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dc.creatorCintra Francischinelli, Mariana
dc.creatorPizzo, Paola
dc.creatorAngulo Ugalde, Yamileth
dc.creatorGutiérrez, José María
dc.creatorMontecucco, Cesare
dc.creatorLomonte, Bruno
dc.date.accessioned2016-11-29T12:56:44Z
dc.date.available2016-11-29T12:56:44Z
dc.date.issued2010-02
dc.identifier.citationhttp://www.sciencedirect.com/science/article/pii/S0041010109005029es_ES
dc.identifier.issn0041-0101
dc.identifier.urihttp://hdl.handle.net/10669/29330
dc.description.abstractMyotoxins 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 mechanisms of action are still poorly understood, but there is evidence that the C-terminal region is involved in membrane damage leading to myotoxicity. To investigate the effect of the C-terminal peptide 115–129 of Agkistrodon contortrix laticinctus myotoxin on the plasma membrane of myoblasts and myotubes, the entry of Ca2+ was monitored by fluorescence imaging, and the ensuing cytotoxicity was determined. The myotoxin synthetic peptide was found to act selectively on myotubes, which were rapidly overloaded with Ca2+ with ensuing necrosis. The profile of intracellular Ca2+ increase induced by the C-terminal peptide, but not by its scrambled version control, reproduces the second, prominent wave of the biphasic response documented in previous studies using whole Lys49 myotoxins. These observations provide relevant insights into the mechanism of action of this family of toxins, with implications for the understanding of their structure–function relationships.es_ES
dc.description.sponsorshipTelethon/GGP06133//es_ES
dc.description.sponsorshipInternational Centre of Genetic Engeneering and Biotechnology - Collaborative Research Programme/[COS-08-03]/ICGEB/Italiaes_ES
dc.description.sponsorshipUniversidad de Costa Rica//UCR/Costa Ricaes_ES
dc.description.sponsorshipFondazione Cariparo Progetto ‘‘Physiopathology of the synapse: neurotransmitters, neurotoxins and novel therapies"///Italiaes_ES
dc.language.isoen_USes_ES
dc.sourceToxicon; Volumen 55, Número 2-3. 2010es_ES
dc.subjectMyotubeses_ES
dc.subjectCalciumes_ES
dc.subjectMyotoxines_ES
dc.subjectPhospholipase A2 homologuees_ES
dc.subjectLys49es_ES
dc.subjectPeptidees_ES
dc.subjectVenomes_ES
dc.subjectSnake venomes_ES
dc.titleThe C-terminal region of a Lys49 myotoxin mediates Ca2þ influx in C2C12 myotubeses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1016/j.toxicon.2009.10.013
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES


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