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Binding of von Willebrand factor to the small proteoglycan decorin
Author(s) -
Guidetti Gianni F.,
Bartolini Barbara,
Bernardi Bruno,
Tira Maria E.,
Berndt Michael C.,
Balduini Cesare,
Torti Mauro
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.08.011
Subject(s) - decorin , proteoglycan , iduronic acid , chemistry , fibronectin , extracellular matrix , von willebrand factor , biochemistry , dermatan sulfate , glycosaminoglycan , chondroitin sulfate , chondroitin sulfate proteoglycan , biglycan , microbiology and biotechnology , heparan sulfate , immunology , biology , platelet
The small proteoglycan decorin plays an important role in the organisation of the extracellular matrix by binding to several components, including collagen and fibronectin. In this work, we report the dose‐dependent and saturable interaction of decorin with the adhesive glycoprotein, von Willebrand factor (VWF). This interaction was mediated by the glycosaminoglycan side chain of decorin and was critically regulated by the degree of sulfation, but not by the amount of iduronic acid. Both chondroitin sulfate and dermatan sulfate, in addition to heparin, were found to bind VWF equally well. Although soluble decorin prevented VWF binding to heparin, purified VWF‐A1 domain failed to interact with the proteoglycan. These results identify VWF as a new partner for the small proteoglycan, decorin, in the structural organisation of the extracellular matrix.