The small dermatan sulphate protein decorin interacts via its core pro
tein with fibrillar collagens, and its glycosaminoglycan chains were p
roposed to be capable of self-association. It was therefore of interes
t to study the role of decorin in the contraction of cell-populated co
llagen lattices. Stable transection of dihydrofolate reductase-deficie
nt CHO cells with decorin cDNA resulted in impaired collagen lattice c
ontraction. Using normal human skin fibroblasts in serum-free cultures
, inclusion of 0.3 mu M decorin in the culture medium also led to a de
layed collagen gel contraction. Protein-free dermatan sulphate and the
dermatan sulphate-degrading enzyme chondroitin ABC lyase were ineffec
tive. Potential interactions between dermatan sulphate chains were stu
died by gel filtration. A shift in the elution position of [S-35]sulph
ate-labelled decorin-derived glycosaminoglycans by unlabelled decorin
could be observed only when the chains were prepared by trypsin. Chain
s liberated by beta-elimination or by cathepsin C were eluted at ident
ical positions in the presence or absence of decorin. It is therefore
unlikely, that the effect of decorin on collagen-gel retraction is bro
ught about solely by glycosaminoglycan-glycosaminoglycan interactions.