Release of Excess Amyloid β Protein from a Mutant Amyloid β Protein Precursor

Cai, Xiao-Dan; Golde, Todd E.; Younkin, Steven G.

doi:10.1126/science.8424174

Cited by 913Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

Release of Excess Amyloid β Protein from a Mutant Amyloid β Protein Precursor

Cai, Xiao-Dan, Golde, Todd E., Younkin, Steven G.·1993·Science

DOI 10.1126/science.8424174

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Abstract

The 4-kilodalton amyloid beta protein (A beta), which forms fibrillar deposits in Alzheimer's disease (AD), is derived from a large protein referred to as the amyloid beta protein precursor (beta APP). Human neuroblastoma (M17) cells transfected with constructs expressing wild-type beta APP or a mutant, beta APP delta NL, recently linked to familial AD were compared. After continuous metabolic labeling for 8 hours, cells expressing beta APP delta NL had five times more of an A beta-bearing, carboxyl terminal, beta APP derivative than cells expressing wild-type beta APP and they released six times more A beta into the medium. Thus this mutant beta APP may cause AD because its processing is altered in a way that releases increased amounts of A beta.

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“It is well established that this mutation causes concomitant increases in secreted A␤42 and A␤40 (Cai et al., 1993;Citron et al., 1994;Scheuner et al., 1996).”
From Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease (2001) · cites this paper as Cai et al., 1993
Secreted Aβ is readily detected in CSF, plasma, and medium conditioned by a wide variety of cultured cells.
“Secreted A␤ is readily detected in CSF, plasma, and in medium conditioned by a wide variety of cultured cells”
From Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease (2001) · cites this paper as Cai et al., 1993

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Authors: Cai, X.-D., Golde, T. E., & Younkin, S. G.
Affiliations: Case Western Reserve University (US)
ORCID: Golde, Todd E.
Younkin, Steven G.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1993-01-22
Volume: 259
Issue: 5094
Pages: 514-516
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.8424174
OpenAlex: W1969810313
Cited by: 913
References: 7
Citations by year: 2026: 2 · 2025: 4 · 2024: 9 · 2023: 9 · 2022: 13 · 2021: 11 · 2020: 9 · 2019: 16 · 2018: 8 · 2017: 13 · 2016: 14 · 2015: 10 · 2014: 17 · 2013: 15 · 2012: 22
FWCI: 63.85
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute on Aging (AG06656, R01AG006656)
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-beta, amyloid precursor protein, Alzheimer's disease, familial Alzheimer's disease, neuroblastoma cells, protein processing
MeSH terms: Alzheimer Disease, Amino Acid Sequence, Base Sequence, Cloning, Molecular, Humans, Molecular Sequence Data, Neuroblastoma, Oligodeoxyribonucleotides, Transfection, Tumor Cells, Cultured, Polymerase Chain Reaction, Amyloid beta-Peptides, Mutagenesis, Site-Directed, Amyloid beta-Protein Precursor

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Release of Excess Amyloid β Protein from a Mutant Amyloid β Protein Precursor

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