Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state

Pike, CJ; Burdick, D; Walencewicz, AJ; Glabe, CG; Cotman, CW

doi:10.1523/jneurosci.13-04-01676.1993

Cited by 1,417Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsDementia and Cognitive Impairment Research

Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state

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Pike, CJ, Burdick, D, Walencewicz, AJ, Glabe, CG, Cotman, CW·1993·The Journal of Neuroscience

DOI 10.1523/jneurosci.13-04-01676.1993PMC PMC6576726

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Abstract

The progressive neurodegeneration of Alzheimer's disease has been hypothesized to be mediated, at least in part, by beta-amyloid protein. A relationship between the aggregation state of beta-amyloid protein and its ability to promote degeneration in vitro has been previously suggested. To evaluate this hypothesis and to define a structure- activity relationship for beta-amyloid, aggregation properties of an overlapping series of synthetic beta-amyloid peptides (beta APs) were investigated and compared with beta AP neurotoxic properties in vitro. Using light microscopy, electrophoresis, and ultracentrifugation assays, we found that few beta APs assembled into aggregates immediately after solubilization, but that over time peptides containing the highly hydrophobic beta 29–35 region formed stable aggregations. In short-term neuronal cultures, toxicity was associated specifically with those beta APs that also exhibited significant aggregation. Further, upon the partial reversal of beta 1–42 aggregation, a concomitant loss of toxicity was observed. A synthetic peptide derived from a different amyloidogenic protein, islet amyloid polypeptide, exhibited aggregation but not toxicity, suggesting that beta AP-induced neurotoxicity in vitro is not a nonspecific reaction to aggregated protein. The correlation between beta AP aggregation and neurotoxicity was also observed in long-term neuronal cultures but not in astrocyte cultures. These data are consistent with the hypothesis that beta-amyloid protein contributes to neurodegeneration in Alzheimer's disease.

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Aβ(22-35) rapidly aggregates in aqueous solutions.
“It has the experimental advantage for in vitro studies of rapidly aggregating in aqueous solutions (Pike et al., 1993).”
From The mitochondria-targeted antioxidant MitoQ prevents loss of spatial memory retention and early neuropathology in a transgenic mouse model of Alzheimer’s disease (2011) · cites this paper as Pike et al., 1993
The PAP aggregation section and Table 1 (p. 1687) show that freshly prepared Aβ(25–35) forms visible aggregates in aqueous stock solution. The cited paper reports this for Aβ(25–35), not the claimed Aβ(22–35), so it does not establish that the specified fragment rapidly aggregates. (LLM, conf=0.84)
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“Preparation and treatment of Aβ1‐42 The preparation procedure for Aβ 1-42 (Bachem AG, Switzerland) involved the incubation of fresh solubilized peptides at a concentration of 500 μM in sterile distilled water for a period of 5 days at a temperature of 37 °C [60].”
Method
Primary cilia-mediated regulation of microglial secretion in Alzheimer’s disease
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Authors: Pike, C., Burdick, D., Walencewicz, A., Glabe, C., & Cotman, C.
Affiliations: University of California, Irvine (US)
Venue: The Journal of Neuroscience
Publisher: Society for Neuroscience
Published: 1993-04-01
Volume: 13
Issue: 4
Pages: 1676-1687
ISSN: 0270-6474 (ISSN-L)
1529-2401
DOI: 10.1523/jneurosci.13-04-01676.1993
PMC: PMC6576726
OpenAlex: W1960543132
Cited by: 1,417
References: 7
Citations by year: 2026: 9 · 2025: 11 · 2024: 15 · 2023: 33 · 2022: 15 · 2021: 20 · 2020: 27 · 2019: 24 · 2018: 17 · 2017: 22 · 2016: 28 · 2015: 21 · 2014: 32 · 2013: 32 · 2012: 32
FWCI: 38.25
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-sa
creativecommons.org/licenses/by-nc-sa/4.0/ (vor, 183 d)
Locations: Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute on Aging (R35AG007918, AG07918)
National Institute of Mental Health (MH 14599, T32MH014599)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: amyloid-beta, Alzheimer's disease, neurodegeneration, neurotoxicity, peptide aggregation, structure-activity relationship, amylin, neuronal culture, astrocytes, amyloid fibril formation
MeSH terms: Amino Acid Sequence, Amyloid, Animals, Cells, Cultured, Molecular Sequence Data, Nerve Degeneration, Neurons, Neurotoxins, Peptide Mapping, Structure-Activity Relationship, Time Factors, Amyloid beta-Peptides, Islet Amyloid Polypeptide

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Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state

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