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Mecanismo de acción de miotoxinas aisladas de venenos de serpientes
(1984)
Biochemically and pharmacologically, myotoxins isolated from snake venoms can be placed in four main groups: myolaxic phospholipases A, low molecular weight basic toxins, cardiotoxins, and hemorrhagic myotoxins. The myotoxic ...
Cytotoxicity induced in myotubes by a Lys49 phospholipase A2 homologue from the venom of the snake Bothrops asper: Evidence of rapid plasma membrane damage and a dual role for extracellular calcium
(2007-12)
Acute muscle tissue damage, myonecrosis, is a typical consequence of envenomations by snakes of the family Viperidae. Catalytically-inactive Lys49 phospholipase A2 homologues are abundant myotoxic components in viperid ...
A cellular deficiency of gangliosides causes hypersensitivity to Clostridium perfringens phospholipase C
(2005-07-22)
Clostridium perfringens phospholipase C (Cp-PLC), also called alpha-toxin, is the major virulence factor in the pathogenesis of gas gangrene. Previously, a cellular UDP-Glc deficiency was related with a hypersensitivity ...
Effect of calcineurin inhibitors on myotoxic activity of crotoxin and Bothrops asper phospholipase A2 myotoxins in vivo and in vitro
(2006-07)
Previous studies have shown that calcineurin activity plays a critical role in the myotoxic activity induced by crotoxin (CTX), a group II phospholipase A2 (PLA2) with neurotoxic and myotoxic actions. In order to address ...
Muscle phospholipid hydrolysis by Bothrops asper Asp49 and Lys49 phospholipase A2 myotoxins – distinct mechanisms of action
(2013-07-12)
Bothrops snakes are the major cause of ophidian envenomings in Latin America. Their venom contains myotoxins that cause prominent muscle damage, which may lead to permanent disability. These toxins include myotoxins Mt-I ...
A Lys49-PLA2 myotoxin of Bothrops asper triggers a rapid death of macrophages that involves autocrine purinergic receptor signaling
(Cell Death and Disease (2012) 3, e343, 2012-07-05)
Lys49-PLA2 myotoxins, an important component of various viperid snake venoms, are a class of PLA2-homolog proteins deprived of catalytic activity. Similar to enzymatically active PLA2 (Asp49) and to other classes of ...
Functional analysis of DM64, an antimyotoxic protein with immunoglobulin-like structure from Didelphis marsupialis serum
(2002-12-11)
Bothrops snake venoms are known to induce local tissue damage such as hemorrhage and myonecrosis. The opossum Didelphis marsupialis is resistant to these snake venoms and has natural venom inhibitors in its plasma. The aim ...
Poor regenerative outcome after skeletal muscle necrosis induced by Bothrops asper venom: alterations in microvasculature and nerves
(PLoS ONE 6(5): e19834, 2011-05-24)
Background: Viperid snakebite envenoming is characterized by prominent local tissue damage, including muscle necrosis. A frequent outcome of such local pathology is deficient skeletal muscle regeneration, which causes ...
High-Resolution Crystal Structure of the Snake Venom Metalloproteinase BaP1 Complexed with a Peptidomimetic: Insight into Inhibitor Binding
(2009-07-07)
BaP1, a zinc-dependent endopeptidase belonging to the P-I class of snake venom metalloproteinases, exerts multiple tissue-damaging activities, leading to hemorrhage, myonecrosis, dermonecrosis, blistering, and edema. ...
Mionecrosis, hemorragia y edema inducidos por el veneno de Bothrops asper en ratón blanco
(1980)
Pathogenesis of the myonecrotic, hemorrhagic and edema-forming effects in white mice inoculated with Bothrops asper venom was studied at different time intervals by means of light microscopy, determination of serum levels ...