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Kringle domains and plasmin denaturation
1Biochemistry Department, Medical College, National Cheng-Kung University, Tainan, Taiwan, Republic of China.
Abstract:
The rate of plasmin denaturation was in the order of Lys-plasmin greater than miniplasmin greater than microplasmin. Fibrinogen degradation products (FDP) dose dependently increased the denaturation rate of Lys-plasmin and mini-plasmin with a maximal rate constant at the FDP/plasmin ratio of about 0.5. The denaturation rate constant of microplasmin was not affected. FDP increased the rate of plasmin denaturation was in parallel with its effect on the interaction among kringle domains. Without FDP only trace amounts of plasminogen dimer could be detected by cross-linking with bis-(sulfo-succinimidyl)-suberate followed by SDS gel electrophoresis. In the low concentration of FDP significant amounts of oligomers of Glu-, mini-plasminogens, kringle 1-3 and kringle 1-5 were observed. High concentration of FDP, however, decreased plasminogen oligomer.
Insights
Fibrinogen degradation products (FDP) accelerate plasmin denaturation, particularly affecting Lys-plasmin and mini-plasmin. FDP also influences plasminogen oligomerization, with effects varying by concentration.
Area of Science:
- Biochemistry
- Molecular Biology
- Protein Chemistry
Background:
- Plasmin plays a crucial role in fibrinolysis.
- Understanding plasmin stability and interactions is vital for thrombolytic therapies.
- Fibrinogen degradation products (FDP) are generated during clot breakdown.
Purpose of the Study:
- To investigate the effect of FDP on plasmin denaturation rates.
- To explore the influence of FDP on plasminogen oligomerization and interactions.
Main Methods:
- Assessing plasmin denaturation rates using different plasmin forms (Lys-plasmin, miniplasmin, microplasmin).
- Quantifying FDP-induced changes in denaturation kinetics.
- Analyzing plasminogen oligomer formation using cross-linking and SDS-PAGE.
Main Results:
- Denaturation rates followed the order: Lys-plasmin > miniplasmin > microplasmin.
- FDP dose-dependently increased denaturation rates of Lys-plasmin and mini-plasmin.
- FDP affected plasminogen oligomerization, with low concentrations promoting oligomer formation and high concentrations decreasing it.
- FDP's effect on plasmin denaturation correlated with its impact on kringle domain interactions.
Conclusions:
- FDP significantly modulates plasmin stability and denaturation.
- FDP influences the aggregation state of plasminogen, impacting its interactions.
- These findings provide insights into the complex interplay between fibrinolysis components.