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Structure and Function of Snake Venom Metalloproteinase Family
Structure and Function of Snake Venom Metalloproteinase FamilyABBREVIATIONS PREFACE PART I:The High Molecular Mass Hemorrhagic Protein, HR1B, Isolated from the Venom of Trimeresurus flavoviridis PART II:Coagulation Factor X Activating Enzyme from Russell's Viper Venom (RVV-X):A NOVEL METALLOPROTEINASE WITH DISINTEGRIN(PLATELET AGGREGATIONINHIBITOR)-LIKE AND C-TYPE LECTIN- LIKE DOMAIN CONCLUSION ...
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Snake venom metalloproteinases:Their role in the pathogenesis of local tissue damage
Biochimie, 2000 The biochemical characteristics of hemorrhagic metalloproteinases isolated from snake venoms are reviewed, together with their role in the pathogenesis of the local tissue damage characteristic of crotaline and viperine snake envenomations.
José María Gutiérrez +2 more
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Platelets as targets of snake venom metalloproteinases
Toxicon, 2005For centuries snake venoms have been known to interfere with haemostasis and this is now known basically due either to toxins activating/inhibiting clotting factors, having effects on blood vessels or interfering with platelet function. In this short review, the interaction of one major group of toxins, the snake venom metalloproteinases, with ...
Aura S Kamiguti
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Snake venom metalloproteinases
Toxicon, 2013Recent proteomic analyses of snake venoms show that metalloproteinases represent major components in most of the Crotalid and Viperid venoms. In this chapter we discuss the multiple activities of the SVMPs. In addition to hemorrhagic activity, members of the SVMP family also have fibrin(ogen)olytic activity, act as prothrombin activators, activate ...
Francis S Markland
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Unraveling the Processing and Activation of Snake Venom Metalloproteinases
Journal of Proteome Research, 2014Snake venom metalloproteinases (SVMPs) are zinc-dependent enzymes responsible for most symptoms of human envenoming. Like matrix metalloproteinases (MMPs) and a disintegrin and metalloproteinase (ADAM) proteins, SVMPs are synthesized as zymogens, and enzyme activation is regulated by hydrolysis of their prodomain, but the processing of SVMPs is still ...
Fabio Nogueira +2 more
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Angiostatin-like molecules are generated by snake venom metalloproteinases
Biochemical and Biophysical Research Communications, 2002Angiostatin is a plasminogen-derived anti-angiogenic factor composed of its first four kringle structures. This molecule is generated by proteolytic cleavage of plasminogen by some proteolytic enzymes in vitro. Since venoms of viper snakes are a rich source of both serine- and metalloproteinase, we hypothesized that angiostatin-like polypeptides could ...
Solange M T Serrano +2 more
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Hemorrhage Caused by Snake Venom Metalloproteinases: A Journey of Discovery and Understanding † [PDF]
Toxins, 2016 The historical development of discoveries and conceptual frames for understanding the hemorrhagic activity induced by viperid snake venoms and by hemorrhagic metalloproteinases (SVMPs) present in these venoms is reviewed. Histological and ultrastructural tools allowed the identification of the capillary network as the main site of action of SVMPs ...
José María Gutiérrez +2 more
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Hemorrhagic metalloproteinases from snake venoms
Pharmacology & Therapeutics, 1994One of the more significant consequences of crotalid envenomation is hemorrhage. Over the past 50 years of investigation, it is clear that the primary factors responsible for hemorrhage are metalloproteinases present in the venom of these snakes.
J B, Bjarnason, J W, Fox
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Natural inhibitors of snake venom hemorrhagic metalloproteinases
Toxicon, 2005Metalloproteinases play an important role in the poisoning process by snake venoms. They evoke systemic injury, by degrading or activating host blood factors, and local damage by acting on endothelial cell surface proteins. Plasma and/or muscle of venomous and non-venomous snakes as well as of some special mammals possess metalloproteinase inhibitors ...
Jonas, Perales +3 more
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Comparative Biochemistry and Physiology Part - C: Toxicology and Pharmacology, 2004 Metalloproteinases (MPs) are Zn+-dependent endoproteolytic enzymes, abundant in crotalid and viperid snake venoms. Most snake venom metalloproteinases (svMPs) are active on extracellular matrix components and this effect is thought to result in bleeding ...
Heloisa S Selistre-de-Araujo +2 more
exaly +2 more sources