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dc.creatorRangel Hasbún, José Andrés
dc.creatorQuesada, Orestes
dc.creatorGutiérrez, José María
dc.creatorAngulo Ugalde, Yamileth
dc.creatorLomonte, Bruno
dc.date.accessioned2017-02-24T20:49:07Z
dc.date.available2017-02-24T20:49:07Z
dc.date.issued2011-04-19
dc.identifier.citationhttp://onlinelibrary.wiley.com/doi/10.1002/cbf.1758/pdfes_ES
dc.identifier.issn1099-0844
dc.identifier.urihttp://hdl.handle.net/10669/29554
dc.description19-04-2081 Embargo por política editoriales_ES
dc.description.abstractLys49 phospholipase A2 (PLA2) homologues present in crotalid snake venoms lack enzymatic activity, yet they induce skeletal muscle necrosis by a membrane permeabilizing mechanism whose details are only partially understood. The present study evaluated the effect of altering the membrane cholesterol content on the cytolytic activity of myotoxin II, a Lys49 PLA2 isolated from the venom of Bothrops asper, using the myogenic cell line C2C12 as a model target. Cell membrane cholesterol depletion by methyl-β-cyclodextrin (MβCD) treatment enhanced the cytolytic action of myotoxin II, as well as of its bioactive C-terminal synthetic peptide p(115-129) . Conversely, cell membrane cholesterol enrichment by preformed cholesterol-MβCD complexes reduced the cytolytic effect of myotoxin II. The toxic actions of myotoxin I, a catalytically active PLA2 from the same venom, as well as of the cytolytic peptide melittin from bee venom, also increased in cholesterol-depleted cells. Although physical and functional changes resulting from variations in membrane cholesterol are complex, these findings suggest that membrane fluidity could be a relevant parameter to explain the observed modulation of the cytolytic mechanism of myotoxin II, possibly influencing bilayer penetration. In concordance, the cytolytic effect of myotoxin II decreased in direct proportion to lower temperature, a physical factor that affects membrane fluidity. In conclusion, physicochemical properties that depend on membrane cholesterol content significantly influence the cytolytic mechanism of myotoxin II, reinforcing the concept that the primary site of action of Lys49 PLA2 myotoxins is the plasma membrane.es_ES
dc.description.sponsorshipUniversidad de Costa Rica/[741‐A9‐513]/UCR/Costa Ricaes_ES
dc.description.sponsorshipinternational Centre for Genetic Engeneering and Biotechnology - Collaborative Research Programme/[COS‐ 08‐03)]/ICGEB‐CRP/Italiaes_ES
dc.language.isoen_USes_ES
dc.sourceCell Biochemistry and Function; Volumen 29, Número 5. 2011es_ES
dc.subjectCholesteroles_ES
dc.subjectMembranees_ES
dc.subjectFluidityes_ES
dc.subjectMyotoxines_ES
dc.subjectSnake venomes_ES
dc.subjectPhospholipase A2es_ES
dc.subjectCytolysises_ES
dc.subjectC2C12 myoblastses_ES
dc.titleMembrane cholesterol modulates the cytolytic mechanism of myotoxin II, a Lys49 phospholipase A2 homologue from the venom of Bothrops asperes_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1002/cbf.1758
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES


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