Influence of Constituents of Proteoglycans on Type II Collagen Fibrillogenesis

Abstract

Turbimetry was used to study the influence of glycosaminoglycans of cartilage proteoglycans on type II collagen fibrillogenesis. The monosaccharides, D-glucuronate, N-acetyl-D-galactosamine, N-acetyl-D-glucosamine and D-galactose, all decreased the rate of the fibril formation. D-glucuronate had the strongest effect. The influence of chondroitin sulphate on type II collagen fibrillogenesis depended on the pH of the final solution, the length of the chondroitin sulphate chains and the concentration of chondroitin sulphate. At pH = 7.3 all chondroitin sulphate preparations decreased the rate of fibrillogenesis, while at pH = 6.9 and lower fibrillogenesis was stimulated by chondroitin sulphate (whale/shark), chondroitin 4-sulphate (whale) and chondroitin 6-sulphate (shark). The chain length of these three appeared to be longer than the chain length of chondroitin sulphate (human) and chondroitin sulphate oligosaccharides (whale/shark). At high concentrations (more than 3 mg/ml) fibril formation was less strongly retarded by keratan sulphate (human) than by chondroitin sulphate. At low concentrations a slight stimulation was observed in the presence of keratan sulphate. Glycosaminoglycans did not bind to collagen fibrils. At 0.5 mg/ml chondroitin 4-sulphate had a large solubilizing effect on fibrils compared to chondroitin 6-sulphate. Fibrillogenesis of type II collagen is in many aspects not comparable with fibrillogenesis of type I collagen.