Portal de Periódicos da CAPES

Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon

1984; Portland Press; Volume: 223; Issue: 3 Linguagem: Inglês

10.1042/bj2230587

1470-8728

Kathryn G. Vogel, Mats Paulsson, Dick Heinegård,

Protease and Inhibitor Mechanisms

The small dermatan sulphate proteoglycan of bovine tendon demonstrated a unique ability to inhibit fibrillogenesis of both type I and type II collagen from bovine tendon and cartilage respectively in an assay performed in vitro. None of the other proteoglycan populations from cartilage, tendon or aorta, even those similar in size and chemical structure, had this effect. Alkali treatment of the small proteoglycan of tendon eliminated its ability to inhibit fibrillogenesis, whereas chondroitinase digestion did not. This indicates that its interaction with collagen depends on the core protein. Fibrillogenesis of pepsin-digested collagens was affected similarly, indicating that interaction with the collagen telopeptides is not involved. The results suggest that interactions between collagen and proteoglycans may be quite specific both for the type of proteoglycan and its tissue of origin.