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Complexation of fibronectin with tissue transglutaminase
1Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208.
Biochemistry
|January 24, 1989
Summary
This study shows that erythrocyte transglutaminase binds to fibronectin in a 2:1 ratio. This non-covalent interaction involves fibronectin
Area of Science:
- Biochemistry
- Cell Biology
- Protein Interactions
Background:
- Previous research suggested fibronectin acts as a carrier for transglutaminases released from cells into plasma.
- Understanding these interactions is crucial for cellular and extracellular protein dynamics.
Purpose of the Study:
- To investigate the specific association between purified human erythrocyte transglutaminase and human plasma fibronectin.
- To characterize the stoichiometry, nature, and binding domains involved in this complex formation.
Main Methods:
- Nondenaturing electrophoresis with activity staining and immunoblotting.
- High-Performance Liquid Chromatography (HPLC) gel filtration.
- Limited proteolysis of fibronectin followed by binding assays.
Main Results:
- Complexation of erythrocyte transglutaminase (80K) with plasma fibronectin (440K) was confirmed with a 2:1 stoichiometry.
- The binding is non-covalent and does not involve protein cross-linking.
- Fibronectin's gelatin-binding fragments (56K and 46K) also bind transglutaminase, indicating specific interaction domains.
Conclusions:
- Erythrocyte transglutaminase forms a stable, non-covalent complex with plasma fibronectin.
- The interaction is independent of Ca2+, suggesting a non-catalytic site involvement on transglutaminase.
- Specific domains within fibronectin, including gelatin-binding regions, mediate this association.
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