Binding of von Willebrand factor to the small proteoglycan decorin.
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.
Guidetti
Gianni F
GF
Department of Biochemistry, Center of Excellence for Applied Biology, University of Pavia, Pavia, Italy.
Bartolini
Barbara
B
Bernardi
Bruno
B
Tira
Maria E
ME
Berndt
Michael C
MC
Balduini
Cesare
C
Torti
Mauro
M
D058575:Decorin; D016326:Extracellular Matrix Proteins; D011485:Protein Binding; D011509:Proteoglycans / Q000737:chemistry / Q000378:metabolism*; D014841:von Willebrand Factor / Q000378:metabolism*
D058575:Decorin; D016326:Extracellular Matrix Proteins; D011509:Proteoglycans; D014841:von Willebrand Factor