Apolipoprotein E: a pathological chaperone protein in patients with cerebral and systemic amyloid
Open accessAbstract
Many biochemically diverse proteins can give rise to amyloid fibrils; however, they are all accompanied by P component and glucosaminoglycans. With antibodies specific to apolipoprotein E (apo E) we used immunohistochemical techniques to test for the presence of this protein in both cerebral and systemic amyloid. We found apo E immunoreactivity in all tested types of cerebral and systemic amyloid. In amyloid deposits apo E P, component and glucosaminoglycans may be acting as 'pathological molecular chaperones'. The latter we define as a group of unrelated proteins that induce beta-pleated conformation in amyloidogenic polypeptides.
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Along with other amyloid-associated proteins, apoE is found in amyloid plaques.
“Along with other amyloid-associated proteins, apoE is found in amyloid plaques (Namba et al., 1991; Wisniewski and Frangione, 1992).”
From Anti-apoE immunotherapy inhibits amyloid accumulation in a transgenic mouse model of Aβ amyloidosis (2012) · cites this paper as Wisniewski and Frangione, 1992
ApoE coaggregates with both parenchymal plaques and CAA.
“Many studies demonstrated that ApoE coaggregates with both parenchymal plaques and CAA [30,31].”
From Apolipoprotein E metabolism and functions in brain and its role in Alzheimer's disease (2017) · cites this paper as [30]
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Opposing Roles of apolipoprotein E in aging and neurodegeneration
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Potter, H. (2016) · JAMA Neurology · doi:10.1001/jamaneurol.2016.0407 · Cited by 3 · see citing works
- Authors
- Wisniewski, T., & Frangione, B.
- Affiliations
- NYU Langone Health (US)
- Corresponding author
- Frangione, Blas
- Venue
- Neuroscience Letters
- Publisher
- Elsevier BV
- Published
- 1992-02
- Volume
- 135
- Issue
- 2
- Pages
- 235-238
- ISSN
- 0304-3940 (ISSN-L)
- OpenAlex
- W1965496447
- Cited by
- 802
- References
- 1
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 8 · 2023: 6 · 2022: 19 · 2021: 10 · 2020: 12 · 2019: 13 · 2018: 12 · 2017: 12 · 2016: 12 · 2015: 15 · 2014: 12 · 2013: 18 · 2012: 15
- FWCI
- 35.50
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Neuroscience Letters (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (R01AG008721, AG-08721)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR02594)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Amyloidosis: Diagnosis, Treatment, Outcomes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- apolipoprotein E, amyloid fibrils, cerebral amyloid, P component, glycosaminoglycans, amyloidogenic proteins, immunoreactivity
- MeSH terms
- Amyloid, Serum Amyloid P-Component, Apolipoproteins E, Brain Chemistry, Glycosaminoglycans, Humans, Nervous System Diseases, Microscopy, Immunoelectron, Paraffin Embedding
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