Novel animal model defines genetic contributions for neuron-to-neuron transfer of α-synuclein

Sci Rep. 2017 Aug 8;7(1):7506. doi: 10.1038/s41598-017-07383-6.

Abstract

Cell-to-cell spreading of misfolded α-synuclein (α-syn) is suggested to contribute to the progression of neuropathology in Parkinson's disease (PD). Compelling evidence supports the hypothesis that misfolded α-syn transmits from neuron-to-neuron and seeds aggregation of the protein in the recipient cells. Furthermore, α-syn frequently appears to propagate in the brains of PD patients following a stereotypic pattern consistent with progressive spreading along anatomical pathways. We have generated a C. elegans model that mirrors this progression and allows us to monitor α-syn neuron-to-neuron transmission in a live animal over its lifespan. We found that modulation of autophagy or exo/endocytosis, affects α-syn transfer. Furthermore, we demonstrate that silencing C. elegans orthologs of PD-related genes also increases the accumulation of α-syn. This novel worm model is ideal for screening molecules and genes to identify those that modulate prion-like spreading of α-syn in order to target novel strategies for disease modification in PD and other synucleinopathies.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / antagonists & inhibitors
  • Adenosine Triphosphatases / genetics
  • Adenosine Triphosphatases / metabolism
  • Aldehyde Oxidoreductases / antagonists & inhibitors
  • Aldehyde Oxidoreductases / genetics
  • Aldehyde Oxidoreductases / metabolism
  • Animals
  • Autophagy / drug effects
  • Autophagy / genetics*
  • Brain / drug effects
  • Brain / metabolism
  • Brain / pathology
  • Caenorhabditis elegans / genetics*
  • Caenorhabditis elegans / metabolism
  • Caenorhabditis elegans Proteins / antagonists & inhibitors
  • Caenorhabditis elegans Proteins / genetics
  • Caenorhabditis elegans Proteins / metabolism
  • Cell Communication
  • Discoidin Domain Receptor 2 / genetics
  • Discoidin Domain Receptor 2 / metabolism
  • Disease Models, Animal*
  • Endocytosis / drug effects
  • Exocytosis / drug effects
  • Gene Expression Regulation
  • Genes, Reporter
  • Green Fluorescent Proteins / genetics
  • Green Fluorescent Proteins / metabolism
  • Humans
  • Neurons / drug effects
  • Neurons / metabolism
  • Neurons / pathology
  • Parkinson Disease, Secondary / drug therapy
  • Parkinson Disease, Secondary / genetics*
  • Parkinson Disease, Secondary / metabolism
  • Parkinson Disease, Secondary / pathology
  • Protein Aggregates / drug effects
  • Protein Serine-Threonine Kinases / antagonists & inhibitors
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism
  • Protein Transport / drug effects
  • RNA, Small Interfering / genetics
  • RNA, Small Interfering / metabolism
  • Sirolimus / pharmacology
  • Spectrometry, Fluorescence
  • Tryptophan Hydroxylase / genetics
  • Tryptophan Hydroxylase / metabolism
  • Ubiquitin-Protein Ligases / antagonists & inhibitors
  • Ubiquitin-Protein Ligases / genetics
  • Ubiquitin-Protein Ligases / metabolism
  • alpha-Synuclein / chemistry
  • alpha-Synuclein / genetics
  • alpha-Synuclein / metabolism*

Substances

  • Caenorhabditis elegans Proteins
  • Protein Aggregates
  • RNA, Small Interfering
  • alpha-Synuclein
  • enhanced green fluorescent protein
  • Green Fluorescent Proteins
  • Tryptophan Hydroxylase
  • Aldehyde Oxidoreductases
  • DJR-1.2 protein, C elegans
  • Ubiquitin-Protein Ligases
  • parkin protein
  • Discoidin Domain Receptor 2
  • LRK-1 protein, C elegans
  • Protein Serine-Threonine Kinases
  • Adenosine Triphosphatases
  • CATP-6 protein, C elegans
  • Sirolimus