The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Amyloid-associated proteins α1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filaments
Abstract
The protease inhibitor alpha 1-antichymotrypsin and the lipid transport protein apolipoprotein E (apoE) are intimately associated with the 42-amino-acid beta-peptide (A beta) in the filamentous amyloid deposits of Alzheimer's disease. We report here that these two amyloid-associated proteins serve a strong stimulatory role in the polymerization of A beta into amyloid filaments. Addition of either alpha 1-anti-chymotrypsin or apoE to the A beta peptide promoted a 10- to 20-fold increase in filament formation, with apoE-4, the isoform recently linked to the development of late-onset Alzheimer's disease, showing the highest catalytic activity. These and other experiments suggest that Alzheimer amyloid deposits arise when A beta is induced to form filaments by amyloid-promoting factors (pathological chaperones) expressed in certain brain regions.
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In the citing paper
“lipid-free apoE4 was found to facilitate Aβ fibrillization in vitro to a greater degree compared to apoE3 [(47, 48); see (39) for a review].”
From Human ApoE isoforms differentially regulate brain amyloid-β peptide clearance (2011) · cites this paper as [47]
In the citing paper
“ApoE has also been reported to promote A 𝛃 aggregation (5)”
From Therapeutic Idol reduction ameliorates amyloidosis and improves cognitive function in APP/PS1 mice (2020) · cites this paper as [5]
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 [13]
In the citing paper
“In vitro, apoE and apoJ form stable complexes with A (11, 16 -20), alter the aggregation of various A peptides (21)(22)(23), and affect A neurotoxicity (24 -27).”
From Apolipoprotein E Receptors Mediate the Effects of β-Amyloid on Astrocyte Cultures (2000) · cites this paper as [21]
In the citing paper
“Together these data expand previous studies in mouse models of Aβ aggregation suggesting a pathogenic role for C4b and Serpina3n23,24,44,45, as well as genetic studies linking the human homologue SERPINA3 to AD risk46”
From Human and mouse single-nucleus transcriptomics reveal TREM2-dependent and TREM2-independent cellular responses in Alzheimer’s disease (2020) · cites this paper as [45]
Citations
Cites
Corder, E. H., Saunders, A. M., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Small, G. W., Roses, A. D., Haines, J. L., & Pericak-Vance, M. A. (1993) · Science · doi:10.1126/science.8346443 · Cited by 9,429
Strittmatter, W. J., Saunders, A. M., Schmechel, D., Pericak-Vance, M., Enghild, J., Salvesen, G. S., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.5.1977 · Cited by 4,268
Amyloid β-peptide is produced by cultured cells during normal metabolism
Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921
Protective effect of apolipoprotein E type 2 allele for late onset Alzheimer disease
Corder, E. H., Saunders, A. M., Risch, N. J., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Rimmler, J. B., Locke, P. A., Conneally, P. M., Schmader, K. E., et al. (1994) · Nature Genetics · doi:10.1038/ng0694-180 · Cited by 1,920
Iwatsubo, T., Odaka, A., Suzuki, N., Mizusawa, H., Nukina, N., & Ihara, Y. (1994) · Neuron · doi:10.1016/0896-6273(94)90458-8 · Cited by 1,774
Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids
Seubert, P., Vigo-Pelfrey, C., Esch, F., Lee, M., Dovey, H., Davis, D., Sinha, S., Schiossmacher, M., Whaley, J., Swindlehurst, C., et al. (1992) · Nature · doi:10.1038/359325a0 · Cited by 1,731
Schmechel, D. E., Saunders, A. M., Strittmatter, W. J., Crain, B. J., Hulette, C. M., Joo, S. H., Pericak-Vance, M. A., Goldgaber, D., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.20.9649 · Cited by 1,525
