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Originally published In Press as doi:10.1074/jbc.M001443200 on May 5, 2000

J. Biol. Chem., Vol. 275, Issue 28, 21255-21261, July 14, 2000
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Tandem Repeats Are Involved in G1 Domain Inhibition of Versican Expression and Secretion and the G3 Domain Enhances Glycosaminoglycan Modification and Product Secretion via the Complement-binding Protein-like Motif*

Bing L. YangDagger , Liu CaoDagger , Chris Kiani, Vivian Lee, Yaou Zhang, Mark E. Adams§, and Burton B. Yang

From the Sunnybrook & Women's College Health Sciences Centre and Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario M4N 3M5, Canada

The large aggregating chondroitin sulfate proteoglycans, including aggrecan, versican (PG-M), neurocan, and brevican, are characterized by N-terminal and C-terminal globular (or selectin-like) domains known as the G1 and G3 domains, respectively. For this study, we generated a series of expression constructs containing various combinations of chicken versican/PG-M domains and a leading peptide of link protein in order to examine the roles of the G1 and G3 domains in versican function. In transfection studies, we observed that the presence of the G1 domain was sufficient to inhibit product secretion, while the G3 domain enhanced this process. We also demonstrated that the G1 domain inhibited the attachment of glycosaminoglycan chains to the core proteins, while the G3 domain enhanced this process. Further studies revealed that inhibition of secretion by G1 was mediated by its two tandem repeats, while G3's promotion of glycosaminoglycan chain attachment was apparently dependent on G3's complement-binding protein (CBP)-like motif. The modulatory effects of these two molecular domains may contribute to versican's biological activities.

* This work was supported by Medical Research Council of Canada Grant MOP-13730 (to B. B. Y.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger The first two authors contributed equally to this study.

§ On sabbatical from the University of Calgary.

Scholar of the Arthritis Society of Canada. To whom correspondence should be addressed: Research Bldg., Sunnybrook & Women's College Health Sciences Centre, 2075 Bayview Ave., Toronto, Ontario M4N 3M5 Canada. Tel.: 416-480-5874; Fax: 416-480-5737; E-mail: Burton.Yang@swchsc.on.ca.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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