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Molecular consequences of presenilin-1 mutation

Author

Listed:
  • Sam Gandy

    (Sir James McCusker Alzheimer Research Unit, University of Western Australia
    New York University School of Medicine)

  • Jan Naslund

    (Karolinska Institutet)

  • Christer Nordstedt

    (AstraZeneca)

Abstract

Alzheimer's disease is characterized by accumulation in the brain of a family of insoluble amyloid peptides (Aβ peptides)1, which are produced as a result of the normal processing of β-amyloid precursor protein (β-APP). Russo et al.2 claim that a truncated Aβ peptide that lacks the first ten amino acids accumulates in the brains of patients carrying a mutant form of pre-senilin 1 (PS1), a protein that is involved in cleavage of β-APP. However, we have found that this same species is also overrepresented in Alzheimer's patients with mutations in β-APP itself3. Our findings do not support the conclusion of Russo et al. that pathogenic PS1 mutations may control cleavage of β-APP by β-secretase4,5.

Suggested Citation

  • Sam Gandy & Jan Naslund & Christer Nordstedt, 2001. "Molecular consequences of presenilin-1 mutation," Nature, Nature, vol. 411(6838), pages 654-655, June.
    • Handle: RePEc:nat:nature:v:411:y:2001:i:6838:d:10.1038_35079682
    DOI: 10.1038/35079682
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