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.
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Gandy, S., Naslund, J. & Nordstedt, C. Molecular consequences of presenilin-1 mutation. Nature 411, 654–655 (2001). https://doi.org/10.1038/35079682
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DOI: https://doi.org/10.1038/35079682
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