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Plasminogen activator inhibitors--a review.
1Department of Medicine, University Hospital, Lausanne, Switzerland.
Enzyme
|January 1, 1988
Summary
Plasminogen activator inhibitors (PAIs) regulate plasminogen activator (PA) activity. This review details the physicochemical properties and primary structures of PAI-1, PAI-2, protease nexin, and PAI-3, comparing them within the serpin protein family.
Area of Science:
- Biochemistry
- Molecular Biology
- Protein Science
Background:
- Plasminogen activators (PAs) are enzymes crucial for fibrinolysis.
- Plasminogen activator inhibitors (PAIs) are key regulators of PA activity.
- Several PAI proteins, belonging to the serpin superfamily, are known to inhibit PAs.
Purpose of the Study:
- To provide an overview of the physicochemical characteristics of major PAIs.
- To compare the primary structures of PAI-1, PAI-2, protease nexin, and PAI-3.
- To contextualize these inhibitors within the broader serpin protein family.
Main Methods:
- Literature review focusing on physicochemical properties.
- Comparative analysis of primary protein structures.
- Examination of reaction rate constants for inhibition.
Main Results:
- PAIs exhibit distinct physicochemical properties.
- The primary structures of PAI-1, PAI-2, protease nexin, and PAI-3 show similarities and differences.
- Inhibitor efficacy varies, with PAI-1 demonstrating the fastest reaction rate.
Conclusions:
- PAIs are diverse serpins with varying inhibitory capacities.
- Understanding PAI structure-function relationships is vital for studying fibrinolysis.
- This review consolidates key information on PAIs for researchers in the field.