Alzheimer's-associated Aβ oligomers show altered structure, immunoreactivity and synaptotoxicity with low doses of oleocanthal

Pitt, Jason; Roth, William; Lacor, Pascale; Smith, Amos B.; Blankenship, Matthew; Velasco, Pauline; De Felice, Fernanda; Breslin, Paul; Klein, William L.

doi:10.1016/j.taap.2009.07.018

Cited by 134Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsDementia and Cognitive Impairment Research

Alzheimer's-associated Aβ oligomers show altered structure, immunoreactivity and synaptotoxicity with low doses of oleocanthal

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Pitt, Jason, Roth, William, Lacor, Pascale, Smith, Amos B., Blankenship, Matthew, Velasco, Pauline, De Felice, Fernanda, Breslin, Paul +1 more·2009·Toxicology and Applied Pharmacology

DOI 10.1016/j.taap.2009.07.018PMC PMC2808212

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Abstract

It now appears likely that soluble oligomers of amyloid-beta1-42 peptide, rather than insoluble fibrils, act as the primary neurotoxin in Alzheimer's disease (AD). Consequently, compounds capable of altering the assembly state of these oligomers (referred to as ADDLs) may have potential for AD therapeutics. Phenolic compounds are of particular interest for their ability to disrupt Abeta oligomerization and reduce pathogenicity. This study has focused on oleocanthal (OC), a naturally-occurring phenolic compound found in extra-virgin olive oil. OC increased the immunoreactivity of soluble Abeta species, when assayed with both sequence- and conformation-specific Abeta antibodies, indicating changes in oligomer structure. Analysis of oligomers in the presence of OC showed an upward shift in MW and a ladder-like distribution of SDS-stable ADDL subspecies. In comparison with control ADDLs, oligomers formed in the presence of OC (Abeta-OC) showed equivalent colocalization at synapses but exhibited greater immunofluorescence as a result of increased antibody recognition. The enhanced signal at synapses was not due to increased synaptic binding, as direct detection of fluorescently-labeled ADDLs showed an overall reduction in ADDL signal in the presence of OC. Decreased binding to synapses was accompanied by significantly less synaptic deterioration assayed by drebrin loss. Additionally, treatment with OC improved antibody clearance of ADDLs. These results indicate oleocanthal is capable of altering the oligomerization state of ADDLs while protecting neurons from the synaptopathological effects of ADDLs and suggest OC as a lead compound for development in AD therapeutics.

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Not all Aβ oligomers are toxic, even those of a given size; subtle conformation changes affect toxicity and immunoreactivity.
“And in fact, not all oligomers are toxic, even those oligomers of a given size. Subtle conformation changes affect toxicity and immunoreactivity (Chromy et al., 2003; Pitt et al., 2009).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Pitt et al., 2009

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Authors: Pitt, J., Roth, W., Lacor, P., Smith, A. B., Blankenship, M., Velasco, P., De Felice, F., Breslin, P., & Klein, W. L.
Affiliations: Northwestern University (US)
Monell Chemical Senses Center (US)
Western Illinois University (US)
Rutgers, The State University of New Jersey (US)
Corresponding author: Pitt, Jason
Breslin, Paul
Klein, William L.
ORCID: Pitt, Jason
Smith, Amos B.
Breslin, Paul
Klein, William L.
Venue: Toxicology and Applied Pharmacology
Publisher: Elsevier BV
Published: 2009-10
Volume: 240
Issue: 2
Pages: 189-197
ISSN: 0041-008X (ISSN-L)
DOI: 10.1016/j.taap.2009.07.018
PMC: PMC2808212
OpenAlex: W2025825556
Cited by: 134
References: 53
Citations by year: 2026: 1 · 2025: 4 · 2024: 3 · 2023: 2 · 2022: 5 · 2021: 10 · 2020: 5 · 2019: 11 · 2018: 12 · 2017: 13 · 2016: 9 · 2015: 10 · 2014: 5 · 2013: 15 · 2012: 17
FWCI: 6.41
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Toxicology and Applied Pharmacology (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Rutgers University Community Repository (Rutgers University) (submittedVersion)
Funders: National Institutes of Health (5p50dc006760-05, 5t32ag020418-08)
National Institute on Aging (5 T32 AG020418, R01AG022547, R01AG029460, T32-AG020418)
National Institute on Deafness and Other Communication Disorders (P50 DC06760, P50-DC006760)
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: Alzheimer's disease, amyloid-beta oligomers, oleocanthal, extra virgin olive oil, phenolic compounds, synaptotoxicity, oligomerization, immunoreactivity, drebrin, antibody clearance, neuroprotection, Alzheimer's disease therapeutics
MeSH terms: Cyclopentane Monoterpenes, Aldehydes, Animals, Antibodies, Antigen-Antibody Reactions, Cells, Cultured, Dose-Response Relationship, Drug, Electrophoresis, Polyacrylamide Gel, Fluorescent Antibody Technique, Hippocampus, Humans, Molecular Weight, Neuropeptides, Peptide Fragments, Phenols, Protein Conformation, Synapses, Immunoblotting, Amyloid beta-Peptides, Microscopy, Confocal, Neuroprotective Agents, Protein Multimerization

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Alzheimer's-associated Aβ oligomers show altered structure, immunoreactivity and synaptotoxicity with low doses of oleocanthal

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