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Originally published In Press as doi:10.1074/jbc.M100625200 on March 19, 2001

J. Biol. Chem., Vol. 276, Issue 22, 18947-18952, June 1, 2001
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Biglycan and Decorin Bind Close to the N-terminal Region of the Collagen VI Triple Helix*

Charlotte WibergDagger , Erik Hedbom§, Alfia KhairullinaDagger , Shireen R. Lamandé, Åke OldbergDagger , Rupert Timpl||, Matthias MörgelinDagger , and Dick HeinegårdDagger **

From the Dagger  Department of Cell and Molecular Biology, University of Lund, BMC Plan C12, Lund S-221 84, Sweden, the § Laboratory for Experimental Cartilage Research, Center for Rheumatology and Bone Disease, Zürich CH-8038, Switzerland, the  Cell and Matrix Biology Research Unit, Department of Pediatrics, University of Melbourne, Royal Childrens Hospital, Parkville VIC 3052, Australia, and the || Max-Planck-Institut für Biochemie, Martinsried D-82152, Germany

The binding of native biglycan and decorin to pepsin-extracted collagen VI from human placenta was examined by solid phase assay and by measurement of surface plasmon resonance in the BIAcoreTM2000 system. Both proteoglycans exhibited a strong affinity for collagen VI with dissociation constants (KD) of ~30 nM. Removal of the glycosaminoglycan chains by chondroitinase ABC digestion did not significantly affect binding. In coprecipitation experiments, biglycan and decorin bound to collagen VI and equally competed with the other, suggesting that biglycan and decorin bind to the same binding site on collagen VI. This was confirmed by electron microscopy after negative staining of complexes between gold-labeled proteoglycans and collagen VI, demonstrating that both biglycan and decorin bound exclusively to a domain close to the interface between the N terminus of the triple helical region and the following globular domain. In solid phase assay using recombinant collagen VI fragments, it was shown that the alpha 2(VI) chain probably plays a role in the interaction.

* This work was supported by the Swedish Medical Research Council, Konung Gustaf V's 80-årsfond, Greta och Johan Kock's stiftelser, Alfred Österlund's Stiftelse, Reumatikerförbundet, and the Medical Faculty, Lund University.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.

** To whom correspondence should be addressed. Tel.: 46-46-222-8570; Fax: 46-46-211-3417; E-mail: dick.heinegard@medkem.lu.se.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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