Cited by 1,757Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

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Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production

Citron, Martin, Oltersdorf, Tilman, Haass, Christian, McConlogue, Lisa, Hung, Albert Y., Seubert, Peter, Vigo-Pelfrey, Carmen, Lieberburg, Ivan, Selkoe, Dennis J.·1992·Nature

DOI 10.1038/360672a0

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Abstract

Progressive cerebral deposition of the 39-43-amino-acid amyloid beta-protein (A beta) is an invariant feature of Alzheimer's disease which precedes symptoms of dementia by years or decades. The only specific molecular defects that cause Alzheimer's disease which have been identified so far are missense mutations in the gene encoding the beta-amyloid precursor protein (beta-APP) in certain families with an autosomal dominant form of the disease (familial Alzheimer's disease, or FAD). These mutations are located within or immediately flanking the A beta region of beta-APP, but the mechanism by which they cause the pathological phenotype of early and accelerated A beta deposition is unknown. Here we report that cultured cells which express a beta-APP complementary DNA bearing a double mutation (Lys to Asn at residue 595 plus Met to Leu at position 596) found in a Swedish FAD family produce approximately 6-8-fold more A beta than cells expressing normal beta-APP. The Met 596 to Leu mutation is principally responsible for the increase. These data establish a direct link between a FAD genotype and the clinicopathological phenotype. Further, they confirm the relevance of the continuous A beta production by cultured cells for elucidating the fundamental mechanism of Alzheimer's disease.

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Authors: Citron, M., Oltersdorf, T., Haass, C., McConlogue, L., Hung, A. Y., Seubert, P., Vigo-Pelfrey, C., Lieberburg, I., & Selkoe, D. J.
Affiliations: Brigham and Women's Hospital (US)
ORCID: Citron, Martin
Haass, Christian
McConlogue, Lisa
Hung, Albert Y.
Selkoe, Dennis J.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1992-12
Volume: 360
Issue: 6405
Pages: 672-674
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/360672a0
OpenAlex: W2090150925
Cited by: 1,757
References: 17
Citations by year: 2026: 19 · 2025: 19 · 2024: 28 · 2023: 24 · 2022: 33 · 2021: 39 · 2020: 37 · 2019: 43 · 2018: 41 · 2017: 39 · 2016: 50 · 2015: 37 · 2014: 59 · 2013: 45 · 2012: 59
FWCI: 52.80
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: familial Alzheimer's disease, amyloid precursor protein, APP mutations, genotype-phenotype correlation, amyloid deposition, cultured cells, autosomal dominant inheritance
MeSH terms: Alzheimer Disease, Amino Acid Sequence, Base Sequence, Cell Line, Humans, Kidney, Molecular Sequence Data, Mutation, Oligodeoxyribonucleotides, Sweden, Transfection, Restriction Mapping, Amyloid beta-Peptides, Amyloid beta-Protein Precursor

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Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production

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