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Glycobiology Advance Access published online on August 23, 2005
Glycobiology, doi:10.1093/glycob/cwj027
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© The Author 2005. Published by Oxford University Press. All rights reserved. The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oupjournals.org
Received March 22, 2005
Revised July 6, 2005
Accepted August 5, 2005

Article

Regulation of the Chondroitin/Dermatan fine structure by Transforming Growth Factor-{beta}1 through effects on Polymer-modifying enzymes

Kerstin Tiedemann 1 {ddagger}, Benny Olander 2 {ddagger}, Erik Eklund 3 {ddagger}, Lizbet Todorova 2, Martin Bengtsson 4, Marco Maccarana 2, Gunilla Westergren-Thorsson 2, and Anders Malmström 2*

1 Present address: Department of Anatomy and Cell Biology, McGill University, 3640, University Street, Montreal, Quebec H3A 2B2, Canada
2 From the Department of Cell and Molecular Biology, Lund University, BMC C13, S-221 84 Lund, Sweden
3 Present address: The Burnham Institute, Program for Glycobiology and Carbohydrate Chemistry, 10901 N. Torrey Pines Rd, La Jolla, 92037 CA, USA
4 From the Department of Physiological Sciences, BMC B11, S-221 84 Lund, Sweden

* To whom correspondence should be addressed.
Anders Malmström, E-mail: Anders.Malmstrom{at}medkem.lu.se


  Abstract

The chondroitin/dermatan sulfate proteoglycans biglycan, decorin and versican play several important roles in extracellular matrix influencing matrix organization, cell proliferation and recruitment. Moreover, they bind and regulate growth factors in the extracellular matrix. We have previously shown that cultured human lung fibroblasts treated with TGF-{beta} alone or in combination with epidermal growth factor and platelet-derived growth factor, increase the production of these proteoglycans. In this report we describe that the structure of their galactosaminoglycan side-chains is altered albeit there is no alteration of polysaccharide length. The findings showed that iduronic acid content is reduced by 50% in decorin and biglycan, while 4-O-sulfation is increased 2-fold in versican. To unravel the mechanism behind these changes, the activities of chondroitin C-5 epimerase and of O-sulfotransferases in cellular fractions prepared from fibroblasts were quantitated, and transcript levels of the relevant sulfotransferases were measured by real time PCR. The C-5 epimerase activity was reduced by 25% in TGF-{beta}1 treated cells and 50 % in fibroblasts treated with the growth factor combination. No change in activity in dermatan 4-O-sulfotranferase was observed and only a minor decrease in dermatan 4-O-sulfotransferase-I (D4ST-1) mRNA was observed. On the other hand, chondroitin 4-O-sulfotranferase activity increased two-fold upon TGF-{beta}1 treatment, and three-fold upon treatment with the growth-factor combination. This is in agreement with a two-fold up-regulation of 4-O-sulfotransferase-I (C4ST-1) mRNA, and no changes in C4ST-2 mRNA. Thus cellular activity and transcript level correlated well with the changes in the structure of the dermatan/chondroitin sulfate chains.

Keywords: Chondroitin/Dermatan/glucuronyl C5-epimerase/Sulfotransferase/Glycosaminoglycan.
{ddagger}These authors contributed equally to the study
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