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Synaptic dysfunction in prion diseases: a trafficking problem?

Assunta Senatore1, Elena Restelli1, Roberto Chiesa1

  • 1Dulbecco Telethon Institute and Department of Neuroscience, IRCCS-Istituto di Ricerche Farmacologiche "Mario Negri," Via G. La Masa 19, 20156 Milano, Italy.

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Summary
This summary is machine-generated.

Misfolded prion protein (PrP(C)) accumulation in the endoplasmic reticulum causes synaptic dysfunction in prion diseases, not through unfolded protein response, but by impairing calcium channel trafficking and affecting PrP(C)-interacting proteins.

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Area of Science:

  • Neurodegenerative diseases
  • Prion diseases
  • Cellular biology

Background:

  • Synaptic dysfunction is a key feature of prion diseases.
  • Misfolded cellular prion protein (PrP(C)) accumulation in the endoplasmic reticulum (ER) is implicated in synaptic failure.
  • The unfolded protein response (UPR) pathway has been investigated as a potential mechanism.

Purpose of the Study:

  • To investigate the role of the UPR translational repression pathway in genetic prion disease models.
  • To explore the mechanism by which ER-retained PrP(C) contributes to synaptic dysfunction.
  • To propose a model for prion disease pathogenicity.

Main Methods:

  • Analysis of mouse models of genetic prion disease.
  • Investigation of the unfolded protein response pathway.
  • Assessment of endoplasmic reticulum stress markers.
  • Evaluation of secretory trafficking of calcium channels.

Main Results:

  • The UPR translational repression pathway is not active in mouse models of genetic prion disease.
  • Endoplasmic reticulum (ER) stress is not involved in the observed synaptic dysfunction.
  • ER retention of mutant PrP(C) impairs the trafficking of essential calcium channels.
  • A model of pathogenicity involving intracellular PrP(C) retention is proposed.

Conclusions:

  • The pathogenesis of prion diseases does not involve the UPR translational repression pathway.
  • Intracellular retention of misfolded PrP(C) leads to synaptic dysfunction by disrupting calcium channel trafficking.
  • This mechanism, involving loss of function or gain of toxicity of PrP(C)-interacting proteins, may explain the diverse clinical presentations of prion diseases.