Elsevier

Brain Research

Volume 799, Issue 2, 20 July 1998, Pages 301-306
Brain Research

Short communication
Human recombinant NACP/α-synuclein is aggregated and fibrillated in vitro: Relevance for Lewy body disease

https://doi.org/10.1016/S0006-8993(98)00514-9Get rights and content

Abstract

The precursor of non-amyloid β protein component of Alzheimer's disease amyloid (NACP/α-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/α-synuclein may play a crucial role in pathogenesis of disorders with Lewy bodies such as Parkinson's disease.

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Acknowledgements

This work was supported by NIH Grants (AG05131 and AG10689) and the Yamanouchi Pharmaceutical. We thank Drs. Leon Thal, Robert Katzman, and Makoto Yoshimoto for their continuous encouragement.

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