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dc.rights.licenseopenen_US
dc.contributor.authorHORNEDO ORTEGA, Ruth
hal.structure.identifierUnité de Recherche Oenologie [Villenave d'Ornon] [OENO]
dc.contributor.authorDA COSTA, Gregory
dc.contributor.authorCEREZO, Ana B.
dc.contributor.authorTRONCOSO, Ana M.
hal.structure.identifierUnité de Recherche Oenologie [Villenave d'Ornon] [OENO]
dc.contributor.authorRICHARD, Tristan
dc.contributor.authorGARCIA-PARRILLA, M. Carmen
dc.date.accessioned2020-08-27T12:36:18Z
dc.date.available2020-08-27T12:36:18Z
dc.date.issued2018
dc.identifier.issn1613-4125en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10685
dc.description.abstractEnScope: Amyloid-beta peptide is the main component of senile plaques in Alzheimer's disease. The inhibition of amyloid-beta peptide assembly, the destabilization of amyloid-beta peptide aggregates, and the decrease of its cytotoxicity for the prevention of neuronal death are considered neuroprotective effects. In this work, the protective effects against amyloid-beta peptide aggregation and cytotoxicity of eight indolic compounds are evaluated: tryptophan, tryptamine, serotonin, tryptophol, N-acetylserotonin, 3-indoleacetic acid, tryptophan ethyl ester, and melatonin. [br/] Methods and results: Thioflavin T spectroscopic assay, transmission electron microscopy, western blotting, circular dichroism, NMR, cell viability (thiazolyl blue tetrazolium bromide assay), quantitative PCR, and heme oxygenase activity are used. Serotonin is the most effective compound for inhibiting amyloid-beta peptide aggregation. Almost all the indolic compounds tested prevent amyloid-beta peptide-induced and increase cell viability, being between 9 and 25%. Melatonin and serotonin are the most active. Moreover, serotonin increased the expression of SIRT-1 and 2, heat shock protein 70, and heme oxygenase activity, this being a possible mechanism underlying the observed neuroprotective effect. [br/] Conclusion: Melatonin and other related indolic compounds, mainly serotonin, show an inhibitory and destabilizing effect on amyloid-beta peptide fibril formation and they possess neuroprotective properties related to the vitagenes system.
dc.language.isoENen_US
dc.subjectPeptide Amyloïde
dc.subjectÉlectrophorèse
dc.subjectMaladie d'Alzheimer
dc.subjectNeuroprotection
dc.subject.enAmyloid-Beta
dc.subject.enFibril Formation
dc.subject.enIndolic
dc.subject.enNeuroprotection
dc.subject.enVitagene System
dc.title.enIn vitro effects of serotonin, melatonin, and other related indole compounds on amyloid-β kinetics and neuroprotection
dc.title.alternativeMol. nutr. food res.en_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1002/mnfr.201700383en_US
dc.subject.halSciences du Vivant [q-bio]/Biologie végétaleen_US
bordeaux.journalMolecular Nutrition and Food Researchen_US
bordeaux.page1-12en_US
bordeaux.volume62en_US
bordeaux.hal.laboratoriesOenologie - EA 4577en_US
bordeaux.issue3en_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.exportfalse
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Molecular%20Nutrition%20and%20Food%20Research&rft.date=2018&rft.volume=62&rft.issue=3&rft.spage=1-12&rft.epage=1-12&rft.eissn=1613-4125&rft.issn=1613-4125&rft.au=HORNEDO%20ORTEGA,%20Ruth&DA%20COSTA,%20Gregory&CEREZO,%20Ana%20B.&TRONCOSO,%20Ana%20M.&RICHARD,%20Tristan&rft.genre=article


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