Skip Navigation



Glycobiology Advance Access published online on October 27, 2007
Glycobiology, doi:10.1093/glycob/cwm121
This Article
Right arrow Advance Access manuscript (PDF) Freely available
Right arrow Supplementary Data
Right arrow All Versions of this Article:
18/1/53    most recent
cwm121v1
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 Dick, G.
Right arrow Articles by Prydz, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dick, G.
Right arrow Articles by Prydz, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2007. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Over-expression of the 3'-phosphoadenosine 5'-phosphosulfate (PAPS) Transporter 1 Increases Sulfation of Chondroitin Sulfate in the Apical Pathway of MDCK II Cells

Gunnar Dick, Frøy Grøndahl and Kristian Prydz

From Department of Molecular Biosciences, University of Oslo, Box 1041 Blindern, 0316 Oslo, Norway

Address correspondence to: Kristian Prydz, Department of Molecular Biosciences, University of Oslo, Box 1041, 0316 Oslo, Norway. Tel: (+47) 22856753 Fax: (+47) 22854443, e-mail: kristian.prydz{at}imbv.uio.no

Received on July 13, 2007; accepted on October 24, 2007

The canine 3'-phosphoadenosine 5'-phosphosulfate (PAPS) transporter 1 fused to GFP was stably expressed with a typical Golgi localization in MDCK II cells (MDCK II-PAPST1). The capacity for PAPS uptake into Golgi vesicles was enhanced to almost three times that of Golgi vesicles isolated from untransfected cells. We have previously shown that chondroitin sulfate proteoglycans (CSPGs) are several times more intensely sulfated in the basolateral than the apical secretory pathway in MDCK II cells (Tveit et al. 2005. J. Biol. Chem. 280, 29596-603). Here we demonstrate that increased availability of PAPS in the Golgi lumen enhances the sulfation of CSPG in the apical pathway several times, while sulfation of CSPGs in the basolateral pathway shows minor changes. Sulfation of heparan sulfate proteoglycans are essentially unchanged. Our data indicate that CS sulfation in the apical pathway of MDCK II cells occurs at suboptimal conditions, either because the sulfotransferases involved have high Km values, or there is a lower PAPS concentration in the lumen of the apical secretory route than in the basolateral counterpart.

Key words: Golgi apparatus / MDCK epithelial cells / PAPS / proteoglycan / sulfation


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




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.