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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
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Prion-like disorders: blurring the divide between transmissibility and infectivity

Mimi Cushman1, Brian S Johnson, Oliver D King

  • 1Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, 805b Stellar-Chance Laboratories, 422 Curie Boulevard, Philadelphia, PA 19104, USA.

Journal of Cell Science
|April 2, 2010
PubMed

Insights

Prions and similar self-templating proteins can spread, causing neurodegenerative diseases like Alzheimer's and Parkinson's. This transmissibility necessitates caution with new cell-based therapies to prevent disease spread.

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Protein Chemistry

Background:

  • Prions are self-templating proteins causing transmissible diseases.
  • Amyloid formation is not exclusive to prions and is linked to neurodegenerative disorders.
  • Proteins like FUS and TDP-43, implicated in neurodegenerative diseases, share prion-like domains.

Purpose of the Study:

  • To review advances in understanding the transmissibility of amyloid forms associated with neurodegenerative diseases.
  • To explore the potential 'infectious' nature of proteins linked to Alzheimer's, Parkinson's, and Huntington's diseases.
  • To reassess the safety and optimization of neuronal graft and stem-cell therapies in light of protein transmissibility.

Main Methods:

  • Review of current scientific literature on prion diseases and protein misfolding.
  • Analysis of studies demonstrating cell-to-cell spread of amyloid conformers in neurodegenerative conditions.
  • Evaluation of the implications of protein transmissibility for therapeutic strategies.

Main Results:

  • Amyloid conformers associated with Alzheimer's, Parkinson's, and Huntington's diseases can spread from cell to cell.
  • This cell-to-cell spread contributes to the progression of distinct neurodegenerative phenotypes.
  • The findings highlight the 'infectious' potential of misfolded proteins in the brain.

Conclusions:

  • The transmissibility of amyloid conformers necessitates a re-evaluation of neuronal graft and stem-cell therapies.
  • Strategies must be developed to mitigate the risk of transmitting these neurodegenerative agents through therapies.
  • Optimizing treatments to overcome transmissible conformers is crucial for patient safety and therapeutic efficacy.

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