Biglycan and decorin bind close to the n-terminal region of the collagen VI triple helix
Författare
Summary, in English
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.
Avdelning/ar
- Åke Oldberg´s group
- Infektionsmedicin
- Reumatologi och molekylär skelettbiologi
Publiceringsår
2001
Språk
Engelska
Sidor
18947-18952
Publikation/Tidskrift/Serie
Journal of Biological Chemistry
Volym
276
Issue
22
Dokumenttyp
Artikel i tidskrift
Förlag
American Society for Biochemistry and Molecular Biology
Ämne
- Cell and Molecular Biology
Status
Published
Forskningsgrupp
- Åke Oldberg´s group
ISBN/ISSN/Övrigt
- ISSN: 1083-351X