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dc.creatorBustillo, Soledad
dc.creatorGarcía Denegri, María Emilia
dc.creatorGay, Carolina
dc.creatorVan de Velde, Andrea C.
dc.creatorAcosta, Ofelia
dc.creatorAngulo Ugalde, Yamileth
dc.creatorLomonte, Bruno
dc.creatorGutiérrez, José María
dc.creatorLeiva, Laura
dc.date.accessioned2017-07-07T14:03:07Z
dc.date.available2017-07-07T14:03:07Z
dc.date.issued2015-10-05
dc.identifier.citationhttp://www.sciencedirect.com/science/article/pii/S0009279715300314es_ES
dc.identifier.issn0009-2797
dc.identifier.urihttp://hdl.handle.net/10669/30334
dc.description.abstractMicrovessel 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 Bothrops alternatus, displays a potent hemorrhagic effect, and a moderate myotoxicity in vivo. Previous studies described the ability of this SVMP to induce the detachment of C2C12 myoblasts in culture, without causing cytolysis. Surprisingly, a purified acidic phospholipase A2 (PLA2) from the same venom was found to increase this detaching activity of the SVMP on myoblasts. Since endothelial cells are a natural target of SVMPs in vivo, the possibility that this synergistic effect is also observed on this cell type was explored in the present work. In addition, a first approach of the mechanism of action of this effect was studied. Results clearly confirm that the acidic PLA2, despite lacking toxicity towards endothelial cells, significantly enhances the detaching effect of the SVMP even at a concentration as low as 1 μg/mL. Inhibition of enzymatic activity of the PLA2 by chemical modification with p-bromophenacyl bromide did not affect the synergistic activity, suggesting that this effect is not dependent on phospholipase enzymatic activity and may instead be the consequence of an interaction of the PLA2 with endothelial cell plasma membrane. To our knowledge, this is the first report of a synergistic action of a non toxic PLA2 in enhancing the detachment of endothelial cells induced by a metalloproteinase.es_ES
dc.description.sponsorshipUniversidad Nacional del Nordeste/[PI B013-2010]/UNNE/Argentinaes_ES
dc.description.sponsorshipUniversidad Nacional del Nordeste/[PI CF02-2013]/UNNE/Argentinaes_ES
dc.description.sponsorshipFondo para la Investigación Científica y Tecnológica/[PICTO 2007-00143]/FonCyT/Argentinaes_ES
dc.description.sponsorshipSecretaría General de Ciencia y Tecnología - Universidad Nacional del Nordeste/[PICTO 2007-00143]/SGCyT UNNE/Argentinaes_ES
dc.description.sponsorshipUniversidad de Costa Rica/[741-B4-100]/UCR/Costa Ricaes_ES
dc.description.sponsorshipUniversidad de Costa Rica/[741-B3-760]/UCR/Costa Ricaes_ES
dc.language.isoen_USes_ES
dc.sourceChemico-Biological Interactions; Volumen 240. 2015es_ES
dc.subjectMetalloproteinasees_ES
dc.subjectPhospholipase A2es_ES
dc.subjectEndothelial cellses_ES
dc.subjectSnake venomes_ES
dc.subjectSynergismes_ES
dc.titlePhospholipase A2 enhances the endothelial cell detachment effect of a snake venom metalloproteinase in the absence of catalysises_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1016/j.cbi.2015.08.002
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.codproyecto741-B4-100
dc.identifier.codproyecto741-B3-760
dc.identifier.pmid26279213


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