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dc.creatorLeiguez, Elbio
dc.creatorPavan Zuliani, Juliana
dc.creatorMarques Cianciarullo, Aurora
dc.creatorFernandes, Cristina Maria
dc.creatorGutiérrez, José María
dc.creatorTeixeira, Catarina de Fátima
dc.date.accessioned2017-02-27T19:40:57Z
dc.date.available2017-02-27T19:40:57Z
dc.date.issued2011-07
dc.identifier.citationhttp://www.jleukbio.org/content/90/1/155.longes_ES
dc.identifier.issn0741-5400
dc.identifier.urihttp://hdl.handle.net/10669/29560
dc.descriptionVersión final embargada hasta 2081-07 por políticas editorialeses_ES
dc.description.abstractWe investigated the ability of the sPLA(2), known as MT-III, isolated from the viperid snake Bothrops asper, to induce LB formation in macrophages and the major cellular signaling pathways involved in this process. The effects of MT-III on ADRP localization and expression and macrophage ultrastructure were assessed. Our results showed that this sPLA(2) induced a marked increase in LB numbers in macrophages, induced the recruitment of ADRP in macrophages, and up-regulated ADRP expression. Ultrastructural analysis showed the presence of weakly and strongly osmiophilic LBs in sPLA(2)-stimulated cells. Enlargement of the ER and Golgi cisterns was also observed. Pretreatment of cells with H7 or staurosporine (PKC inhibitors), LY294002 or wortmannin (PI3K inhibitors), SB202190 or PD98059 (p38(MAPK) and ERK1/2 inhibitors, respectively), or Pyr-2 or Bel (cPLA(2) and iPLA(2) inhibitors, respectively) significantly reduced sPLA(2)-induced LB formation. Herbimycin (a PTK inhibitor) and indomethacin or etoricoxib (COX inhibitors) failed to alter sPLA(2)-induced effects. In conclusion, our results show for the first time the ability of a venom sPLA(2) to induce the formation of LBs and the expression of ADRP in macrophages. Venom PLA(2)-induced LB formation is dependent on PKC, PI3K, p38(MAPK), ERK1/2, cPLA(2), and iPLA(2) signaling pathways but not on PTK, COX-1, or COX-2 pathways. Activation of the ER and Golgi complex may play an important role in the formation of LBs induced by this sPLA(2) in macrophages.es_ES
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo/[06/58334-8]/FAPESP/Brasiles_ES
dc.description.sponsorshipInstituto Nacional de Ciencia e Tecnologia em Toxinas//INCTTOX/Braziles_ES
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico//CNPq/Brasiles_ES
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo/[08/58988-3]/FAPESP/Brasiles_ES
dc.description.sponsorshipUniversidad de Costa Rica//UCR/Costa Ricaes_ES
dc.language.isoen_USes_ES
dc.sourceJournal of Leukocyte Biology; Volumen 90, Número 1. 2011es_ES
dc.subjectAnimalses_ES
dc.subjectBlotting, Westernes_ES
dc.subjectBothropses_ES
dc.subjectCrotalid Venomses_ES
dc.subjectEndoplasmic Reticulumes_ES
dc.subjectGolgi Apparatuses_ES
dc.subjectGroup II Phospholipases A2es_ES
dc.subjectImmunohistochemistryes_ES
dc.subjectInclusion Bodieses_ES
dc.subjectLipidses_ES
dc.subjectMacrophageses_ES
dc.subjectMalees_ES
dc.subjectMicees_ES
dc.subjectMicroscopy, Electron, Transmissiones_ES
dc.subjectSignal Transductiones_ES
dc.titleA group IIA-secreted phospholipase A2 from snake venom induces lipid body formation in macrophages: the roles of intracellular phospholipases A2 and distinct signaling pathwayses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1189/jlb.0510263
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.pmid21478270


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