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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
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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In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“A 1-42 aged according to this protocol is a mixture of fibrils and soluble globular aggregates, and is active to astrocytes (37,38) and toxic to neurons (26,27).”
From Apolipoprotein E Receptors Mediate the Effects of β-Amyloid on Astrocyte Cultures (2000) · cites this paper as [26]
In the citing paper
“In vitro, apoE and apoJ form stable complexes with A (11, 16 -20), alter the aggregation of various A peptides (21)(22)(23), and affect A neurotoxicity (24 -27).”
From Apolipoprotein E Receptors Mediate the Effects of β-Amyloid on Astrocyte Cultures (2000) · cites this paper as [26]
In the citing paper
“ApoJ has been shown to potentiate the formation of a neurotoxic species of A (26,27).”
From Apolipoprotein E Receptors Mediate the Effects of β-Amyloid on Astrocyte Cultures (2000) · cites this paper as [26]
In the citing paper
“ApoE, apoJ, and most recently ␣ 2 -macroglobulin have been shown to form a complex with A that may facilitate clearance of the peptide (25-27, 50, 51).”
From Apolipoprotein E Receptors Mediate the Effects of β-Amyloid on Astrocyte Cultures (2000) · cites this paper as [26]
In the citing paper
“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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The case for soluble Aβ oligomers as a drug target in Alzheimer's disease
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Self-citationHuman apolipoprotein A–I binds amyloid-β and prevents Aβ-induced neurotoxicity
Paula-Lima, A. C., Tricerri, M. A., Brito-Moreira, J., Bomfim, T. R., Oliveira, F. F., Magdesian, M. H., Grinberg, L. T., Panizzutti, R., & Ferreira, S. T. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.12.003 · Cited by 121
Metadata
- 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)
- Venue
- Experimental Neurology
- Publisher
- Elsevier BV
- Published
- 1995-11
- Volume
- 136
- Issue
- 1
- Pages
- 22-31
- ISSN
- 0014-4886 (ISSN-L)
- 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
- Locations
- Experimental Neurology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r35ag007909-03)
- National Institute on Aging (AG-1048, AG7909)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › 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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