Tau pathology in a case of familial Alzheimer's disease with a valine to glycine mutation at position 717 in the amyloid precursor protein

Neurosci Lett. 1992 Oct 12;145(2):178-80. doi: 10.1016/0304-3940(92)90016-z.

Abstract

The brain tissue from a case of familial Alzheimer's disease (FAD) caused by a missense (valine to glycine) mutation at codon 717 of the amyloid precursor protein (APP) gene has been examined for the presence of abnormally phosphorylated paired helical filament tau (PHF-tau). There was abundant PHF-tau present, which on Western blots, was indistinguishable from the PHF-tau typical of cases of sporadic Alzheimer's disease and that of another FAD mutation (valine to isoleucine), previously (Neurosci. Lett., 137 (1992) 221-224). This result implies that the cytoskeletal pathology in Alzheimer's disease is biochemically linked to abnormal APP processing and amyloid deposition.

Publication types

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

MeSH terms

  • Alzheimer Disease / genetics
  • Alzheimer Disease / metabolism*
  • Amyloid beta-Protein Precursor / genetics
  • Amyloid beta-Protein Precursor / metabolism*
  • Antibodies, Monoclonal
  • Blotting, Western
  • Electrophoresis, Polyacrylamide Gel
  • Female
  • Glycine / metabolism*
  • Humans
  • Middle Aged
  • Mutation*
  • Valine / metabolism*
  • tau Proteins / immunology
  • tau Proteins / metabolism*

Substances

  • Amyloid beta-Protein Precursor
  • Antibodies, Monoclonal
  • tau Proteins
  • Valine
  • Glycine