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N-Glycans modulate the activation of gp130 in mouse embryonic neural precursor cells
- Source :
- Biochemical and Biophysical Research Communications. 386:101-104
- Publication Year :
- 2009
- Publisher :
- Elsevier BV, 2009.
-
Abstract
- gp130 is a ubiquitously expressed glycoprotein and signal transducer of interleukin 6 family of cytokines. It has been reported that gp130 has 11 potential N-glycosylation sites in the extracellular domain, and nine of them are actually N-glycosylated. However, the structure and functional role of the carbohydrate chains carried by gp130 are totally unknown. In this study, we examined the functional role of N-glycans of gp130 in mouse neuroepithelial cells. In neuroepithelial cells treated with tunicamycin, an N-glycosylation inhibitor, unglycosylated form of gp130 was detected. The unglycosylated gp130 was not phosphorylated in response to leukemia inhibitory factor stimulation. Although the unglycosylated gp130 was found to be expressed on the cell surface, it could not form a heterodimer with leukemia inhibitory factor receptor. These results suggest that N-glycans are required for the activation, but not for the localization, of gp130 in neuroepithelial cells.
- Subjects :
- Glycosylation
Biophysics
Apoptosis
Leukemia inhibitory factor receptor
Biology
Leukemia Inhibitory Factor
digestive system
Biochemistry
Article
Mice
chemistry.chemical_compound
Polysaccharides
Stress, Physiological
Cytokine Receptor gp130
Animals
Phosphorylation
Molecular Biology
Embryonic Stem Cells
Neurons
chemistry.chemical_classification
Tunicamycin
digestive, oral, and skin physiology
Cell Biology
Glycoprotein 130
biological factors
Cell biology
Neuroepithelial cell
chemistry
cardiovascular system
Protein Multimerization
biological phenomena, cell phenomena, and immunity
Signal transduction
Glycoprotein
Leukemia inhibitory factor
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 386
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi.dedup.....b46322bb2d1534ef795f44eb220c6dab