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Published on: May 8, 2012
WISP-1 binds to decorin and biglycan
L Desnoyers1, D Arnott, D Pennica
1Department of Protein Chemistry, Genentech Inc., 1 DNA Way, South San Francisco, CA 94080, USA. desnoyer@gene.com
The Journal of Biological Chemistry
|October 13, 2001
Summary
Wnt-1-induced secreted protein 1 (WISP-1) binds to decorin and biglycan, which are dermatan sulfate proteoglycans. These interactions regulate WISP-1
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Wnt-1-induced secreted protein 1 (WISP-1) is a CCN family growth factor.
- CCN family member activity is modulated by interactions with sulfated glycoconjugates.
Purpose of the Study:
- To characterize WISP-1's tissue and cellular interaction specificity.
- To identify WISP-1 binding factors and elucidate its mechanism of action.
Main Methods:
- Solid phase assay to identify binding factors in fibroblast conditioned media.
- Competitive inhibition assays using glycosaminoglycans.
- Treatment with glycosaminoglycan lyases and proteases.
- Mass spectrometric analysis to identify binding proteins.
Main Results:
- WISP-1 binding was specific to colon tumor stroma and fibroblasts.
- Dermatan sulfate proteoglycans mediated WISP-1 binding.
- Decorin and biglycan were identified as WISP-1 binding factors.
- Decorin and biglycan directly interacted with WISP-1 and inhibited its binding.
Conclusions:
- Decorin and biglycan are key WISP-1 binding factors.
- These interactions mediate and modulate WISP-1's interaction with fibroblast surfaces.
- This interaction likely regulates WISP-1 function in biological processes.
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