Amyloidosis: The Key to the Epidemiology and Pathogenesis of Transmissible Spongiform Encephalopathies

  • Heino Diringer
  • Michael Beekes
  • Elizabeth Baldauf
  • Sven Cassens
  • Muhsin Özel
Part of the Serono Symposia USA Norwell, Massachusetts book series (SERONOSYMP)

Abstract

Numerous results have made it very clear that TSEs are pathogenetically closely related to the many nontransmissible amyloidoses (1). These results include the discovery of a disease-specific amyloid fibril (SAF) (2–4), its protein constituent (5–11), and of the gene coding for the amyloid protein precursor (12–18). Further findings provide evidence for the association of familial forms of human TSE (see Chapter 1) and of the susceptibility of sheep breeds to scrapie (19) with specific mutations in the amyloid-coding gene. This gene has been shown to be identical with the sinc gene in mice (20–23) or the sip gene in sheep (24, 25) [some groups prefer to call it the prion gene (20, 21, 23)]. In the absence of this gene, neither amyloidosis, infectivity, nor clinical symptoms develop (27, 28). As the amyloidogenic protein is preferentially located at the surface of neurons (29–31), it becomes clear why these cells are particularly vulnerable to infection and why TSEs present as degenerative diseases of the brain.

Keywords

Codon Dementia Neurol Fibril Sine 

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© Springer-Verlag New York, Inc. 1996

Authors and Affiliations

  • Heino Diringer
  • Michael Beekes
  • Elizabeth Baldauf
  • Sven Cassens
  • Muhsin Özel

There are no affiliations available

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