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Biglycan and decorin bind close to the n-terminal region of the collagen VI triple helix

Wiberg, Charlotte; Hedbom, Erik; Khairullina, Alfia; Lamande, Shireen R.; Oldberg, Åke LU ; Timpl, Rupert; Mörgelin, Matthias LU and Heinegård, Dick LU (2001) In Journal of Biological Chemistry 276(22). p.18947-18952
Abstract
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 BIAcore(TM)2000 system. Both proteoglycans exhibited a strong affinity for collagen VI with dissociation constants (K(D)) of approximately 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... (More)
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 BIAcore(TM)2000 system. Both proteoglycans exhibited a strong affinity for collagen VI with dissociation constants (K(D)) of approximately 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 alpha2(VI) chain probably plays a role in the interaction. (Less)
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author
organization
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type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
276
issue
22
pages
18947 - 18952
publisher
ASBMB
external identifiers
  • pmid:11259413
  • scopus:0035378666
ISSN
1083-351X
DOI
language
English
LU publication?
yes
id
d139342f-ea3a-41d2-a34e-61b2acea9031 (old id 1120393)
date added to LUP
2008-07-18 14:20:46
date last changed
2018-05-29 11:38:18
@article{d139342f-ea3a-41d2-a34e-61b2acea9031,
  abstract     = {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 BIAcore(TM)2000 system. Both proteoglycans exhibited a strong affinity for collagen VI with dissociation constants (K(D)) of approximately 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 alpha2(VI) chain probably plays a role in the interaction.},
  author       = {Wiberg, Charlotte and Hedbom, Erik and Khairullina, Alfia and Lamande, Shireen R. and Oldberg, Åke and Timpl, Rupert and Mörgelin, Matthias and Heinegård, Dick},
  issn         = {1083-351X},
  language     = {eng},
  number       = {22},
  pages        = {18947--18952},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Biglycan and decorin bind close to the n-terminal region of the collagen VI triple helix},
  url          = {http://dx.doi.org/},
  volume       = {276},
  year         = {2001},
}