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Biglycan organizes collagen VI into hexagonal-like networks resembling tissue structures.

Wiberg, Charlotte; Heinegård, Dick LU ; Wenglén, Christina LU ; Timpl, Rupert and Mörgelin, Matthias LU (2002) In Journal of Biological Chemistry 277(51). p.49120-49126
Abstract
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... (More)
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 while 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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
277
issue
51
pages
49120 - 49126
publisher
ASBMB
external identifiers
  • wos:000180028900005
  • scopus:0345894336
ISSN
1083-351X
DOI
10.1074/jbc.M206891200
language
English
LU publication?
yes
id
6b8e8868-1afd-41d6-808d-4fc5532ec3af (old id 110853)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12354766&dopt=Abstract
date added to LUP
2007-07-20 08:54:26
date last changed
2017-07-23 03:46:23
@article{6b8e8868-1afd-41d6-808d-4fc5532ec3af,
  abstract     = {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 while 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.},
  author       = {Wiberg, Charlotte and Heinegård, Dick and Wenglén, Christina and Timpl, Rupert and Mörgelin, Matthias},
  issn         = {1083-351X},
  language     = {eng},
  number       = {51},
  pages        = {49120--49126},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Biglycan organizes collagen VI into hexagonal-like networks resembling tissue structures.},
  url          = {http://dx.doi.org/10.1074/jbc.M206891200},
  volume       = {277},
  year         = {2002},
}