A prion disease with a novel 96-base pair insertional mutation in the prion protein gene

Neurology. 1996 Mar;46(3):761-6. doi: 10.1212/wnl.46.3.761.

Abstract

There are coding mutations in the prion protein gene in familial Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler-Scheinker disease, and other phenotypes that make up the inherited prion diseases. Insertional mutations consisting of two, five, six, seven, eight, and nine additional octapeptide repeat elements are seen in the inherited prion diseases and usually present as atypical dementias with considerable intrafamilial phenotypic variability. A four-octarepeat insertion was reported previously in an individual without neurodegenerative disease who died of hepatic cirrhosis. Here we report a novel four-octarepeat insertional mutation in a case with classical clinical, electroencephalographic and histopathologic features of CJD with the unusual finding of pronounced prion protein immunoreactivity of the molecular layer of the cerebellum.

Publication types

  • Case Reports
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Composition
  • Base Sequence
  • Brain / pathology
  • DNA / genetics
  • DNA Transposable Elements*
  • Humans
  • Male
  • Middle Aged
  • Molecular Probes / genetics
  • Molecular Sequence Data
  • Mutation*
  • Prion Diseases / genetics*
  • Prion Diseases / pathology
  • Prions / genetics*

Substances

  • DNA Transposable Elements
  • Molecular Probes
  • Prions
  • DNA