Modulation of collagen gel contraction by decorin.

The small dermatan sulphate protein decorin interacts via its core protein with fibrillar collagens, and its glycosaminoglycan chains were proposed to be capable of self-association. It was therefore of interest to study the role of decorin in the contraction of cell-populated collagen lattices. Stable transfection of dihydrofolate reductase-deficient CHO cells with decorin cDNA resulted in impaired collagen lattice contraction. Using normal human skin fibroblasts in serum-free cultures, inclusion of 0.3 microM decorin in the culture medium also led to a delayed collagen gel contraction. Protein-free dermatan sulphate and the dermatan sulphate-degrading enzyme chondroitin ABC lyase were ineffective. Potential interactions between dermatan sulphate chains were studied by gel filtration. A shift in the elution position of [35S]sulphate-labelled decorin-derived glycosaminoglycans by unlabelled decorin could be observed only when the chains were prepared by trypsin. Chains liberated by beta-elimination or by cathepsin C were eluted at identical positions in the presence or absence of decorin. It is therefore unlikely, that the effect of decorin on collagen-gel retraction is brought about solely by glycosaminoglycan-glycosaminoglycan interactions.