Please use this identifier to cite or link to this item: http://repositorio.unifesp.br/handle/11600/35828
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dc.contributor.authorBatista, Wagner L. [UNIFESP]
dc.contributor.authorOgata, Fernando T. [UNIFESP]
dc.contributor.authorCurcio, Marli F. [UNIFESP]
dc.contributor.authorMiguel, Rodrigo B. [UNIFESP]
dc.contributor.authorArai, Roberto J.
dc.contributor.authorMatsuo, Alisson L. [UNIFESP]
dc.contributor.authorMoraes, Miriam S. [UNIFESP]
dc.contributor.authorStern, Arnold
dc.contributor.authorMonteiro, Hugo P. [UNIFESP]
dc.date.accessioned2016-01-24T14:31:04Z-
dc.date.available2016-01-24T14:31:04Z-
dc.date.issued2013-01-01
dc.identifierhttp://dx.doi.org/10.1089/ars.2011.4455
dc.identifier.citationAntioxidants & Redox Signaling. New Rochelle: Mary Ann Liebert Inc, v. 18, n. 3, p. 221-238, 2013.
dc.identifier.issn1523-0864
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/35828-
dc.description.abstractAims: S-nitrosylation of Cys118 is a redox-based mechanism for Ras activation mediated by nitric oxide (NO) at the plasma membrane. Results: Ras signaling pathway stimulation by 50 and/or 100 mu M of S-nitrosoglutathione (GSNO) causes proliferation of HeLa cells. Proliferation was not observed in HeLa cells overexpressing non-nitrosatable H-Ras(C118S). HeLa cells overexpressing H-Ras(wt) containing the spatiotemporal probe green fluorescent protein (GFP) fused to the Ras-binding domain of Raf-1 (GFP-RBD) incubated with 100 mu M GSNO stimulated a rapid and transient redistribution of GFP-RBD to the plasma membrane, followed by a delayed and sustained recruitment to the Golgi. No activation of H-Ras at the plasma membrane occurred in cells overexpressing H-Ras(C118S), contrasting with a robust and sustained activation of the GTPase at the Golgi. Inhibition of Src kinase prevented cell proliferation and activation of H-Ras by GSNO at the Golgi. Human umbilical vein endothelial cells (HUVECs) stimulated with bradykinin to generate NO were used to differentiate cell proliferation and Ras activation at the plasma membrane versus Golgi. in this model, Src kinase was not involved in cell proliferation, whereas Ras activation proceeded only at the plasma membrane, indicating that HUVEC proliferation induced by NO resulted only from stimulation of Ras. Innovation: the present work is the first to demonstrate that NO-mediated activation of Ras in different subcellular compartments regulates different downstream signaling pathways. Conclusion: S-nitrosylation of H-Ras at Cys(118) and the activation of Src kinase are spatiotemporally linked events of the S-nitrosothiol-mediated signaling pathway that occurs at the plasma membrane and at the Golgi. the nonparticipation of Src kinase and the localized production of NO by endothelial NO synthase at the plasma membrane limited NO-mediated Ras activation to the plasma membrane. Antioxid. Redox Signal. 18, 221-238.en
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.format.extent221-238
dc.language.isoeng
dc.publisherMary Ann Liebert Inc
dc.relation.ispartofAntioxidants & Redox Signaling
dc.rightsAcesso restrito
dc.titleS-Nitrosoglutathione and Endothelial Nitric Oxide Synthase-Derived Nitric Oxide Regulate Compartmentalized Ras S-Nitrosylation and Stimulate Cell Proliferationen
dc.typeArtigo
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionNYU
dc.description.affiliationUniversidade Federal de São Paulo, CTCMOL, Dept Biochem Mol Biol, BR-04044010 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biol Sci, BR-04044010 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Microbiol Parasitol & Immunol, BR-04044010 São Paulo, Brazil
dc.description.affiliationUniv São Paulo, Sch Med, São Paulo Canc Inst, São Paulo, Brazil
dc.description.affiliationNYU, Sch Med, Dept Pharmacol, New York, NY USA
dc.description.affiliationUnifespUniversidade Federal de São Paulo, CTCMOL, Dept Biochem Mol Biol, BR-04044010 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biol Sci, BR-04044010 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Microbiol Parasitol & Immunol, BR-04044010 São Paulo, Brazil
dc.description.sponsorshipIDFAPESP: 07/59617-6
dc.description.sponsorshipIDFAPESP: 09/52730-7
dc.description.sponsorshipIDFAPESP: 11/14392-2
dc.identifier.doi10.1089/ars.2011.4455
dc.description.sourceWeb of Science
dc.identifier.wosWOS:000312007900001
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