Introduction. Collagen is used as a coating on titanium implants and as a scaffold material in bone tissue engineering. Proteoglycans (PGs), consisting of a protein core connected to glycosaminoglycan chains, may be bound to collagen fibrils. PGs can affect osteoblast behaviour and also bind and influence the effect of growth factors such as TGF-β1, which stimulates extra-cellular matrix production. The aim of this work is to characterise fibrils of the collagen types I, II and III with regard to amount of decorin and biglycan bound and to study the reaction of primary rat (RO) and human (HO) osteoblasts to titanium surfaces coated with fibrils containing decorin and biglycan. The influence of PGs on the effect of TGF-β1 on osteoblasts was also examined. Adhesion, proliferation and collagen synthesis were investigated. Methods Fibrils of collagen types I, II and III containing decorin and biglycan were formed at 37ºC in a 30 mM phosphate buffer at pH 7.4 at different PG:collagen ratios. PG content of fibrils was determined colormetrically. Fibril morphology was studied by atomic force microscpoy (AFM). Results and Discussion. Decorin caused a reduction in fibril diameter, but biglycan did not. Collagen type II fibrils bound more PGs than type I and III fibrils, with more biglycan than decorin bound by all collagen types. Biglycan promoted the formation of focal adhesions, and also stimulated HO proliferation, as did decorin but not as strongly. Biglycan but not decorin inhibited RO collagen synthesis. TGF-β1 reduced the proliferation and enhanced the collagen synthesis of HOs. However the decrease in proliferation was lower and the increase in collagen synthesis was higher when decorin was present instead of biglycan. Conclusions. The ability of collagen fibrils to bind PGs varies according to PG and collagen type. Biglycan and decorin influence primary osteoblast behaviour by themselves, but also influence the effect of TGF-β1.

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