Results 131 to 140 of about 32,635 (169)
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Natural Inhibitors of Snake Venom Metalloproteinases
Australian Journal of Chemistry, 2020Snakebites are a hazard in the tropical world. Although antivenom therapy is effective, it is beset with inherent drawbacks. A better understanding of the major components of snake venoms and their neutralisation will help in improving snakebite treatment.
Narumi Aoki-Shioi +2 more
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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 ...
José A, Portes-Junior +9 more
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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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Triacontyl p-coumarate: An inhibitor of snake venom metalloproteinases
Phytochemistry, 2013Snake venom metalloproteinases (SVMPs) participate in a number of important biological, physiological and pathophysiological processes and are primarily responsible for the local tissue damage characteristic of viperid snake envenomations. The use of medicinal plant extracts as antidotes against animal venoms is an old practice, especially against ...
Mendes, M. M. +9 more
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Timeline of key events in snake venom metalloproteinase research
Journal of Proteomics, 2009It is reasonable to state that snake venom toxinology has been actively pursued for at least the past 400 to 500 years. Early on it was appreciated that the venoms of the Viperidae produced profound local effects, notably hemorrhage. For the past 100 years, with the advent of modern chemistry and biochemistry significant progress has been gained ...
Jay W, Fox, Solange M T, Serrano
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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 ...
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Molecular characterisation of endogenous snake venom metalloproteinase inhibitors
Biochemical and Biophysical Research Communications, 2008Viper venoms contain one of the most potent mixtures of proteases in natural existence and yet the venom gland and proteins in this mixture are refractory to degradation. Here we demonstrate that the sub-10-kDa components of venom from two African viper species (Echis ocellatus and Cerastes cerastes cerastes) are predominantly composed of the tri ...
Wagstaff, Simon C. +7 more
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On the ancestral recruitment of metalloproteinases into the venom of snakes
Toxicon, 2012Tracing the evolutionary history of proteins can reveal insights into gene alterations responsible for changes in structure and function. Here, the origin of snake venom metalloproteinases was rigorously reassessed using phylogenetics and the reconstruction of ancestral sequences.
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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 ...
Paulo Lee, Ho +8 more
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Insights into the mechanism of haemorrhage caused by snake venom metalloproteinases
Toxicon, 1996Local and systemic haemorrhage are common consequences of crotaline and viperine envenoming. Several studies carried out using purified toxins have indicated that local haemorrhage can be attributed to a distinct class of venom metalloproteinases. Analyses of their cDNAs predict multi-domain enzymes, with an N-terminal metalloproteinase domain, a ...
A S, Kamiguti +3 more
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