The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Amino- and carboxyl-terminal heterogeneity of β-amyloid peptides deposited in human brain
Abstract
We aimed to determine quantitatively the fine amino- and carboxyl-terminal structure of A beta peptides deposited in human brain using a set of 12 anti-A beta antibodies that distinguish between terminal modifications including isomerization, stereoisomerization, limited proteolysis, and cyclization. Immunochemical examination of cortical blocks from aged subjects distinguished by their total plaque load and from a young Down's syndrome patient identified the major invariantly deposited species as A beta x-42 (X = 1(D-aspartate) and 3(pyroglutamate) and/or 11(pyroglutamate)). These molecular forms, presumably representing by-products of metabolic intermediates toward degradation, are similar in being resistant to major aminopeptidases. A beta 17-42 ("p3' fragment), a major secreted form of truncated A beta with high insolubility, was found to be a minor one. A possible interpretation for these observations would be that proteolysis of A beta from its amino terminus may limit the rate of A beta catabolism.
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In the citing paper
“Thus, it appears that N-terminally modified or truncated forms of A, which predominate in AD brain (Saido et al., 1995(Saido et al., , 1996;;Hosoda et al., 1998), are minor species in Tg2576 brain that only begin to appear in very old mice.”
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 Saido et al., 1996
In the citing paper
“Much of the A in AD brain is N-terminally truncated or modified (Saido et al., 1995(Saido et al., , 1996;;Hosoda et al., 1998)”
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 Saido et al., 1996
In the citing paper
“Because N-terminally truncated or modified A [especially forms beginning with pyroglutamate at position 3 (3pE)] and oligomers are resistant to proteolysis (Saido et al., 1996;Kuo et al., 1998)”
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 Saido et al., 1996
In the citing paper
“these modifications of A are thought to be important for amyloid deposition.”
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 Saido et al., 1996
In the citing paper
“N-terminal Aβ1-x/βCTF-specific antibodies also fail to label N-truncated Aβ42 peptides that appear to be particularly important in AD [60, 98, 157, 158, 206].”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [157]
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“The posttranslational modification observed at position 1 (pyroglutamate) was previously found in other brain amyloids, i.e., peptides derived from Alzheimer A (Mori et al., 1992; Saido et al., 1996; Tekirian et al., 1998).”
BackgroundWild-Type and Mutated Nicastrins Do Not Display Aminopeptidase M- and B-like Activities
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Self-citationTsai, K., Zhang, Y., Kao, H.-Y., Fung, K.-M., & Tseng, T. (2022) · Food & Function · doi:10.1039/d2fo02507h · Cited by 11
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“A peptide bearing an amino-terminal pyroglutamate at position 3 [A N3(pE)] has been shown to be a major N-truncated, modified constituent of intracellular, extracellular and vascular A deposits in AD brain tissue (Saido et al., 1996; Harigaya et al., 2000).”
BackgroundN-truncated Aβ peptides in complex fluids unraveled by new specific immunoassays
Ranaldi, S., Caillava, C., Promé, S., Rubrecht, L., Cobo, S., Salvetat, N., Paty, E. D., Galéa, P., Aldrian, G., Le‐Nguyen, D., et al. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.05.016 · Cited by 10
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“Despite p3 peptides’ aggregation-prone behavior ( Kuhn and Raskatov, 2020 ) and their accumulation in AD brain ( Higgins et al., 1996 ; Saido et al., 1996 ; Lalowski et al., 1996 ; Gowing et al., 1994 ), the neurotoxicity of these peptides is not well defined ( Walsh et al., 2002 ).”
BackgroundNakayoshi, T., Kato, K., Kurimoto, E., & Oda, A. (2019) · Molecular Physics · doi:10.1080/00268976.2019.1702727 · Cited by 8
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“This peptide is detected in the human brain only under pathological conditions [56], hastens the aggregation of other A β peptides in a prion-like manner [57], and shows enhanced stability [58].”
BackgroundOzaki, M., Shimotsuma, M., Kuranaga, T., Kakeya, H., & Hirose, T. (2023) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c23-00439 · Cited by 7
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“…repeatedly that most of A β in the brains of aged humans and in Down syndrome starts with pyroglutamate (pE) at position 3 and ends at position 42 (A β 3pE-42) (Harigaya et al, 1995; Saido et al, 1995, 1996; Iwatsubo et al, 1996; Lemere et al, 1996; Kawarabayashi et al, 2001; Frost et al, 2013).”
InfluentialSelf-citationBehof, W. J., Haynes, J. R., Whitmore, C. A., Cheung, Y., Tantawy, M. N., Peterson, T. E., Wijesinghe, P., Matsubara, J. A., & Pham, W. N. (2024) · ACS Sensors · doi:10.1021/acssensors.4c00313 · Cited by 6
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“In addition to the main A b species A b 40 and A b 42 , other variants originate from post-translational modi fi cations such as truncation, racemization, isomerization, phosphorylation, metal-induced oxidation, and pyro-glutamination [20 e 33].”
BackgroundModulation of the Activity of the Insulin-Degrading Enzyme by Aβ Peptides
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“…in the pathogenesis of AD, with increased QC activity closely associated with the accumulation of pE-A β 3-42 in cerebral plaques and blood vessels (Saido et al., 1996; Harigaya et al., 2000; Ezura et al., 2004; Batliwalla et al., 2005; Muthusamy et al., 2006; Thouennon et al., 2007; Cynis et al.,…”
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“1998) [such as peptide truncations (Hartig et al. 2010; Kuo et al. 1997; Miravalle et al. 2005; Saido et al. 1996; Tekirian et al. 1998), racemization (Mori et al.”
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“Pyroglutamate Ab is not normally present in vivo; it is, however, found in amyloid plaques (Saido et al., 1996).”
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“8,16,17,53 We thus examined the in vivo half-lives of various A β X-42 isoforms in rat hippocampus using internally radiolabeled A β s and found that most A β variants lacking the N-terminal amino acid(s) except A β 3pE-42 were more short-lived (half-life: approximately 10 min) than A β 1-42…”
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Self-citation
Metadata
- Authors
- Saido, T. C., Yamao-Harigaya, W., Iwatsubo, T., & Kawashima, S.
- Affiliations
- Tokyo Metropolitan Institute of Medical Science (JP)
- The University of Tokyo (JP)
- Corresponding author
- Saido, Takaomi C.
- Venue
- Neuroscience Letters
- Publisher
- Elsevier BV
- Published
- 1996-09
- Volume
- 215
- Issue
- 3
- Pages
- 173-176
- ISSN
- 0304-3940 (ISSN-L)
- OpenAlex
- W2012288880
- Cited by
- 270
- References
- 11
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 11 · 2023: 11 · 2022: 4 · 2021: 7 · 2020: 14 · 2019: 6 · 2018: 6 · 2017: 14 · 2016: 4 · 2015: 9 · 2014: 14 · 2013: 15 · 2012: 8
- FWCI
- 5.63
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neuroscience Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Uehara Memorial Foundation
- Ministry of Education, Culture, Sports, Science and Technology
- Naito Foundation
- 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 plaques, terminal modification, pyroglutamic acid, D-aspartate, anti-amyloid antibodies, Down syndrome, proteolysis, human brain
- MeSH terms
- Adult, Alzheimer Disease, Brain, Humans, Blotting, Western, Amyloid beta-Protein Precursor
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