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Snake venom proteases affecting hemostasis and thrombosis
T Matsui1, Y Fujimura, K Titani
1Division of Biomedical Polymer Science, Institute for Comprehensive Medical Science, Fujita Health University, Toyoake, Aichi, Japan.
Biochimica Et Biophysica Acta
|March 10, 2000
Summary
Snake venom proteases, including serine proteases and metalloproteinases, significantly impact hemostasis and thrombosis. Their unique activities offer potential for novel medical applications in treating bleeding and clotting disorders.
Area of Science:
- Biochemistry
- Pharmacology
- Toxicology
Background:
- Snake venom proteases are diverse enzymes affecting hemostasis and thrombosis.
- Over 150 proteases identified, with about one-third structurally characterized.
- Classified into serine proteases and metalloproteinases, they exhibit varied functions.
Purpose of the Study:
- To review the structure and function of snake venom proteases.
- To focus on their effects on hemostasis and thrombosis.
- To compare snake venom proteases with mammalian counterparts.
Main Methods:
- Literature review of snake venom protease research.
- Classification of proteases into serine proteases and metalloproteinases.
- Analysis of enzymatic activities and substrate specificities.
Main Results:
- Serine proteases exhibit fibrin(ogen)olytic, kininogenase, and factor-activating activities.
- Metalloproteinases display fibrin(ogen)olytic, hemorrhagic, and unique substrate specificities.
- Chimeric metalloproteinases possess domains like disintegrin-like, facilitating platelet interaction.
Conclusions:
- Snake venom proteases possess unique mechanisms influencing hemostasis and thrombosis.
- Their distinct enzymatic properties and substrate specificities warrant further investigation.
- Potential therapeutic applications in thrombosis and hemostasis are significant.
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