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Complexation with heparin prevents adhesion between fibrin-coated surfaces
G S Retzinger1, L J Chandler, B C Cook
1Department of Pathology, Medical College of Wisconsin, Milwaukee 53226.
The Journal of Biological Chemistry
|December 5, 1992
Summary
Heparin binds strongly to fibrinogen and fibrin, preventing bead aggregation. This interaction suggests heparin
Area of Science:
- Biochemistry
- Biomaterials Science
- Hematology
Background:
- Heparin is a crucial anticoagulant.
- Fibrinogen and fibrin play key roles in blood clotting and adhesion.
- Understanding molecular interactions is vital for developing diagnostic tools.
Purpose of the Study:
- To investigate the binding of heparin to fibrinogen and fibrin.
- To elucidate the mechanism by which heparin affects fibrin aggregation.
- To explore the application of these interactions in analytical methods for heparin quantitation.
Main Methods:
- Heparin binding to fibrinogen and fibrin adsorbed onto polystyrene-divinylbenzene beads was studied.
- The effect of heparin-fibrin(ogen) complex formation on bead aggregation was analyzed.
- Mechanisms including desorption, thrombin inhibition, and electrostatic repulsion were ruled out.
Main Results:
- Heparin binds with high affinity (Kd ~100 nM) to adsorbed fibrinogen and fibrin.
- Heparin binding inhibits the aggregation of fibrin-coated beads and dissociates preformed aggregates.
- The observed effects are attributed to direct interference with fibrin dimer formation.
Conclusions:
- Heparin directly interferes with fibrin dimer formation, inhibiting aggregation.
- These findings support the development of novel analytical methods for heparin quantitation.
- Endogenous heparin may play a physiological role in regulating fibrin-mediated adhesion.