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Related Experiment Videos

Nonneuronal cellular prion protein.

J G Fournier1

  • 1Service de Neurovirologie, CEA-DSV/DRM, Fontenay aux Roses, France.

International Review of Cytology
|August 21, 2001
PubMed
Summary
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The normal cellular prion protein (PrP(c)) can change into a disease-causing form (PrP(sc)) outside the brain. Understanding PrP(c) in nonneuronal cells may reveal its function and prion disease mechanisms.

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Pathology

Background:

  • The normal cellular prion protein (PrP(c)) is a sialoglycoprotein with an unknown function.
  • PrP(c) can misfold into a pathological form (PrP(sc)), the agent of transmissible spongiform encephalopathies (prion diseases).
  • Prion diseases affect both animals (scrapie, BSE) and humans (Creutzfeldt-Jakob disease).

Purpose of the Study:

  • To evaluate data on PrP(c)-expressing nonneuronal cells in various tissues.
  • To understand the biological function of PrP(c).
  • To gain insights into the physiopathological processes of prion diseases.

Main Methods:

  • Review of existing scientific literature and data.
  • Analysis of the tissue, cellular, and subcellular localization of PrP(c).

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Main Results:

  • PrP(c) to PrP(sc) conversion occurs in the brain, influencing disease phenotype.
  • PrP(c) misfolding can also happen in nonneuronal cells, particularly in lymphoid tissue where the prion agent replicates.
  • PrP(c) in nonneuronal cells of peripheral organs may act as a receptor for prion agent entry.

Conclusions:

  • PrP(c) is present in nonneuronal cells in both cerebral and extracerebral tissues.
  • Understanding the localization of PrP(c) is crucial for elucidating its biological role.
  • Further analysis of PrP(c) localization may illuminate the mechanisms underlying prion diseases.