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Cryptic self-association sites in type III modules of fibronectin
1American Red Cross Holland Laboratory, Rockville, Maryland 20855, USA.
The Journal of Biological Chemistry
|January 17, 1997
Summary
Fibronectin domain III1 has two cryptic self-association sites. One site binds Fn fragments as a peptide, while another site, exposed in isolated domains, recognizes other fibronectin type III domains, crucial for extracellular matrix assembly.
Area of Science:
- Biochemistry
- Molecular Biology
- Extracellular Matrix Research
Background:
- Fibronectin (Fn) domain III1 possesses a cryptic site involved in Fn fibril formation.
- Previous studies indicated a synthetic peptide from domain III1 binds Fn, but the interaction site remained unknown.
Purpose of the Study:
- To investigate interactions between fibronectin domains, particularly focusing on domain III1.
- To identify the specific domains and conditions involved in fibronectin self-association.
Main Methods:
- Affinity chromatography using peptide-agarose and Sepharose matrices.
- Testing interactions of plasma fibronectin fragments with immobilized domains before and after denaturation.
- Analysis of subfragments to pinpoint interacting domains.
Main Results:
- Domain III1 contains two cryptic self-association sites.
- One site recognizes Fn fragments when presented as a peptide.
- Another site, exposed in isolated domains, interacts with denatured domains III7 and III15 within other Fn fragments.
Conclusions:
- Fibronectin domain III1 exhibits dual cryptic self-association capabilities.
- These interactions between type III domains are important for fibronectin multimer assembly in the extracellular matrix.