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.

Section snippets

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.

References (29)

  • J Kim

    Evidence that the precursor protein of non-Ab component of Alzheimer's disease amyloid (NACP) has an extended structure primarily composed of random-coil

    Mol. Cells

    (1997)
  • L Maroteaux et al.

    The rat brain synucleins; family of proteins transiently associated with neuronal membrane

    Mol. Brain Res.

    (1991)
  • G.S Withers et al.

    Delayed localization of synelfin (synucleinm NACP) to presynaptic terminals in cultured rat hippocampal neurons

    Dev. Brain Res.

    (1997)
  • M Baba et al.

    Aggregation of α-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies

    Am. J. Pathol.

    (1998)
  • Cited by (253)

    • Towards a biological diagnosis of PD

      2024, Parkinsonism and Related Disorders
    • An α-synuclein decoy peptide prevents cytotoxic α-synuclein aggregation caused by fatty acid binding protein 3

      2021, Journal of Biological Chemistry
      Citation Excerpt :

      These results demonstrated that the formation of the αSyn–FABP3 complex in cells results in an increase in cytotoxicity that is sensitive to perturbations that focus on the C-terminal region of αSyn. The deposition of Lewy bodies, composed of αSyn aggregates, in neurons is considered to be an important event in the progression of PD (44–46). Many studies have demonstrated that a multitude of cellular factors contribute to this intracellular deposition of αSyn (47, 48).

    View all citing articles on Scopus
    View full text