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dc.creatorGiannotti, Karina Cristinaes_ES
dc.creatorLeiguez, Elbioes_ES
dc.creatorMoreira, Vanessaes_ES
dc.creatorGalvão Nascimento, Neidees_ES
dc.creatorLomonte, Brunoes_ES
dc.creatorGutiérrez, José Maríaes_ES
dc.creatorLopes de Melo, Robsones_ES
dc.creatorTeixeira, Catarina de Fátimaes_ES
dc.date.accessioned2016-12-09T19:23:21Zes_ES
dc.date.available2016-12-09T19:23:21Zes_ES
dc.date.issued2013es_ES
dc.identifier.citationhttps://www.hindawi.com/journals/bmri/2013/807982/es_ES
dc.identifier.issn2314-6141es_ES
dc.identifier.urihttp://hdl.handle.net/10669/29383es_ES
dc.description.abstractMT-II, a Lys49PLA2 homologue devoid of catalytic activity from B. asper venom, stimulates inflammatory events in macrophages. We investigated the ability of MT-II to induce formation of lipid droplets (LDs), key elements of inflammatory responses, in isolated macrophages and participation of protein kinases and intracellular PLA2s in this effect. Influence of MT-II on PLIN2 recruitment and expression was assessed, and the effects of some synthetic peptides on LD formation were further evaluated. At noncytotoxic concentrations, MT-II directly activated macrophages to form LDs. This effect was reproduced by a synthetic peptide corresponding to the C-terminal sequence 115–129 of MT-II, evidencing the critical role of C-terminus for MT-II-induced effect. Moreover, MT-II induced expression and recruitment of PLIN2. Pharmacological interventions with specific inhibitors showed that PKC, PI3K, ERK1/2, and iPLA2, but not P38MAPK or cPLA2, signaling pathways are involved in LD formation induced by MT-II. This sPLA2 homologue also induced synthesis of PGE2 that colocalized to LDs. In conclusion, MT-II is able to induce formation of LDs committed to PGE2 formation in a process dependent on C-terminal loop engagement and regulated by distinct protein kinases and iPLA2. LDs may constitute an important inflammatory mechanism triggered by MT-II in macrophages.es_ES
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo/[2011/21341-5]/FAPESP/Brasiles_ES
dc.description.sponsorshipUniversidad de Costa Rica//UCR/Costa Ricaes_ES
dc.language.isoen_USes_ES
dc.rightsAtribución 3.0 Costa Ricaes_ES
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/cr/es_ES
dc.sourceBioMed Research International; Volumen 2013. 2013es_ES
dc.subjectPhospholipase A2es_ES
dc.subjectAnimalses_ES
dc.subjectSnake venomes_ES
dc.titleA Lys49 Phospholipase A2, Isolated from Bothrops asper Snake Venom, Induces Lipid Droplet Formation in Macrophages Which Depends on Distinct Signaling Pathways and the C-Terminal Regiones_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1155/2013/807982es_ES
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES


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Atribución 3.0 Costa Rica
Except where otherwise noted, this item's license is described as Atribución 3.0 Costa Rica