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Modulation of collagen gel contraction by decorin
K Bittner1, C Liszio, P Blumberg
1Institute of Physiological Chemistry and Pathobiochemistry, University of Münster, Germany.
The Biochemical Journal
|February 15, 1996
Summary
Decorin protein binding to collagen impairs cell-driven collagen lattice contraction. This effect is not solely due to decorin
Area of Science:
- Biochemistry
- Cell Biology
- Biomaterials Science
Background:
- Decorin, a small leucine-rich proteoglycan, binds to fibrillar collagens via its core protein.
- Decorin's glycosaminoglycan chains have been suggested to self-associate.
- The role of decorin in modulating collagen matrix dynamics is not fully understood.
Purpose of the Study:
- To investigate the role of decorin in the contraction of cell-populated collagen lattices.
- To determine if decorin's glycosaminoglycan chains mediate its effects on collagen gel contraction.
- To elucidate the mechanism by which decorin influences collagen matrix remodeling.
Main Methods:
- Stable transfection of CHO cells with decorin cDNA.
- Assessment of collagen lattice contraction in cell cultures.
- Analysis of decorin-derived glycosaminoglycan interactions using gel filtration.
Main Results:
- Decorin expression in CHO cells significantly impaired collagen lattice contraction.
- Addition of decorin to human skin fibroblast cultures delayed collagen gel contraction.
- Protein-free dermatan sulfate and chondroitin ABC lyase did not affect contraction.
- Glycosaminoglycan-glycosaminoglycan interactions were unlikely to solely mediate decorin's effect.
Conclusions:
- Decorin significantly inhibits cell-mediated collagen gel contraction.
- The inhibitory effect of decorin is likely mediated by its core protein interaction with collagen, not solely by glycosaminoglycan self-association.
- Decorin plays a crucial role in regulating collagen matrix remodeling.