Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease

Nature. 1991 Feb 21;349(6311):704-6. doi: 10.1038/349704a0.

Abstract

A locus segregating with familial Alzheimer's disease (AD) has been mapped to chromosome 21, close to the amyloid precursor protein (APP) gene. Recombinants between the APP gene and the AD locus have been reported which seemed to exclude it as the site of the mutation causing familial AD. But recent genetic analysis of a large number of AD families has demonstrated that the disease is heterogeneous. Families with late-onset AD do not show linkage to chromosome 21 markers. Some families with early-onset AD show linkage to chromosome 21 markers, but some do not. This has led to the suggestion that there is non-allelic genetic heterogeneity even within early onset familial AD. To avoid the problems that heterogeneity poses for genetic analysis, we have examined the cosegregation of AD and markers along the long arm of chromosome 21 in a single family with AD confirmed by autopsy. Here we demonstrate that in this kindred, which shows linkage to chromosome 21 markers, there is a point mutation in the APP gene. This mutation causes an amino-acid substitution (Val----Ile) close to the carboxy terminus of the beta-amyloid peptide. Screening other cases of familial AD revealed a second unrelated family in which this variant occurs. This suggests that some cases of AD could be caused by mutations in the APP gene.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alzheimer Disease / genetics*
  • Amino Acid Sequence
  • Amyloid beta-Peptides / genetics*
  • Amyloid beta-Protein Precursor
  • Base Sequence
  • Chromosomes, Human, Pair 21
  • Exons / genetics
  • Genetic Linkage
  • Genetic Testing
  • Genotype
  • Humans
  • Molecular Sequence Data
  • Mutation
  • Pedigree
  • Polymerase Chain Reaction
  • Polymorphism, Restriction Fragment Length
  • Protein Precursors / genetics*

Substances

  • Amyloid beta-Peptides
  • Amyloid beta-Protein Precursor
  • Protein Precursors