Altered cleavage and secretion of a recombinant β–APP bearing the Swedish familial Alzheimer's disease mutation

Felsenstein, Kevin M.; Hunihan, Lisa W.; Roberts, Susan B.

doi:10.1038/ng0394-251

Cited by 90Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

Altered cleavage and secretion of a recombinant β–APP bearing the Swedish familial Alzheimer's disease mutation

Felsenstein, Kevin M., Hunihan, Lisa W., Roberts, Susan B.·1994·Nature Genetics

DOI 10.1038/ng0394-251

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Abstract

Mutations within the beta-amyloid precursor protein gene cosegregate with the early-onset form of familial Alzheimer's Disease (FAD). It is not known how these mutations result in disease; however, one early-onset AD mutation in a Swedish kindred increases potentially amyloidogenic fragments and beta-protein production in cells expressing the mutant beta-APP. Using a novel recombinant reporter system we found a qualitative change in the secreted product, from cleavage within the beta-protein sequence to cleavage near the N-terminal region of the beta-protein, even though the total amount of secreted mutant product is similar to wild-type. The results suggest that the increased formation of potentially amyloidogenic fragments in cells expressing the Swedish FAD occurs by enzymatic cleavage in the secretory pathway. Alterations in the secretory process may predispose an individual to AD.

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APP and CTFβ are much more abundant than Aβ inside cells, especially in FAD mutant mice such as 5xFAD mice expressing the Swedish mutation, which triggers β-cleavage of APP.
“Both APP and CTFβ are much more abundant than Aβ inside the cells [36], especially in FAD mutant mice (such as 5xFAD mice) expressing the Swedish mutation, which is known to trigger the β-cleavage of APP [31].”
From Senescence-related impairment of autophagy induces toxic intraneuronal amyloid-β accumulation in a mouse model of amyloid pathology (2023) · cites this paper as [31]

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Authors: Felsenstein, K. M., Hunihan, L. W., & Roberts, S. B.
Affiliations: Bristol-Myers Squibb (United States) (US)
Venue: Nature Genetics
Publisher: Springer Science and Business Media LLC
Published: 1994-03
Volume: 6
Issue: 3
Pages: 251-256
ISSN: 1061-4036 (ISSN-L)
1546-1718
DOI: 10.1038/ng0394-251
OpenAlex: W2053060747
Cited by: 90
References: 36
Citations by year: 2024: 1 · 2023: 1 · 2021: 2 · 2020: 1 · 2019: 3 · 2017: 1 · 2016: 2 · 2015: 2 · 2013: 1 · 2012: 5
FWCI: 9.05
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Genetics (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Physiology › 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: amyloid precursor protein, Swedish mutation, familial Alzheimer's disease, early-onset Alzheimer's disease, APP cleavage, secretory pathway, protein secretion, APP gene mutations
MeSH terms: Alzheimer Disease, Cell Line, Cloning, Molecular, Glycosylation, Humans, Mutation, Protein Processing, Post-Translational, Recombinant Fusion Proteins, Sweden, Transfection, Amyloid beta-Protein Precursor, Genes, Reporter

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Altered cleavage and secretion of a recombinant β–APP bearing the Swedish familial Alzheimer's disease mutation

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