for N-linked glycosylation. N-Glycosylation of E-selectin was analyzed by endoglycosidase treatment. Analysis of immunoprecipitated E-selectin from human umbilical vein endothelial cells (HUVEC) by polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate showed that E-selectin was completely resistant to endoglycosidase H, but sensitive to peptide N-glycanase F digestion. This suggested that all N-linked oligosaccharide chains were of the complex type. The role of N-linked glycosylation in surface expression and secretion of E-selectin was studied using interleukin-1-stimulated HUVEC, cultured in the presence of the soluble glycosylation inhibitors tunicamycin or castanospermine. Cell surface expression was analyzed by indirect flow cytometry. N-Glycosylation was blocked by tunicamycin, and resulted in a significantly reduced surface expression of E-selectin, whereas castanospermine only marginally reduced E-selectin expression. The deglycosylated forms of E-selectin were also found to be fully capable of mediating adhesion of HT-29 cells in vitro. In conclusion, these studies show that E-selectin is heavily glycosylated with complex type N-linked oligosaccharides and that N-glycosylation is important for expression of E-selectin on human endothelial cells.

Place, publisher, year, edition, pages
1995. Vol. 25, no 9, 2452-2459 p.
Keyword [en]
Cell Adhesion, E-Selectin/*metabolism, Endothelium; Vascular/cytology/*metabolism, Enzyme Inhibitors/pharmacology, Flow Cytometry, Glycoside Hydrolases, Glycosylation/drug effects, Humans, Indolizines/pharmacology, Interleukin-1/pharmacology, Research Support; Non-U.S. Gov't, Tumor Cells; Cultured, Tunicamycin/pharmacology
Identifiers
URN: urn:nbn:se:hj:diva-7139PubMedID: 7589110OAI: oai:DiVA.org:hj-7139DiVA: diva2:128004
Available from: 2008-12-11 Created: 2008-12-11 Last updated: 2009-12-02Bibliographically approved

Open Access in DiVA

No full text

Other links

PubMedhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Retrieve&list_uids=7589110&dopt=Citation

Search in DiVA

By author/editor
Strindhall, Jan
By organisation
HHJ, Dep. of Natural Science and BiomedicineHHJ. Ageing - living conditions and healthHHJ. Biomedical Platform
In the same journal
European Journal of Immunology

Search outside of DiVA

GoogleGoogle Scholar

Altmetric score

Total: 197 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf