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Decreased cell surface prion protein in mouse models of prion disease

Jennifer K Griffin1, Linda A Terry, Roy Jackman

  • 1Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, Canada.

Neuroreport
|January 30, 2007
PubMed

Insights

Transmissible spongiform encephalopathies (TSEs) reduce cell surface prion protein and Thy-1 levels in mouse brains. This suggests early alterations in prion protein expression or trafficking during TSE disease progression.

Area of Science:

  • Neuroscience
  • Prion Biology
  • Cellular Immunology

Background:

  • Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases.
  • These diseases are caused by prions, which are misfolded prion proteins.
  • Prions form aggregates that damage brain tissue.

Purpose of the Study:

  • To analyze neural antigen density in mouse brains affected by TSEs.
  • To investigate changes in prion protein (PrP), Thy-1, and glial fibrillary acidic protein (GFAP).
  • To understand early molecular events in TSE pathogenesis.

Main Methods:

  • Flow cytometry was used to analyze dissociated mouse brain cells.
  • Mice were inoculated with mouse-adapted TSE agents.
  • Immunoreactivity for PrP, Thy-1, and GFAP was quantified.

Main Results:

  • TSE infection induced gliosis, indicated by increased intracellular GFAP.
  • Cell surface PrP immunoreactivity decreased 2.8-3.8-fold.
  • Surface Thy-1 protein levels decreased 1.5-4-fold.
  • Loss of brain cells expressing high levels of PrP and Thy-1 was observed.

Conclusions:

  • TSEs cause significant reductions in cell surface PrP and Thy-1.
  • Preferential reduction of PrP suggests early disease-related changes.
  • Prion protein expression, trafficking, or consumption may be altered early in TSEs.

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