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Accumulation of α-synuclein triggered by presynaptic dysfunction.

Yasuto Nakata1, Toru Yasuda, Masahiro Fukaya

  • 1Department of Neurology, Division of Neuroregenerative Medicine, Kitasato University School of Medicine, Sagamihara, Kanagawa 252-0374, Japan.

The Journal of Neuroscience : the Official Journal of the Society for Neuroscience
|December 1, 2012
PubMed
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SNARE complex dysfunction, not alpha-synuclein (αSyn) itself, may initiate Lewy body diseases. This study in Snap25 mutant mice shows SNARE dysfunction triggers αSyn mislocalization and accumulation, suggesting a key role in α-synucleinopathies.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Pathology

Background:

  • Abnormal alpha-synuclein (αSyn) aggregates are hallmarks of dementia with Lewy bodies and Parkinson's disease.
  • αSyn interacts with the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex, crucial for neurotransmission.
  • Previous studies noted altered SNARE protein distribution in αSyn-related neurodegenerative diseases.

Purpose of the Study:

  • To investigate the impact of SNARE complex dysfunction on endogenous αSyn.
  • To explore the role of synaptosomal-associated protein of 25 kDa (SNAP-25) phosphorylation in αSyn pathology.
  • To determine if SNARE dysfunction is an initiating factor in α-synucleinopathies.

Main Methods:

  • Utilized Snap25(S187A/S187A) mutant mice with unphosphorylatable SNAP-25.
  • Performed age-dependent analysis of αSyn and phosphorylated αSyn distribution.
  • Employed electron microscopy to examine synaptic vesicle morphology and protein localization in glutamatergic nerve terminals.

Main Results:

  • Snap25(S187A/S187A) mice exhibited age-dependent αSyn mislocalization and accumulation in hypertrophied glutamatergic terminals.
  • Electron microscopy revealed condensed synaptic vesicles and αSyn in the periactive zone.
  • No abnormalities were observed in the nigrostriatal dopaminergic system of these mutant mice.

Conclusions:

  • SNARE complex dysfunction, specifically altered SNAP-25, appears to be an initial trigger for αSyn mislocalization and aggregation.
  • This dysfunction may represent a critical pathomechanism in the development of α-synucleinopathies.
  • Findings implicate SNARE complex integrity as a potential therapeutic target.