Results 181 to 190 of about 51,201 (249)

Natural inhibitors of snake venom metalloproteinases

open access: yesNatural inhibitors of snake venom metalloproteinases
openaire  

Role of inflammation in the pulmonary hemorrhage induced by a snake venom metalloproteinase

Journal of Immunology, 2022
Snakebite envenoming (a neglected tropical disease that affects millions of people worldwide every year) is characterized by a complex pathophysiology.
A. C. Castro   +3 more
semanticscholar   +1 more source

Jararhagin, a snake venom metalloproteinase, induces mechanical hyperalgesia in mice with the neuroinflammatory contribution of spinal cord microglia and astrocytes.

International Journal of Biological Macromolecules, 2021
Jararhagin is a hyperalgesic metalloproteinase from Bothrops jararaca venom. In rodents, jararhagin induces nociceptive behaviors that correlate with an increase in peripheral cytokine levels.
C. R. Ferraz   +11 more
semanticscholar   +1 more source

Expression and bioinformatic analysis of snake venom metalloproteinase (svmp) from Naja nigricollis snake venom gland

Bayero Journal of Pure and Applied Sciences, 2021
Elapid snake venom is highly valuable and also a source of medically important peptides. The venom of Naja nigricollis is unique among elapids in that it contains mainly cytotoxins, but also with other components.
B. Kurfi, N.I. Liman, Y. Yusuf
semanticscholar   +1 more source

Apoptosis induced by a snake venom metalloproteinase from Bothrops alternatus venom in C2C12 muscle cells

open access: yesApoptosis, 2017
In this study, the apoptosis inducing effects of baltergin as well as its influence on cell adhesion and migration on muscles cells in vitro were studied. Morphological analysis made by scanning electron and phase contrast microscopy demonstrated typical futures of programmed cell death, apoptosis. This mechanism was confirmed by fluorescence staining,
S. Bustillo   +4 more
semanticscholar   +6 more sources

Snake venom metalloproteinases

Toxicon, 2013
Recent 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, Stephen, Swenson
openaire   +2 more sources

Natural Inhibitors of Snake Venom Metalloproteinases

Australian Journal of Chemistry, 2020
Snakebites 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. Snake venom metalloproteinases (SVMPs) are responsible for severe haemorrhage, the inhibition of
Narumi Aoki-Shioi   +2 more
openaire   +1 more source

Hemorrhagic metalloproteinases from snake venoms

Pharmacology & Therapeutics, 1994
One 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
openaire   +2 more sources

Natural inhibitors of snake venom hemorrhagic metalloproteinases

Toxicon, 2005
Metalloproteinases 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
openaire   +2 more sources

Molecular characterisation of endogenous snake venom metalloproteinase inhibitors

Biochemical and Biophysical Research Communications, 2008
Viper 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 ...
Simon C, Wagstaff   +7 more
openaire   +2 more sources

Home - About - Disclaimer - Privacy