12-HETE is a regulator of PGE2 production via COX-2 expression induced by a snake venom group IIA phospholipase A2 in isolated peritoneal macrophages

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dc.contributorLab. Farmacologiapt_BR
dc.contributor.authorMoreira, Vanessapt_BR
dc.contributor.authorGutiérrez, José Maríapt_BR
dc.contributor.authorLomonte, Brunopt_BR
dc.contributor.authorVinolo, Marco Aurélio Ramirezpt_BR
dc.contributor.authorCuri, Ruipt_BR
dc.contributor.authorLambeau, Gérardpt_BR
dc.contributor.authorTeixeira, Catarina de Fátima Pereirapt_BR
dc.date.accessioned2020-07-09T21:26:45Z-
dc.date.available2020-07-09T21:26:45Z-
dc.date.issued2020pt_BR
dc.identifier.citationMoreira V, Gutiérrez JM, Lomonte B, Vinolo MAR, Curi R, Lambeau G, et al. 12-HETE is a regulator of PGE2 production via COX-2 expression induced by a snake venom group IIA phospholipase A2 in isolated peritoneal macrophages. Chem. Biol. Interact.. 2020 Feb;317:108903. doi:10.1016/j.cbi.2019.108903.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/2959-
dc.description.abstractThe snake venom miotoxin (MT)-III is a group IIA secreted phospholipase A2 (sPLA2) with pro-inflammatory activities. Previous studies have demonstrated that MT-III has the ability to stimulate macrophages to release inflammatory lipid mediators derived from arachidonic acid metabolism. Among them, we highlight prostaglandin (PG)E2 produced by the cyclooxygenase (COX)-2 pathway, through activation of nuclear factor (NF)-capaB. However, the mechanisms coordinating this process are not fully understood. This study investigates the regulatory mechanisms exerted by other groups of bioactive eicosanoids derived from 12-lipoxygenase (12-LO), in particular 12-hydroxyeicosatetraenoic (12-HETE), on group IIA sPLA2-induced (i) PGE2 release, (ii) COX-2 expression, and (iii) activation of signaling pathways p38 mitogen-activated protein kinases(p38MAPK), protein C kinase (PKC), extracellular signal-regulated kinase 1/2 (ERK1/2), and NF-?B. Stimulation of macrophages with group IIA sPLA2 resulted in release of 12-HETE without modification of 12-LO protein levels. Pre-treatment of these cells with baicalein, a 12-LO inhibitor, decreased the sPLA2-induced PGE2 production, significantly reduced COX-2 expression, and inhibited sPLA2-induced ERK; however, it did not affect p38MAPK or PKC phosphorylation. In turn, sPLA2-induced PGE2 release and COX-2 expression, but not NF-capaB activation, was attenuated by pre-treating macrophages with PD98059 an inhibitor of ERK1/2. These results suggest that, in macrophages, group IIA sPLA2-induced PGE2 release and COX-2 protein expression are distinctly mediated through 12-HETE followed by ERK1/2 pathway activation, independently of NF-?B activation. These findings highlight an as yet undescribed mechanism by which 12-HETE regulates one of the distinct signaling pathways for snake venom group IIA sPLA2-induced PGE2 release and COX-2 expression in macrophages.pt_BR
dc.description.sponsorship(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulopt_BR
dc.description.sponsorship(CNPq) Conselho Nacional de Desenvolvimento Científico e Tecnológicopt_BR
dc.format.extent108903pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofChemico-Biological Interactionspt_BR
dc.rightsRestricted accesspt_BR
dc.title12-HETE is a regulator of PGE2 production via COX-2 expression induced by a snake venom group IIA phospholipase A2 in isolated peritoneal macrophagespt_BR
dc.typeArticlept_BR
dc.identifier.doi10.1016/j.cbi.2019.108903pt_BR
dc.identifier.urlhttps://doi.org/10.1016/j.cbi.2019.108903pt_BR
dc.contributor.external(UNIFESP) Universidade Federal de São Paulopt_BR
dc.contributor.external(UCR) Universidad de Costa Ricapt_BR
dc.contributor.external(UNICAMP) Universidade Estadual de Campinaspt_BR
dc.contributor.external(USP) Universidade de São Paulopt_BR
dc.identifier.citationvolume317pt_BR
dc.subject.keywordSnake venom group IIA phospholipase A2pt_BR
dc.subject.keywordProstaglandin E2pt_BR
dc.subject.keywordCyclooxygenase-2pt_BR
dc.subject.keyword12-Hydroxyeicosatetraenoic acidpt_BR
dc.subject.keyword2-Lipoxygenasept_BR
dc.subject.keywordmacrophagespt_BR
dc.relation.ispartofabbreviatedChem Biol Interactpt_BR
dc.identifier.citationabntv. 317, 108903, fev. 2020pt_BR
dc.identifier.citationvancouver2020 Feb;317:108903pt_BR
dc.contributor.butantanTeixeira, Catarina de Fátima Pereira|:Pesquisador:Docente Permanente PPGTOX|:Lab. Farmacologia|:pt_BR
dc.sponsorship.butantan(CNPq) Conselho Nacional de Desenvolvimento Científico e Tecnológico¦¦306099/2008-0pt_BR
dc.sponsorship.butantan(CNPq) Conselho Nacional de Desenvolvimento Científico e Tecnológico¦¦202077/2008-0pt_BR
dc.sponsorship.butantan(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo¦¦07/03336-9pt_BR
dc.sponsorship.butantan(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo¦¦07/03337-5pt_BR
dc.sponsorship.butantan(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo¦¦12/10653-9pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
item.openairetypeArticle-
item.grantfulltextembargo_29990101-
item.fulltextCom Texto completo-
item.languageiso639-1English-
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