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Role of N-linked gl...
Role of N-linked glycosylation in expression of E-selectin on human endothelial cells.
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- Påhlsson, Peter (författare)
- Linköpings universitet,Klinisk kemi,Hälsouniversitetet
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- Strindhall, Jan (författare)
- Linköpings universitet,Jönköping University,HHJ, Avdelningen för naturvetenskap och biomedicin,HHJ. Åldrande - livsvillkor och hälsa,HHJ. Biomedicinsk plattform,Klinisk kemi,Hälsouniversitetet
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- Srinivas, U (författare)
- Hospital Pharmacy, University Hospital, Linköping, Sweden
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- Lundblad, Arne (författare)
- Linköpings universitet,Klinisk kemi,Hälsouniversitetet
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(creator_code:org_t)
- Wiley, 1995
- 1995
- Engelska.
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Ingår i: European Journal of Immunology. - : Wiley. - 0014-2980 .- 1521-4141. ; 25:9, s. 2452-2459
- Relaterad länk:
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http://www.ncbi.nlm....
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https://urn.kb.se/re...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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.
Nyckelord
- 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
- MEDICINE
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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