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Human prion diseases

S B Prusiner1, K K Hsiao

  • 1Department of Neurology, University of California, San Francisco 94143-0518.

Annals of Neurology
|April 1, 1994
PubMed
Summary

Prion diseases, or transmissible spongiform encephalopathies, involve abnormal prion protein (PrP) metabolism. This process includes conformational changes and is linked to PrP gene mutations in inherited forms, affecting both humans and animals.

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Area of Science:

  • Neuroscience
  • Protein biochemistry
  • Genetics

Background:

  • Prion diseases, including Creutzfeldt-Jakob disease and bovine spongiform encephalopathy, were historically misattributed to viral causes.
  • These disorders affect both humans and animals, manifesting in sporadic, inherited, and infectious forms.

Purpose of the Study:

  • To elucidate the central role of prion protein (PrP) in the pathogenesis of transmissible spongiform encephalopathies.
  • To highlight the aberrant metabolism and conformational changes of PrP as a common characteristic across diverse prion diseases.

Main Methods:

  • Analysis of the molecular mechanisms underlying prion protein (PrP) misfolding and conversion.
  • Examination of genetic linkage between PrP gene mutations and inherited prion diseases.
  • Review of transmissibility studies in experimental animal models.

Main Results:

  • Identified aberrant prion protein (PrP) metabolism as the unifying feature of all prion diseases.
  • Demonstrated that the cellular PrP is converted to a pathogenic scrapie isoform via posttranslational conformational changes.
  • Confirmed transmissibility of human prion diseases to animals and segregation of inherited forms with PrP gene mutations.

Conclusions:

  • Prion diseases are fundamentally disorders of prion protein (PrP) metabolism and conformation.
  • Understanding PrP's aberrant processing is crucial for diagnosing and potentially treating these neurodegenerative conditions.
  • Genetic factors, specifically PrP gene mutations, play a significant role in the etiology of inherited prion diseases.

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