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Interactions between thrombospondin and the small proteoglycan decorin: interference with cell attachment.
M Winnemöller1, P Schön, P Vischer
1Institut für Physiologische Chemie und Pathobiochemie, Universität Münster, Deutschland.
European Journal of Cell Biology
|October 1, 1992
Summary
Decorin, a proteoglycan, binds strongly to thrombospondin. This interaction, mediated by decorin's polysaccharide chain, inhibits fibroblast cell attachment and spreading on thrombospondin substrates, highlighting decorin's antiadhesive properties.
Area of Science:
- Biochemistry
- Cell Biology
- Extracellular Matrix Biology
Background:
- Decorin is a small interstitial proteoglycan found in the extracellular matrix.
- It interacts with matrix components like collagen and fibronectin.
- Thrombospondin is another extracellular matrix protein involved in cell adhesion.
Purpose of the Study:
- To investigate the binding interaction between decorin and thrombospondin.
- To determine the role of decorin's structural components in this interaction.
- To assess the functional consequences of this interaction on human skin fibroblast adhesion and spreading.
Main Methods:
- Solid-phase binding assays were used to quantify decorin-thrombospondin interactions.
- Binding studies utilized intact decorin, its glycosaminoglycan-free core protein, and thrombospondin fragments.
- Fibroblast adhesion and spreading assays were performed on thrombospondin substrates with and without decorin.
Main Results:
- Both intact decorin and its core protein showed high-affinity binding to thrombospondin (KD ~5 nM and ~2 nM, respectively).
- The decorin polysaccharide chain was essential for binding to Sepharose-bound thrombospondin.
- Decorin and its core protein significantly delayed human skin fibroblast attachment and reduced attachment strength on thrombospondin substrates.
Conclusions:
- Decorin and thrombospondin interact with high affinity, involving specific structural features of both molecules.
- The decorin polysaccharide chain plays a crucial role in mediating this interaction.
- Decorin exhibits an antiadhesive function, inhibiting fibroblast attachment and spreading on thrombospondin, irrespective of cell spreading support.