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J. Biol. Chem., Vol. 277, Issue 51, 49120-49126, December 20, 2002
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From the The ability of the leucine-rich repeat (LRR)
proteins biglycan, decorin, and chondroadherin to interact with
collagen VI and influence its assembly to supramolecular structures was
studied by electron microscopy and surface plasmon resonance
measurements in the BIAcore 2000 system. Biglycan showed a unique
ability to organize collagen VI into extensive hexagonal-like networks
over a time period of only a few minutes. Only the intact molecule, substituted with two dermatan sulfate chains, had this capacity. Intact
decorin, with one dermatan sulfate chain only, was considerably less
efficient, and aggregates of organized collagen VI were found only
after several hours. Chondroadherin without glycosaminoglycan substitutions did not induce any ordered collagen VI organization. However, all three related LRR proteins were shown to interact with
collagen VI using electron microscopy and surface plasmon resonance.
Biglycan and decorin were exclusively found close to the N-terminal
parts of the collagen VI tetramers, whereas chondroadherin was
shown to bind close to both the N- and C-terminal parts of collagen VI.
In the formed hexagonal networks, biglycan was localized to the
intra-network junctions of the collagen VI filaments. This was
demonstrated by electron microscopy after negative staining of
gold-labeled biglycan in aggregation experiments with collagen VI.
Biglycan Organizes Collagen VI into Hexagonal-like Networks
Resembling Tissue Structures*
,,,¶
Department of Cell and Molecular Biology,
University of Lund, BMC, S-221 84 Lund, Sweden and the
§ Max-Planck-Institut für Biochemie, D-82152
Martinsried, Germany
*
This work was supported by the Swedish Medical Research
Council, Greta and Johan Kock's Foundation, the Swedish Rheumatism Association, Alfred Österlund's Foundation, Konung Gustaf V's 80-årsfond, 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.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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