Clusterin (apoJ) Alters the Aggregation of Amyloid β-Peptide (Aβ1-42) and Forms Slowly Sedimenting Aβ Complexes That Cause Oxidative Stress

Oda, Tomiichiro; Wals, Pat; Osterburg, Heinz H.; Johnson, Steven A.; Pasinetti, Giulio M.; Morgan, Todd E.; Rozovsky, Irina; Stine, W.Blaine; Snyder, Seth W.; Holzman, Thomas F.; Krafft, Grant A.; Finch, Caleb E.

doi:10.1006/exnr.1995.1080

Cited by 352Alzheimer's disease research and treatmentsClusterin in disease pathologyDementia and Cognitive Impairment Research

Clusterin (apoJ) Alters the Aggregation of Amyloid β-Peptide (Aβ1-42) and Forms Slowly Sedimenting Aβ Complexes That Cause Oxidative Stress

Oda, Tomiichiro, Wals, Pat, Osterburg, Heinz H., Johnson, Steven A., Pasinetti, Giulio M., Morgan, Todd E., Rozovsky, Irina, Stine, W.Blaine +4 more·1995·Experimental Neurology

DOI 10.1006/exnr.1995.1080

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Abstract

Clusterin (apoJ), a multifunctional apolipoprotein made by cells in the brain and many other locations, is associated with aggregated amyloid beta-peptide (A beta) in senile and diffuse plaques of Alzheimer's disease (AD). We observed that purified human serum clusterin partially blocked the aggregation of synthetic A beta 1-42, as shown by centrifugal assays (14,000g x 10 min) and by atomic force (scanning probe) microscopy. Slowly sedimenting A beta complexes were formed in the presence of clusterin, which included aggregates > 200 kDa that resist dissociation by low concentrations of SDS. Clusterin enhanced the oxidative stress caused by A beta, as assayed by oxidative stress in PC12 cells with MTT, which is widely used to estimate neurotoxicity. These indications of enhanced neurotoxicity by the MTT assay were observed in the highly aggregated rapidly sedimenting fraction, but also in more slowly sedimenting "soluble" forms. This novel activity of slowly sedimenting A beta may enhance the neurotoxicity of A beta deposits in AD brains, because soluble complexes have a potential for diffusing to damage distal neurons.

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Oligomeric Aβ rather than fibril Aβ is regarded as the toxic species of this peptide.
“oligomeric Aβ rather than fibril Aβ is regarded as the toxic species of this peptide [143,144,145,146].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [143]
APOE and CLU cooperate in suppressing Aβ deposition and may modify Aβ clearance at the blood-brain barrier.
“Furthermore, APOE and CLU have been shown to cooperate in suppressing Aβ deposition 33 and APOE and CLU may critically modify Aβ clearance at the blood brain barrier”
From Genome-wide association study identifies variants at CLU and PICALM associated with Alzheimer's disease (2009) · cites this paper as [33]
Clusterin levels appear to influence amyloid-beta aggregation.
“CLU levels also appear to affect aggregation of Aβ (Oda, et al., 1995,Wilson, et al., 2008)”
From A potential endophenotype for Alzheimer's disease: cerebrospinal fluid clusterin (2016) · cites this paper as Oda, et al., 1995

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Untitled work
Cole (2000) · doi:10.1002/1097-0029(20000815)50:4

Authors: Oda, T., Wals, P., Osterburg, H. H., Johnson, S. A., Pasinetti, G. M., Morgan, T. E., Rozovsky, I., Stine, W. B., Snyder, S. W., Holzman, T. F., Krafft, G. A., & Finch, C. E.
Affiliations: Northwestern University (US)
ORCID: Pasinetti, Giulio M.
Morgan, Todd E.
Snyder, Seth W.
Venue: Experimental Neurology
Publisher: Elsevier BV
Published: 1995-11
Volume: 136
Issue: 1
Pages: 22-31
ISSN: 0014-4886 (ISSN-L)
DOI: 10.1006/exnr.1995.1080
OpenAlex: W1584774790
Cited by: 352
References: 0
Citations by year: 2026: 3 · 2025: 7 · 2024: 5 · 2023: 7 · 2022: 10 · 2021: 8 · 2020: 9 · 2019: 9 · 2018: 7 · 2017: 9 · 2016: 10 · 2015: 10 · 2014: 10 · 2013: 12 · 2012: 17
FWCI: 6.73
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Experimental Neurology (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r35ag007909-03)
National Institute on Aging (AG-1048, AG7909)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Oncology › Clusterin in disease pathology
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: clusterin, amyloid-beta 42, amyloid fibril formation, Alzheimer's disease, oxidative stress, neurotoxicity, amyloid plaques, diffuse plaques, PC12 cells, MTT assay
MeSH terms: Alzheimer Disease, Animals, Complement Inactivator Proteins, Dose-Response Relationship, Drug, Glycoproteins, Humans, Immunohistochemistry, Radioligand Assay, Sucrose, Amyloid beta-Protein Precursor, PC12 Cells, Oxidative Stress, Molecular Chaperones, Clusterin, Rats

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Clusterin (apoJ) Alters the Aggregation of Amyloid β-Peptide (Aβ1-42) and Forms Slowly Sedimenting Aβ Complexes That Cause Oxidative Stress

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