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Appearance of Sodium Dodecyl Sulfate-Stable Amyloid β-Protein (Aβ) Dimer in the Cortex During Aging
Open accessAbstract
We previously noted that some aged human cortical specimens containing very low or negligible levels of amyloid beta-protein (As) by enzyme immunoassay (EIA) provided prominent signals at 6 approximately 8 kd on the Western blot, probably representing sodium dodecyl sulfate (SDS)-stable Abeta dimer. Re-examination of the specificity of the EIA revealed that BAN50- and BNT77-based EIA, most commonly used for the quantitation of Abeta, capture SDS-dissociable Abeta but not SDS-stable Abeta dimer. Thus, all cortical specimens in which the levels of Abeta were below the detection limits of EIA were subjected to Western blot analysis. A fraction of such specimens contained SDS-stable dimer at 6 approximately 8 kd, but not SDS-dissociable A(beta) monomer at approximately 4 kd, as judged from the blot. This A(beta) dimer is unlikely to be generated after death, because (i) specimens with very short postmortem delay contained the A(beta) dimer, and (ii) until 12 hours postmortem, such SDS-stable A(beta) dimer is detected only faintly in PDAPP transgenic mice. The presence of A(beta) dimer in the cortex may characterize the accumulation of A(beta) in the human brain, which takes much longer than that in PDAPP transgenic mice.
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“and it has been suggested that the formation of SDS stable A oligomers may be an early event in AD (Enya et al., 1999).”
From Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease (2001) · cites this paper as Enya et al., 1999
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“Much of the Ab in AD brain is N-terminally truncated or modified (Saido et al., 1995, 1996; Hosoda et al., 1998), and it has been suggested that the formation of SDS stable Ab oligomers may be an early event in AD (Enya et al., 1999).”
Background
Metadata
- Authors
- Enya, M., Morishima-Kawashima, M., Yoshimura, M., Shinkai, Y., Kusui, K., Khan, K., Games, D., Schenk, D., Sugihara, S., Yamaguchi, H., & Ihara, Y.
- Affiliations
- Japan Science and Technology Agency (JP)
- Kyoto Prefectural University of Medicine (JP)
- Tokyo Women's Medical University (JP)
- Gunma Prefectural Cancer Center (JP)
- Gunma University (JP)
- Corresponding author
- Ihara, Yasuo
- Venue
- The American Journal of Pathology
- Publisher
- Elsevier BV
- Published
- 1999-01
- Volume
- 154
- Issue
- 1
- Pages
- 271-279
- ISSN
- 0002-9440 (ISSN-L)
- PMC
- PMC1853431
- OpenAlex
- W2088449278
- Cited by
- 111
- References
- 42
- Citations by year
- 2026: 2 · 2024: 10 · 2023: 4 · 2021: 5 · 2020: 1 · 2019: 3 · 2018: 3 · 2017: 1 · 2016: 1 · 2015: 6 · 2014: 4 · 2012: 5
- FWCI
- 3.78
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- American Journal Of Pathology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministry of Health, Labour and Welfare
- Ministry of Education, Culture, Sports, Science and Technology (09835003)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid-beta, amyloid-beta dimers, cerebral cortex, brain aging, postmortem delay, amyloid accumulation, Alzheimer's disease
- MeSH terms
- Adult, Aged, Aged, 80 and over, Aging, Animals, Antibodies, Monoclonal, Cerebral Cortex, Drug Stability, Female, Humans, Immunoenzyme Techniques, Male, Mice, Transgenic, Middle Aged, Molecular Conformation, Sodium Dodecyl Sulfate, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Dimerization, Mice
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