Skip Navigation



Glycobiology Advance Access published online on June 2, 2004
Glycobiology, doi:10.1093/glycob/cwh103
This Article
Right arrow Advance Access manuscript (PDF) Freely available
Right arrow All Versions of this Article:
14/9/841    most recent
cwh103v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Duvet, S.
Right arrow Articles by Cacan, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Duvet, S.
Right arrow Articles by Cacan, R.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Received April 14, 2004
Revised May 25, 2004
Accepted May 27, 2004

ORIGINAL ARTICLES

Discrimination between lumenal and cytosolic sites of deglycosylation in endoplasmic reticulum associated degradation of glycoproteins by using benzyl mannose in CHO cell lines

Sandrine Duvet 1, François Foulquier 1, Anne-Marie Mir 1, Frédéric Chirat 1, René Cacan 1*

1 Unité de Glycobiologie Structurale et Fonctionnelle, UMR CNRS 8576, IFR 118, GDR CNRS 2590, Université des Sciences et Technologies de Lille, Villeneuve d'Ascq, France

* To whom correspondence should be addressed. E-mail: rene.cacan{at}univ-lille1.fr.


  Abstract

Recent studies demonstrated that deglycosylation step is a prerequisite for endoplasmic reticulum associated degradation of misfolded glycoproteins. Here we report the benefit of the use of benzyl-mannose during pulse-chase experiments to study the subcellular location of the deglycosylation step in CHO cell lines. Benzyl-mannose inhibited in vivo both, the ER-to-cytosol transport of oligomannosides and the trimming of cytosolic labeled oligomannosides by the cytosolic mannosidase. We pointed out the occurrence of two subcellular sites of deglycosylation. The first one is located in the ER lumen and led to the formation of Man8GlcNAc2 (isomer B) in wild type CHO cell line and Man4GlcNAc2 in Man-P-Dol deficient cell line. The second one was revealed in CHO mutant cell lines for which a high rate of glycoprotein degradation was required. It occured in the cytosol and led to the liberation of oligosaccharides species with one GlcNAc residue and with a pattern similar to the one bound onto glycoproteins. The cytosolic deglycosylation site was not specific of CHO mutant cell lines since we demonstrated the occurrence of the cytosolic pathway when the formation of truncated glycans was induced in wild type cells.

Key words: Free oligomannosides, Chinese hamster ovary cells, N-glycosylation, peptide N-glycanase, Endoplasmic reticulum associated degradation, benzyl mannose


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 GlycobiologyHome page
I. Chantret and S. E H Moore
Free oligosaccharide regulation during mammalian protein N-glycosylation
Glycobiology, March 1, 2008; 18(3): 210 - 224.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.