Biological Activities of Snake Venom Metalloproteinases on Platelets, Neutrophils, Endothelial Cells, and Extracellular Matrices
Snake venom metalloproteinases (SVMPs) may be classified into P-I~P-IV SVMP. P-I and P-III groups are abundant in viper venoms, and preserve proteolytic activity. These zinc-dependent SVMPs have profound effects on cellular receptors, plasma proteins and extracellular matrices, and thus affecting haemostasis. In this review, we focus on their interaction with platelet glycoprotein (GP) Ib, GP VI, integrin α2β1, neutrophil PSGL-1, endothelial adherens junction, plasma vWF, fibrinogen and other extracellular matrix, e.g. collagen, in causing antiplatelet, antiinflammation, and endothelial apoptosis. In addition, the in vivo antithrombotic and hemorrhagic activities of these SVMPs are also explored. Through these structure-activity relationship studies using SVMPs as tools for elucidating the ligand-receptor interaction, we may devise useful antidotes for thrombosis, inflammation and human victims of snake envenoming.
KeywordsSnake Venom Protease Domain Coagulation Factor VIII Venom Component Metalloproteinase Domain
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