Estrogen receptor ESR1 regulates the phospholipase C-inositol phosphate signaling in the hippocampus from rats in proestrous and estrous phases

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dc.contributor.author Maruyama, Nadia O.
dc.contributor.author Lucas, Thais F. G. [UNIFESP]
dc.contributor.author Porto, Catarina S. [UNIFESP]
dc.contributor.author Abdalla, Fernando M. F.
dc.date.accessioned 2016-01-24T14:31:04Z
dc.date.available 2016-01-24T14:31:04Z
dc.date.issued 2013-01-01
dc.identifier http://dx.doi.org/10.1016/j.steroids.2012.10.005
dc.identifier.citation Steroids. New York: Elsevier B.V., v. 78, n. 1, p. 8-14, 2013.
dc.identifier.issn 0039-128X
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/35816
dc.description.abstract The aim of the present study was to investigate the involvement of estrogen receptors in the activation of phospholipase C (PLC)-phosphoinositide hydrolysis in the hippocampus from rats in estrous and proestrous phases. 17 beta-Estradiol (E2) and ESR1 -selective agonist PPT, but not ESR2-selective agonist DPN, induced a rapid increase on total [H-3]-inositol phosphate accumulation in the hippocampus from both rats. These effects are mediated by PLC activation, since the inhibition of this protein decreased the total [H-3]-inositol phosphate accumulation. the pretreatment with ESR1 and ESR2 antagonist ICI 182,780, but not with GPER antagonist G-15, blocked the total [H-3]-inositol phosphate accumulation induced by E2 and PPT, confirming that ESR1 is upstream component regulating this rapid effect. SRC family of protein tyrosine kinases inhibitor PP2 blocked the total [H-3]-inositol phosphate accumulation induced by E2 and PPT in hippocampus, suggesting that ESR1 undergoes translocation from the nuclei to the plasma membrane region via SRC to activate rapid signaling pathways. Furthermore, the magnitude of the response to E2 and PPT was higher in hippocampus from rats in proestrous than in estrous. On the other hand, the expression of the ESR1 is higher in hippocampus from rats in estrous than in proestrous, indicating that the regulation of this receptor by estrous cycle does not play a role in the magnitude of the response to E2 and PPT in hippocampus. in conclusion, our results indicate that E2 activates SRC-mediated translocation of ESR1 to the plasma membrane, which results in the activation of PLC-inositol phosphate signaling pathway in rat hippocampus. Thus, these rapid estrogen actions in hippocampus might be a key step mediating cellular events important for learning and memory. (C) 2012 Elsevier Inc. All rights reserved. en
dc.description.sponsorship Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorship Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorship Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.format.extent 8-14
dc.language.iso eng
dc.publisher Elsevier B.V.
dc.relation.ispartof Steroids
dc.rights Acesso restrito
dc.subject Hippocampus en
dc.subject 17 beta-Estradiol en
dc.subject PPT en
dc.subject Inositol phosphate en
dc.subject Estrogen receptors en
dc.title Estrogen receptor ESR1 regulates the phospholipase C-inositol phosphate signaling in the hippocampus from rats in proestrous and estrous phases en
dc.type Artigo
dc.rights.license http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institution Inst Butantan
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.description.affiliation Inst Butantan, Pharmacol Lab, BR-05503900 São Paulo, Brazil
dc.description.affiliation Universidade Federal de São Paulo, Escola Paulista Med, Dept Pharmacol, Sect Expt Endocrinol, São Paulo, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Escola Paulista Med, Dept Pharmacol, Sect Expt Endocrinol, São Paulo, Brazil
dc.description.sponsorshipID FAPESP: 08/56564-1
dc.identifier.doi 10.1016/j.steroids.2012.10.005
dc.description.source Web of Science
dc.identifier.wos WOS:000314432500002



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