Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 276, Issue 22, Pages 18947-18952Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M100625200
Keywords
-
Categories
Ask authors/readers for more resources
The binding of native biglycan and decorin to pepsin-extracted collagen VT 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 similar to 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 VT 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available