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dc.contributor.authorHoppe, J.B.
dc.contributor.authorRattray, Marcus
dc.contributor.authorTu, H.
dc.contributor.authorSalbego, C.G.
dc.contributor.authorCimarosti, H.
dc.date.accessioned2016-02-23T16:26:25Z
dc.date.available2016-02-23T16:26:25Z
dc.date.issued2013-06
dc.identifier.citationHoppe JB, Rattray M, Tu H, Salbego CG and Cimarosti H (2013) SUMO-1 conjugation blocks beta-amyloid-induced astrocyte reactivity. Neuroscience Letters, 546: 51-6.en_US
dc.identifier.urihttp://hdl.handle.net/10454/7805
dc.description-en_US
dc.description.abstractAstrocyte reactivity is implicated in the neuronal loss underlying Alzheimer's disease. Curcumin has been shown to reduce astrocyte reactivity, though the exact pathways underlying these effects are incompletely understood. Here we investigated the role of the small ubiquitin-like modifier (SUMO) conjugation in mediating this effect of curcumin. In beta-amyloid (Aβ)-treated astrocytes, morphological changes and increased glial fibrillary acidic protein (GFAP) confirmed reactivity, which was accompanied by c-jun N-terminal kinase activation. Moreover, the levels of SUMO-1 conjugated proteins, as well as the conjugating enzyme, Ubc9, were decreased, with concomitant treatment with curcumin preventing these effects. Increasing SUMOylation in astrocytes, by over-expression of constitutively active SUMO-1, but not its inactive mutant, abrogated Aβ-induced increase in GFAP, suggesting astrocytes require SUMO-1 conjugation to remain non-reactive.en_US
dc.language.isoenen_US
dc.relation.isreferencedbyhttp://doi.org/10.1016/j.neulet.2013.04.050en_US
dc.subjectAlzheimer's disease; Beta-amyloid peptide; c-Jun N-terminal kinase; Curcumin; Reactivity; Small ubiquitin-like modifier (SUMO) conjugationen_US
dc.titleSUMO-1 conjugation blocks beta-amyloid-induced astrocyte reactivity.en_US
dc.status.refereedyesen_US
dc.typeArticleen_US
dc.type.versionAccepted Manuscripten_US


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