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dc.contributor.authorPountney, DL
dc.contributor.authorLowe, R
dc.contributor.authorQuilty, M
dc.contributor.authorVickers, JC
dc.contributor.authorVoelcker, NH
dc.contributor.authorGai, WP
dc.date.accessioned2017-05-03T15:03:35Z
dc.date.available2017-05-03T15:03:35Z
dc.date.issued2004
dc.identifier.issn0022-3042
dc.identifier.doi10.1111/j.1471-4159.2004.02533.x
dc.identifier.urihttp://hdl.handle.net/10072/16891
dc.description.abstractOligodendroglial cytoplasmic inclusions composed of a-synuclein filamentous aggregates are the pathological hallmark of multiple system atrophy (MSA). We found that cortical tissue from MSA cases contains increased detergent-resistant high-molecular-weight a-synuclein species. To analyse these species, we immunopurified a-synuclein aggregates from pathological samples and examined their ultrastructures using scanning electron and atomic force microscopies. Purified aggregates consisted of bundles of filaments. After treatment with 1% sarcosine or 2% 3-[(3-cholamidopropyl) dimethyl-ammonio]-1-propanesulfonate (CHAPS) detergents, we observed frequent 30-50 nm annular particles, probably released from pathological aggregates due to the dissociation of filaments by the detergents. Antibody recognition imaging using a specific anti-a-synuclein antibody confirmed that the annular structures were positive for a-synuclein. In contrast to pathological a-synuclein, detergent treatment of recombinant a-synuclein yielded only smaller, 10-18 nm spherical particles. Our results demonstrate that detergent treatment of pathological MSA a-synuclein aggregates, but not recombinant a-synuclein, yields discrete a-synuclein-positive species with annular morphologies. The ability of the pathological a-synuclein to form annular aggregates may be an important factor contributing to the toxicity of the protein in disease that may have implications in designing therapeutic strategies aimed at detoxifying a-synuclein aggregates.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherBlackwell
dc.publisher.placeOxford
dc.relation.ispartofpagefrom502
dc.relation.ispartofpageto512
dc.relation.ispartofissue2
dc.relation.ispartofjournalJournal of Neurochemistry
dc.relation.ispartofvolume90
dc.subject.fieldofresearchBiochemistry and cell biology
dc.subject.fieldofresearchNeurosciences
dc.subject.fieldofresearchcode3101
dc.subject.fieldofresearchcode3209
dc.titleAnnular α-synuclein species from purified multiple system atrophy inclusions
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.date.issued2015-05-12T05:11:30Z
gro.hasfulltextNo Full Text
gro.griffith.authorPountney, Dean L.


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