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dc.contributor.authorTramutola A.
dc.contributor.authorLanzillotta C.
dc.contributor.authorArena A.
dc.contributor.authorBarone E.
dc.contributor.authorPerluigi M.
dc.contributor.authorDi Domenico F.
dc.date.accessioned2020-09-02T22:29:22Z
dc.date.available2020-09-02T22:29:22Z
dc.date.issued2016
dc.identifier10.1159/000441419
dc.identifier.citation16, 1-2, 62-68
dc.identifier.issn16602854
dc.identifier.urihttps://hdl.handle.net/20.500.12728/6434
dc.descriptionBackground: Neurodegenerative diseases are characterized by increased levels of oxidative stress and an altered mammalian target of rapamycin (mTOR)/autophagy axis; however, the mutual relationship between these two events is controversial. Previous studies in Down's syndrome (DS) and Alzheimer's disease (AD) suggested that the accumulation of protein oxidative damage results from the increased free radical production, mainly related to metabolic alterations, mitochondrial degeneration and amyloid-β deposition, and aberrant activity of protein degradative systems. Summary: This study analyzed mTOR signaling in Ts65Dn mice, a model of DS, at 6 and 12 months of age compared with euploid mice showing the early aberrant hyperphosphorylation of mTOR coupled with the reduction of autophagosome formation. Moreover, the evaluation of protein oxidation shows an increase in protein nitration and protein-bound 4-hydroxynonenal in 12-month-old Ts65Dn mice suggesting the potential involvement of altered autophagy in the buildup of protein oxidative damage. In addition, data obtained on cell culture support the protective role of autophagy in reducing protein oxidation. Key Messages: Overall, this study provides further evidence for the role of mTOR hyperactivation and reduced autophagy in the accumulation of protein oxidative damage during DS and AD pathologies.Background: Effective therap. © 2015 S. Karger AG, Basel.
dc.language.isoen
dc.publisherS. Karger AG
dc.subjectAlzheimer's disease
dc.subjectAutophagy
dc.subjectDown's syndrome
dc.subjectMammalian target of rapamycin
dc.subjectProtein oxidation
dc.subject4 hydroxynonenal
dc.subjectmammalian target of rapamycin
dc.subjectrapamycin
dc.subjectMTOR protein, human
dc.subjectmTOR protein, mouse
dc.subjecttarget of rapamycin kinase
dc.subjectanimal cell
dc.subjectanimal experiment
dc.subjectanimal model
dc.subjectautophagosome
dc.subjectautophagy
dc.subjectcell viability
dc.subjectConference Paper
dc.subjectcontrolled study
dc.subjectDown syndrome
dc.subjectfemale
dc.subjectmale
dc.subjectmouse
dc.subjectMTT assay
dc.subjectneuroblastoma cell
dc.subjectnonhuman
dc.subjectoxidation
dc.subjectoxidative stress
dc.subjectpriority journal
dc.subjectprotein phosphorylation
dc.subjectreciprocal chromosome translocation
dc.subjectsignal transduction
dc.subjecttrisomy
dc.subjectWestern blotting
dc.subjectanimal
dc.subjectC3H mouse
dc.subjectC57BL mouse
dc.subjectdisease model
dc.subjectDown syndrome
dc.subjecthippocampus
dc.subjecthuman
dc.subjectmetabolism
dc.subjectoxidation reduction reaction
dc.subjectphosphorylation
dc.subjectsignal transduction
dc.subjecttransgenic mouse
dc.subjecttumor cell line
dc.subjectAnimals
dc.subjectBlotting, Western
dc.subjectCell Line, Tumor
dc.subjectDisease Models, Animal
dc.subjectDown Syndrome
dc.subjectHippocampus
dc.subjectHumans
dc.subjectMice, Inbred C3H
dc.subjectMice, Inbred C57BL
dc.subjectMice, Transgenic
dc.subjectOxidation-Reduction
dc.subjectPhosphorylation
dc.subjectSignal Transduction
dc.subjectSirolimus
dc.subjectTOR Serine-Threonine Kinases
dc.titleIncreased mammalian target of rapamycin signaling contributes to the accumulation of protein oxidative damage in a mouse model of down's syndrome
dc.typeConference Paper


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