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dc.creatorTonello, Fiorellaes_ES
dc.creatorSimonato, M.es_ES
dc.creatorAita, A.es_ES
dc.creatorPizzo, Paolaes_ES
dc.creatorFernández Ulate, Juliánes_ES
dc.creatorLomonte, Brunoes_ES
dc.creatorGutiérrez, José Maríaes_ES
dc.creatorMontecucco, Cesarees_ES
dc.date.accessioned2012-08-17T19:53:43Zes_ES
dc.date.available2012-08-17T19:53:43Zes_ES
dc.date.issued2012-07-05es_ES
dc.identifier.citationhttp://www.nature.com/cddis/journal/v3/n7/full/cddis201268a.htmles_ES
dc.identifier.citationhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3406575/pdf/cddis201268a.pdf
dc.identifier.urihttp://hdl.handle.net/10669/688es_ES
dc.descriptionCell Death and Disease (2012) 3, e343; doi:10.1038/cddis.2012.68es_ES
dc.description.abstractLys49-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 myotoxins, they cause severe myonecrosis. Moreover, these toxins are used as tools to study skeletal muscle repair and regeneration, a process that can be very limited after snakebites. In this work, the cytotoxic effect of different myotoxins, Bothrops asper Lys49 and Asp49-PLA2, Notechis scutatus notexin and Naja mossambica cardiotoxin, was evaluated on macrophages, cells that have a key role in muscle regeneration. Only the Lys49-myotoxin was found to trigger a rapid asynchronous death of mouse peritoneal macrophages and macrophagic cell lines through a process that involves ATP release, ATP-induced ATP release and that is inhibited by various purinergic receptor antagonists. ATP leakage is induced also at sublytical doses of the Lys49-myotoxin, it involves Ca2þ release from intracellular stores, and is reduced by inhibitors of VSOR and the maxi-anion channel. The toxin-induced cell death is different from that caused by high concentration of ATP and appears to be linked to localized purinergic signaling. Based on present findings, a mechanism of cell death is proposed that can be extended to other cytolytic proteins and peptides.es_ES
dc.description.sponsorshipUniversidad de Costa Ricaes_ES
dc.language.isoen_USes_ES
dc.publisherCell Death and Disease (2012) 3, e343es_ES
dc.subjectLys49-PLAes_ES
dc.subjectPhospholipase A2es_ES
dc.subjectMyotoxines_ES
dc.subjectNotexines_ES
dc.subjectCardiotoxines_ES
dc.subjectPurenergic signalinges_ES
dc.subjectVeneno de serpientees_ES
dc.titleA Lys49-PLA2 myotoxin of Bothrops asper triggers a rapid death of macrophages that involves autocrine purinergic receptor signalinges_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1038/cddis.2012.68es_ES
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES


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