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The Phospholipase A2 Homologues of Snake Venoms: Biological Activities and Their Possible Adaptive Roles
(2009)
A particular subgroup of toxins with phospholipase A2 (PLA2) structure, but devoid of this enzymatic activity, is commonly found in the venoms of snakes of the family Viperidae, and known as the PLA2 homologues. Among ...
Skeletal muscle necrosis and regeneration after injection of Thalassophryne nattereri (niquim) fish venom in mice
(2001-02)
Stings by Thalassophryne nattereri are responsible for envenomation of fishermen in north-eastern Brazil. Its venom induces prominent local tissue damage, characterized by pain, oedema and necrosis. The pathogenesis of ...
Ability of fucoidan to prevent muscle necrosis induced by snake venom myotoxins: comparison of high- and low-molecular weight fractions
(2008)
Fucoidan, a natural polysaccharide extracted from brown seaweed, inhibits the myotoxic phospholipases A2 present in
the venoms of crotalid snakes. This study evaluated the influence of molecular weight on the ability of ...
Phospholipase A2 enhances the endothelial cell detachment effect of a snake venom metalloproteinase in the absence of catalysis
(2015-10-05)
Microvessel disruption leading to hemorrhage stands among the most dangerous consequences of envenomings by snakes of the family Viperidae. A PIII metalloproteinase (SVMP), balteragin, purified from the venom of the snake ...
Hemostatic effects induced by Thalassophryne nattereri fish venom: a model of endothelium-mediated blood flow impairment.
(2002-08)
Accidents by Thalassophryne nattereri fish venom are characterised by severe local symptoms and signs including pain of fast onset, oedema and necrosis with impaired muscle regeneration. These effects have been related to ...
The C-terminal region of a Lys49 myotoxin mediates Ca2þ influx in C2C12 myotubes
(2010-02)
Myotoxins are abundant components of snake venoms, being a significant public health problem worldwide. Among them, Lys49 phospholipase A2 homologue myotoxins cause extensive necrosis in skeletal muscle tissue. Their ...
Isolation and characterization of a myotoxic phospholipase A2 from the venom of the arboreal snake Bothriechis (Bothrops) schlegelii from Costa Rica
(1997-03)
A new myotoxic phospholipase A2was isolated from the venom of the arboreal snakeBothriechis schlegelii(formerlyBothrops schlegelii) from Costa Rica, by ion-exchange chromatography on CM-Sephadex.B. schlegeliimyotoxin I is ...
Preclinical assessment of a polyspecific antivenom against the venoms of Cerrophidion sasai, Porthidium nasutum and Porthidium ophryomegas: Insights from combined antivenomics and neutralization assays
(2013-03-15)
A polyspecific antivenom is used in Central America for the treatment of envenomings by viperid snakes. This antivenom is generated in horses hyperimmunized with a mixture of venoms from Bothrops asper, Crotalus simus and ...
Tyr→Trp-substituted peptide 115-129 of a Lys49 phospholipase A2 expresses enhanced membrane-damaging activities and reproduces its in vivo myotoxic effect
(1999)
Myotoxin II is a group II Lys49 phospholipase A2 (PLA2) isolated from the venom of the snake Bothrops asper. Previous
studies on a synthetic peptide derived from its heparin-binding, cationic/hydrophobic sequence 115^129 ...
Identification of the myotoxic site of the Lys49 phospholipase A2 from Agkistrodon piscivorus piscivorus snake venom: synthetic C-terminal peptides from Lys49, but not from Asp49 myotoxins, exert membrane-damaging activities
(2001)
Group II phospholipase A2 (PLA2) myotoxins found in the venoms of Crotalidae snakes can be divided into `Asp49' and
`Lys49' isoforms, the latter being considered catalytically-inactive variants. Previous studies on one ...