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. 1998 Jul 20;799(2):301-6.
doi: 10.1016/s0006-8993(98)00514-9.

Human recombinant NACP/alpha-synuclein is aggregated and fibrillated in vitro: relevance for Lewy body disease

M Hashimoto  1 , L J Hsu, A Sisk, Y Xia, A Takeda, M Sundsmo, E Masliah
Affiliations

Human recombinant NACP/alpha-synuclein is aggregated and fibrillated in vitro: relevance for Lewy body disease

M Hashimoto et al. Brain Res. .

Abstract

The precursor of non-amyloid beta protein component of Alzheimer's disease amyloid (NACP/alpha-synuclein) is aggregated and fibrillated under certain conditions, i.e., increasing time lag, high temperature and low pH. These in vitro aggregates form Thioflavine-S-positive filamentous structures, reminiscent of amyloid-like fibrils. Since some Lewy bodies in Parkinson's disease display Thioflavine-S reactivity, our results may suggest that amyloidogenic properties of NACP/alpha-synuclein may play a crucial role in pathogenesis of disorders with Lewy bodies such as Parkinson's disease.

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