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Presenilin-1 mutations in Alzheimer's disease

Author

Listed:
  • C. Russo

    (Institute of Pathology, Case Western Reserve University
    National Institute for Cancer Research Advanced Biotechnology Center, Section of Pharmacology University of Genova)

  • G. Schettini

    (National Institute for Cancer Research Advanced Biotechnology Center, Section of Pharmacology University of Genova)

  • T. C. Saido

    (Laboratory for Proteolytic Neuroscience, RIKEN Brain Science Institute)

  • C. Hulette

    (Kathleen Price Bryan Brain Bank and Neuropathology Core, Duke University Medical Center)

  • C. Lippa

    (MCP Hahnemann University)

  • L. Lannfelt

    (Karolinska Institute, Geriatric Laboratory, Huddinge Hospital)

  • B. Ghetti

    (Indiana University Medical Center)

  • P. Gambetti

    (Institute of Pathology, Case Western Reserve University)

  • M. Tabaton

    (Institute of Neurology)

  • J. K. Teller

    (Institute of Pathology, Case Western Reserve University
    East Carolina University)

Abstract

Mutations in the gene encoding the protein presenilin-1 are the most common cause of familial Alzheimer's disease1 and they often produce a different disease course from sporadic Alzheimer's and another familial form associated with mutations in the gene encoding β-amyloid precursor protein2. Here we show that a peculiar form of β-amyloid that is devoid of the first ten amino acids accumulates in the brains of patients carrying presenilin-1 mutations, and is more abundant than in subjects affected by the other types of Alzheimer's.

Suggested Citation

  • C. Russo & G. Schettini & T. C. Saido & C. Hulette & C. Lippa & L. Lannfelt & B. Ghetti & P. Gambetti & M. Tabaton & J. K. Teller, 2000. "Presenilin-1 mutations in Alzheimer's disease," Nature, Nature, vol. 405(6786), pages 531-532, June.
    • Handle: RePEc:nat:nature:v:405:y:2000:i:6786:d:10.1038_35014735
    DOI: 10.1038/35014735
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