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dc.contributor.authorHernández Garrido, Marita 
dc.contributor.authorFernández de Arriba, Alberto
dc.contributor.authorMerlos, Manel
dc.contributor.authorFuentes, Lucía
dc.contributor.authorSánchez Crespo, Mariano
dc.contributor.authorNieto Callejo, María Luisa
dc.date.accessioned2021-06-23T07:45:36Z
dc.date.available2021-06-23T07:45:36Z
dc.date.issued2001
dc.identifier.citationThe British Journal of Pharmacology, 2001, vol. 132, n. 2. p. 547-555es
dc.identifier.issn1476-5381es
dc.identifier.urihttps://uvadoc.uva.es/handle/10324/47014
dc.descriptionProducción Científicaes
dc.description.abstractThe effect of two derivatives of salicylate, 2-hydroxy-4-trifluoromethylbenzoic acid (HTB) and 2-acetoxy-4-trifluoromethylbenzoic acid (triflusal), on the expression of several proteins displaying pro-inflammatory activities the regulation of which is associated to the transcription factor NF-κB, was assayed in the human astrocytoma cell line 1321N1. Tumour necrosis factor-α (TNF-α) activated NF-κB as judged from both the appearance of κB-binding activity in the nuclear extracts, the degradation of IκB proteins in the cell lysates, and the activation of IκB kinases using an immunocomplex kinase assay with glutathione S-transferase (GST)-IκB proteins as substrates. HTB up to 3 mM did not inhibit the nuclear translocation of NK-κB/Rel proteins as judged from electrophoretic mobility-shift assays; however, HTB inhibited the degradation of IκBβ without significantly affecting the degradation of both IκBα and IκBε. In keeping with their inhibitory effect on IκBβ degradation in the cell lysates, both HTB and triflusal inhibited the phosphorylation of GST-IκBβ elicited by TNF-α, without affecting the phosphorylation of GST-IκBα. The effect of both HTB and triflusal on κB-dependent trans-activation was studied by assaying the expression of both cyclo-oxygenase-2 (COX-2) and vascular cell adhesion molecule-1 (VCAM-1). HTB and triflusal inhibited in a dose-dependent manner the expression of COX-2 and VCAM-1 mRNA and the induction of COX-2 protein at therapeutically relevant concentrations. These findings show the complexity of the biochemical mechanisms underlying the activation of NF-κB in the different cell types and extend the anti-inflammatory effects of HTB and triflusal to neural cells.es
dc.format.mimetypeapplication/pdfes
dc.language.isoenges
dc.publisherWileyes
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subject.classificationAdhesion moleculeses
dc.subject.classificationMoléculas de adhesiónes
dc.subject.classificationAlzheimer’s diseasees
dc.subject.classificationAlzheimer, Enfermedad dees
dc.subject.classificationAspirines
dc.subject.classificationAspirinaes
dc.subject.classificationAstrocyteses
dc.subject.classificationAstrocitoses
dc.titleEffect of 4-trifluoromethyl derivatives of salicylate on nuclear factor κB-dependent transcription in human astrocytoma cellses
dc.typeinfo:eu-repo/semantics/articlees
dc.rights.holder© 2009 Wileyes
dc.identifier.doi10.1038/sj.bjp.0703820es
dc.relation.publisherversionhttps://bpspubs.onlinelibrary.wiley.com/doi/abs/10.1038/sj.bjp.0703820es
dc.peerreviewedSIes
dc.description.projectPlan Nacional de Salud y Farmacia (grant SAF98/0176)es
dc.description.projectComisión Interministerial de Ciencia y Tecnología - Comisión Europea (grant IFD97-0590)es
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersiones


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