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The vicious cycle between α-synuclein aggregation and autophagic-lysosomal dysfunction.

Giovanni Bellomo1, Silvia Paciotti2,3, Leonardo Gatticchi3

  • 1Magnetic Resonance Center (CERM), University of Florence, Sesto Fiorentino, (FI), Italy.

Movement Disorders : Official Journal of the Movement Disorder Society
|November 16, 2019
PubMed
Summary

Misfolded alpha-synuclein (α-syn) aggregation is central to Parkinson's disease (PD). This review explores how impaired autophagic-lysosomal pathways worsen α-syn pathology, suggesting therapeutic targets for PD treatment.

Keywords:
GCaseParkinson's diseasealpha-synucleinautophagycathepsin-Dlysosome

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Genetics

Background:

  • Alpha-synuclein (α-syn) misfolding and aggregation are key pathological features of Parkinson's disease (PD).
  • Cellular protein degradation systems, particularly the autophagic-lysosomal pathway, are crucial for clearing misfolded proteins like α-syn.
  • Genetic studies have linked PD to genes involved in the autophagic-lysosomal pathway, highlighting its role in disease pathogenesis.

Purpose of the Study:

  • To review the evidence and mechanisms underlying the reciprocal relationship between autophagic-lysosomal pathway impairment and α-syn aggregation in PD.
  • To identify potential therapeutic strategies targeting the autophagic-lysosomal pathway for PD treatment.

Main Methods:

  • Literature review of studies investigating α-syn pathology and the autophagic-lysosomal pathway in PD.
  • Analysis of genetic associations and biochemical evidence linking lysosomal dysfunction to α-syn accumulation.
  • Examination of preclinical and clinical data on compounds aimed at restoring autophagic-lysosomal function.

Main Results:

  • Dysfunction of the autophagic-lysosomal pathway is implicated in both genetic and sporadic forms of PD.
  • Decreased lysosomal enzyme activity correlates with α-syn accumulation in specific brain regions, suggesting a direct link.
  • Evidence supports a crosstalk between α-syn aggregation and autophagic-lysosomal impairment, potentially driving disease progression.

Conclusions:

  • Impaired autophagic-lysosomal pathway function exacerbates α-syn aggregation and propagation in Parkinson's disease.
  • Restoring autophagic-lysosomal pathway function represents a promising disease-modifying therapeutic strategy for PD.
  • Further research into this pathway could unveil novel treatments for synucleinopathies.