The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Apolipoprotein E immunoreactivity in cerebral amyloid deposits and neurofibrillary tangles in Alzheimer's disease and kuru plaque amyloid in Creutzfeldt-Jakob disease
Abstract
During the course of our immunohistochemical studies on the change of lipids in Alzheimer's disease brains by using antibody to apolipoprotein E, a protein having a special relevance to nervous tissue, we unexpectedly found that apo E immunoreactivity was associated with amyloid in both senile plaques and cerebral vessels and neurofibrillary tangles. The immunoreactivity was also found in amyloid of kuru plaques in Creutzfeldt-Jakob disease. Pretreatment of the sections with formic acid greatly enhanced immunoreactivity of senile and kuru plaques to antibody to apo E.
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In the citing paper
“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 Namba et al., 1991
In the citing paper
“Because APOE co‐localizes with Aβ, 17 the reduced amyloid deposition in Ldlr‐overexpressing mice may stem from the interaction between APOE and Aβ and their subsequent uptake via these receptors.”
From Deletion of neuronal Idol ameliorates Alzheimer's disease–related pathologies via APOE receptors (2025) · cites this paper as [17]
In the citing paper
“and it also colocalizes with A plaques (Namba et al., 1991).”
From Anti-ApoE Antibody Given after Plaque Onset Decreases Aβ Accumulation and Improves Brain Function in a Mouse Model of Aβ Amyloidosis (2014) · cites this paper as Namba et al., 1991
In the citing paper
“Interestingly, apoE colocalizes with amyloid plaques (Namba et al., 1991).”
From Apolipoprotein E in Synaptic Plasticity and Alzheimer’s Disease: Potential Cellular and Molecular Mechanisms (2014) · cites this paper as Namba et al., 1991
In the citing paper
“As apoE co-deposits with Aβ in the amyloid plaques (13–15), we examined and found that the degree of co-localization between apoE and Aβ deposition appeared to decrease in the brains carrying APOE3-Jac variant compared to those from APOE3 (Fig. S1C–F).”
From APOE3 -Jacksonville (V236E) variant reduces self-aggregation and risk of dementia (2021) · cites this paper as [15]
In the citing paper
“In the brain, plasma, and cerebrospinal fluid as well as in senile plaques A is associated to apolipoprotein E (apoE) (16 -18).”
From Internalization of β-Amyloid Peptide by Primary Neurons in the Absence of Apolipoprotein E (2007) · cites this paper as [16]
In the citing paper
“ApoE was found to be essential for plaque formation during the initial seeding stage121,122.”
From Interplay between innate immunity and Alzheimer disease: APOE and TREM2 in the spotlight (2018) · cites this paper as [122]
Citations
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Jendresen, C., Årskog, V., Daws, M. R., & Nilsson, L. N. G. (2017) · Journal of Neuroinflammation · doi:10.1186/s12974-017-0835-4 · Cited by 94
Apolipoprotein E and Alzheimer's disease: the protective effects of ApoE2 and E3
Rebeck, G. W., Kindy, M., & LaDu, M. J. (2002) · Journal of Alzheimer's Disease · doi:10.3233/jad-2002-4304 · Cited by 89
(2012) · Progress in Molecular Biology and Translational Science · doi:10.1016/b978-0-12-385883-2.00006-0 · Cited by 84
Shifting paradigms: The central role of microglia in Alzheimer’s disease
Schwabe, T., Srinivasan, K., & Rhinn, H. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.104962 · Cited by 84
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Cholinergic systems and long-term potentiation in memory-impaired apolipoprotein E-deficient mice
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Deletion of neuronal Idol ameliorates Alzheimer's disease–related pathologies via APOE receptors
Karahan, H., Hartigan, K., Al‐Amin, M. M., John, S. K., McCord, B., Wijeratne, H. R. S., Acri, D. J., Smith, D. C., Dabin, L. C., Cordero, H. M. R., et al. (2025) · Alzheimer's & Dementia · doi:10.1002/alz.70949 · Cited by 2
“16 Because APOE co-localizes with A β , 17 the reduced amyloid deposition in Ldlr - overexpressing mice may stem from the interaction between APOE and A β and their subsequent uptake via these receptors.”
Metadata
- Authors
- Namba, Y., Tomonaga, M., Kawasaki, H., Otomo, E., & Ikeda, K.
- Affiliations
- Tokyo Institute of Psychiatry (JP)
- The University of Tokyo (JP)
- Yokufukai Hospital (JP)
- Corresponding author
- Namba, Yoshio
- Venue
- Brain Research
- Publisher
- Elsevier BV
- Published
- 1991-02
- Volume
- 541
- Issue
- 1
- Pages
- 163-166
- ISSN
- 0006-8993 (ISSN-L)
- OpenAlex
- W2072682191
- Cited by
- 1,157
- References
- 24
- Citations by year
- 2026: 11 · 2025: 19 · 2024: 13 · 2023: 19 · 2022: 30 · 2021: 34 · 2020: 28 · 2019: 33 · 2018: 19 · 2017: 26 · 2016: 19 · 2015: 17 · 2014: 23 · 2013: 20 · 2012: 21
- FWCI
- 23.38
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Brain Research (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- apolipoprotein E, Alzheimer's disease, Creutzfeldt-Jakob disease, kuru plaques, amyloid plaques, neurofibrillary tangles, formic acid pretreatment, immunoreactivity
- MeSH terms
- Alzheimer Disease, Amyloid, Apolipoproteins E, Brain, Humans, Immunohistochemistry, Creutzfeldt-Jakob Syndrome, Kuru, Neurofibrils
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