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Glycobiology Advance Access originally published online on August 23, 2005
Glycobiology 2005 15(12):1277-1285; 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

Regulation of the chondroitin/dermatan fine structure by transforming growth factor-ß1 through effects on polymer-modifying enzymes

Kerstin Tiedemann1,3,5, Benny Olander1,5, Erik Eklund1,4,5, Lizbet Todorova5, Martin Bengtsson6, Marco Maccarana5, Gunilla Westergren-Thorsson5 and Anders Malmström2,5

5 Department of Cell and Molecular Biology, and 6 Physiological Sciences, Lund University, BMC B11, S-221 84 Lund, Sweden

1 These authors contributed equally to this work.

2 To whom correspondence should be addressed; e-mail: anders.malmstrom{at}medkem.lu.se

3 Present address: Department of Anatomy and Cell Biology, McGill University, 3640, University Street, Montreal, Québec, Canada H3A 2B2

4 Present address: The Burnham Institute, Program for Glycobiology and Carbohydrate Chemistry, 10901 North Torrey Pines Road, La Jolla, CA 92037

Received on March 22, 2005; revised on July 6, 2005; accepted on August 5, 2005

The chondroitin/dermatan sulfate proteoglycans (CS/DSPGs), 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 transforming growth factor-ß (TGF-ß) alone or in combination with epidermal growth factor and platelet-derived growth factor, increase the production of these PGs. 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, whereas 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 polymerase chain reaction (RT–PCR). The C-5 epimerase activity was reduced by 25% in TGF-ß1 treated cells and 50% in fibroblasts treated with the growth factor combination. No change in activity in dermatan 4-O sulfotransferase was observed, and only a minor decrease in dermatan 4-O-sulfotransferase-1 (D4ST-1) mRNA was observed. On the other hand, chondroitin 4-O sulfotransferase activity increased 2-fold upon TGF-ß1 treatment and 3-fold upon treatment with the growth factor combination. This is in agreement with a 2-fold up-regulation of chondroitin-4-O-sulfotransferase 1 (C4ST-1) mRNA, and no changes in chondroitin-4-O-sulfotransferase 2 (C4ST-2) mRNA. Thus, cellular activity and transcript level correlated well with the changes in the structure of the dermatan/chondroitin sulfate chains.

Key words: chondroitin / dermatan / glucuronyl c5-epimerase / sulfotransferase / glycosaminoglycan


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