Glycobiology Advance Access published online on January 4, 2006
Glycobiology, doi:10.1093/glycob/cwj075
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1 From the Department of Molecular Biosciences, University of Oslo, Box 1041, Blindern, 0316 Oslo, Norway
* To whom correspondence should be addressed. Serglycin with a green fluorescent protein tag (SG-GFP) expressed in epithelial Madin-Darby canine kidney (MDCK) cells is secreted mainly (85 %) into the apical medium, but the glycosaminoglycan chains on the SG-GFP protein core secreted basolaterally (15 %) carry most of the sulfate added during biosynthesis (Tveit et al., 2005). Here we report further differences in apical and basolateral glycosaminoglycan synthesis. The less intensely sulfated chondroitin sulfate (CS) chains on apically secreted SG-GFP are longer than CS chains attached to basolateral SG-GFP, while the heparan sulfate (HS) chains are of similar lengths. When the supply of 3'-phosphoadenosine-5'-phosphosulfate (PAPS) is limited by chlorate treatment, the synthesis machinery maintains sulfation of HS chains on basolateral SG-GFP until it is inhibited at 50 mM chlorate, while basolateral CS chains lose sulfate already at 12.5 mM chlorate and become longer. Apically, incorporation of 35S-sulfate into CS is reduced to a lesser extent at higher chlorate concentrations than basolateral CS, although apical CS is less intensely sulfated than basolateral CS in control cells. Similarly to what was found for basolateral HS, sulfation of apical HS was not reduced at chlorate concentrations below 50 mM. Also, protein-free, xyloside-based glycosaminoglycan chains secreted basolaterally are more intensely sulfated than their apical counterpart, supporting the view that separate apical and basolateral pathways exist for glycosaminoglycan synthesis and sulfation. Introduction of benzyl
Received September 23, 2005
Revised December 22, 2005
Accepted December 30, 2005
Article
Differences in the apical and basolateral pathways for glycosaminoglycan biosynthesis in Madin-Darby canine kidney (MDCK) cells
Tram Thu Vuong 1,
Kristian Prydz 1 *,
and
Heidi Tveit 1
Kristian Prydz, E-mail: kristian.prydz{at}imbv.uio.no
Abstract 
-D-xyloside (BX) to the GAG synthesis machinery reduces the apical secretion of SG-GFP dramatically and also the modification of SG-GFP by HS.
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