Cited by 1,452Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

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Oligomeric and Fibrillar Species of Amyloid-β Peptides Differentially Affect Neuronal Viability

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Dahlgren, Karie N., Manelli, Arlene M., Stine, W. Blaine, Baker, Lorinda K., Krafft, Grant A., LaDu, Mary Jo·2002·Journal of Biological Chemistry

DOI 10.1074/jbc.m201750200

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Abstract

Genetic evidence predicts a causative role for amyloid-beta (A beta) in Alzheimer's disease. Recent debate has focused on whether fibrils (amyloid) or soluble oligomers of A beta are the active species that contribute to neurodegeneration and dementia. We developed two aggregation protocols for the consistent production of stable oligomeric or fibrillar preparations of A beta-(1-42). Here we report that oligomers inhibit neuronal viability 10-fold more than fibrils and approximately 40-fold more than unaggregated peptide, with oligomeric A beta-(1-42)-induced inhibition significant at 10 nm. Under A beta-(1-42) oligomer- and fibril-forming conditions, A beta-(1-40) remains predominantly as unassembled monomer and had significantly less effect on neuronal viability than preparations of A beta-(1-42). We applied the aggregation protocols developed for wild type A beta-(1-42) to A beta-(1-42) with the Dutch (E22Q) or Arctic (E22G) mutations. Oligomeric preparations of the mutations exhibited extensive protofibril and fibril formation, respectively, but were not consistently different from wild type A beta-(1-42) in terms of inhibition of neuronal viability. However, fibrillar preparations of the mutants appeared larger and induced significantly more inhibition of neuronal viability than wild type A beta-(1-42) fibril preparations. These data demonstrate that protocols developed to produce oligomeric and fibrillar A beta-(1-42) are useful in distinguishing the structural and functional differences between A beta-(1-42) and A beta-(1-40) and genetic mutations of A beta-(1-42).

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Authors: Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., & LaDu, M. J.
Affiliations: Northwestern University (US)
Corresponding author: LaDu, Mary Jo
ORCID: Baker, Lorinda K.
LaDu, Mary Jo
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2002-08
Volume: 277
Issue: 35
Pages: 32046-32053
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m201750200
OpenAlex: W2168025729
Cited by: 1,452
References: 71
Citations by year: 2026: 25 · 2025: 33 · 2024: 40 · 2023: 46 · 2022: 45 · 2021: 47 · 2020: 49 · 2019: 55 · 2018: 65 · 2017: 58 · 2016: 61 · 2015: 70 · 2014: 78 · 2013: 86 · 2012: 86
FWCI: 22.78
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 6658 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
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: amyloid-beta, amyloid-beta oligomers, amyloid fibrils, Alzheimer's disease, neuronal viability, peptide aggregation, protofibrils, neurotoxicity
MeSH terms: Alzheimer Disease, Cell Survival, Humans, Neuroblastoma, Neurons, Peptide Fragments, Tumor Cells, Cultured, Amyloid beta-Peptides, Microscopy, Atomic Force

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Oligomeric and Fibrillar Species of Amyloid-β Peptides Differentially Affect Neuronal Viability

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