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]
Citations
Cites
Strittmatter, W. J., Weisgraber, K. H., Huang, D. Y., Dong, L. M., Salvesen, G. S., Pericak-Vance, M., Schmechel, D., Saunders, A. M., Goldgaber, D., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.17.8098 · Cited by 1,363
Evidence that production and release of amyloid beta-protein involves the endocytic pathway
Koo, E. H., & Squazzo, S. L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32449-3 · Cited by 829
Roher, A. E., Lowenson, J. D., Clarke, S., Wolkow, C., Wang, R., Cotter, R. J., Reardon, I. M., Zürcher-Neely, H. A., Heinrikson, R. L., & Ball, M. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53661-9 · Cited by 799
Saido, T. C., Iwatsubo, T., Mann, D. M. A., Shimada, H., Ihara, Y., & Kawashima, S. (1995) · Neuron · doi:10.1016/0896-6273(95)90301-1 · Cited by 587
Self-citationMass spectrometry of purified amyloid beta protein in Alzheimer's disease.
Mori, H., Takio, K., OGAWARA, M., & Selkoe, D. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41896-0 · Cited by 486
Physiological production of the β-amyloid protein and the mechanism of Alzheimer's disease
Selkoe, D. J. (1993) · Trends in Neurosciences · doi:10.1016/0166-2236(93)90008-a · Cited by 423
Amyloid β protein (Aβ) deposition: Aβ42(43) precedes Aβ40 in down Syndrome
Iwatsubo, T., Mann, D. M. A., Odaka, A., Suzuki, N., & Ihara, Y. (1995) · Annals of Neurology · doi:10.1002/ana.410370305 · Cited by 386
Self-citationAmino-terminal Deletions Enhance Aggregation of β-Amyloid Peptides in Vitro
Pike, C. J., Overman, M. J., & Cotman, C. W. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.41.23895 · Cited by 302
Genetics and molecular advances in Alzheimer's disease
Mullan, M., & Crawford, F. (1993) · Trends in Neurosciences · doi:10.1016/0166-2236(93)90007-9 · Cited by 181
Spatial resolution of the primary beta-amyloidogenic process induced in postischemic hippocampus.
Saido, T. C., Yokota, M., Maruyama, K., Yamao‐Harigaya, W., Tani, E., Ihara, Y., & Kawashima, S. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36599-7 · Cited by 80
Self-citation
Research works printed but not linked: 1
- Sakura, 1983, Kinetic propitious of placental aminopeptidase A, Biochem. Int., 6, 609
Cited by
Sorted by citations
Karran, E., Mercken, M., & Strooper, B. D. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3505 · Cited by 2,188
“Given the avidity of amyloid-β deposition onto plaques, it is unlikely that even very substantial reductions in the levels of free amyloid-β would mediate a reduction in the formation of amyloid plaques in patients, especially as post-translational modifications of deposited amyloid-β over many years render human amyl…”
BackgroundPetkova, A. T., Ishii, Y., Balbach, J. J., Antzutkin, O. N., Leapman, R. D., Delaglio, F., & Tycko, R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.262663499 · Cited by 1,847
Kawarabayashi, T., Younkin, L. H., Saido, T. C., Shoji, M., Ashe, K. H., & Younkin, S. G. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-02-00372.2001 · Cited by 1,053
“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).”
BackgroundMethodInfluentialSelf-citationWang, J., Dickson, D. W., Trojanowski, J. Q., & Lee, V. M.-Y. (1999) · Experimental Neurology · doi:10.1006/exnr.1999.7085 · Cited by 567
Kuperstein, I., Broersen, K., Benilova, I., Rozenski, J., Jonckheere, W., Debulpaep, M., Vandersteen, A., Segers‐Nolten, I., Van Der Werf, K., Subramaniam, V., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.211 · Cited by 532
“Additional heterogeneity is generated at the aminoterminus by aminopeptidases, glutaminylcyclases and other modifica- tions (Pike et al, 1995; Saido et al, 1996) (reviewed in De Strooper, 2010).”
Background
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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