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

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

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Benzothiazoles
  • Humans
  • Hydrogen-Ion Concentration
  • Nerve Tissue Proteins / physiology*
  • Nerve Tissue Proteins / ultrastructure
  • Osmolar Concentration
  • Parkinson Disease / etiology
  • Recombinant Proteins
  • Synucleins
  • Temperature
  • Thiazoles / metabolism
  • Time Factors

Substances

  • Benzothiazoles
  • Nerve Tissue Proteins
  • Recombinant Proteins
  • Synucleins
  • Thiazoles
  • thioflavin T