Annular alpha-synuclein species from purified multiple system atrophy inclusions

Journal of Neurochemistry
Dean L PountneyWeiPing Gai

Abstract

Oligodendroglial cytoplasmic inclusions composed of alpha-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 alpha-synuclein species. To analyse these species, we immunopurified alpha-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-alpha-synuclein antibody confirmed that the annular structures were positive for alpha-synuclein. In contrast to pathological alpha-synuclein, detergent treatment of recombinant alpha-synuclein yielded only smaller, 10-18 nm spherical particles. Our results demonstrate that detergent treatment of pathological MSA alpha-synuclein aggregates, but not recombinant alpha-synuclein, yields discrete ...Continue Reading

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