Suzuki, N., Cheung, T. T., Cai, X.-D., Odaka, A., Otvos, L., Eckman, C., Golde, T. E., & Younkin, S. G. (1994) · Science · doi:10.1126/science.8191290 · Cited by 1,471
Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing
Shoji, M., Golde, T. E., Ghiso, J., Cheung, T. T., Estus, S., Shaffer, L. M., Cai, X.-D., McKay, D. M., Tintner, R., Frangione, B., et al. (1992) · Science · doi:10.1126/science.1439760 · Cited by 1,447
Namba, Y., Tomonaga, M., Kawasaki, H., Otomo, E., & Ikeda, K. (1991) · Brain Research · doi:10.1016/0006-8993(91)91092-f · Cited by 1,157
Apolipoprotein E in sporadic Alzheimer's disease: Allelic variation and receptor interactions
William Rebeck, G., Reiter, J. S., Strickland, D. K., & Hyman, B. T. (1993) · Neuron · doi:10.1016/0896-6273(93)90070-8 · Cited by 1,107
Abraham, C. R., Selkoe, D. J., & Potter, H. (1988) · Cell · doi:10.1016/0092-8674(88)90462-x · Cited by 900
Self-citationApolipoprotein E: a pathological chaperone protein in patients with cerebral and systemic amyloid
Wisniewski, T., & Frangione, B. (1992) · Neuroscience Letters · doi:10.1016/0304-3940(92)90444-c · Cited by 802
Roher, A. E., Lowenson, J. D., Clarke, S., Woods, A. S., Cotter, R. J., Gowing, E., & Ball, M. J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.22.10836 · Cited by 740
Kirschner, D. A., Inouye, H., Duffy, L. K., Sinclair, A. J., Lind, M., & Selkoe, D. J. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.19.6953 · Cited by 481
Sanan, D. A., Weisgraber, K. H., Russell, S. J., Mahley, R. W., Huang, D., Saunders, A., Schmechel, D., Wisniewski, T., Frangione, B., & Roses, A. D. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117407 · Cited by 404
Abnormal in vivo metabolism of apolipoprotein E4 in humans.
Gregg, R. E., Zech, L. A., Schaefer, E. J., Stark, D., Wilson, D., & Brewer, H. B. (1986) · Journal of Clinical Investigation · doi:10.1172/jci112645 · Cited by 345
Self-citationAlzheimer's disease : basic mechanisms, diagnosis and therapeutic strategies
Iqbal, K. (1991) · Wiley eBooks · Cited by 322
Castaño, E. M., Ghiso, J. A., Prelli, F. C., Gorevic, P. D., Migheli, A., & Frangione, B. (1986) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(86)80241-8 · Cited by 225
Apolipoprotein E: Binding to Soluble Alzheimer′s β-Amyloid
Wisniewski, T., Golabek, A., Matsubara, E., Ghiso, J., & Frangione, B. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.1423 · Cited by 212
Abraham, C. R., Shirahama, T., & Potter, H. (1990) · Neurobiology of Aging · doi:10.1016/0197-4580(90)90045-2 · Cited by 150
Self-citationAstrocytes in Alzheimer's disease gray matter express alpha 1-antichymotrypsin mRNA.
Pasternack, J. M., Abraham, C. R., Dyke, B. J. V., Potter, H., & Younkin, S. G. (1989) · PubMed Central · Cited by 140
Self-citationFraser, P. E., Nguyen, J. T., McLachlan, D. R. C., Abraham, C. R., & Kirschner, D. A. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03568.x · Cited by 138
A special type of senile plaque, possibly an initial stage
Probst, A., Brunnschweiler, H., Lautenschläger, C., & ULRICH, J. (1987) · Acta Neuropathologica · doi:10.1007/bf00692843 · Cited by 127
Rozemüller, A. J. M., Abbink, J. J., Kamp, A. M., Stam, F. C., Hack, C. E., & Eikelenboom, P. (1991) · Acta Neuropathologica · doi:10.1007/bf00294446 · Cited by 97
Cells with a familial Alzheimerʼs disease mutation produce authentic β-peptide
Dovey, H. F., Suomensaari-Chrysler, S., Lieberburg, I., Sinha, S., & Keim, P. S. (1993) · NeuroReport · doi:10.1097/00001756-199308000-00011 · Cited by 71
Distribution of the Protease Inhibitor α1-Antichymotrypsin in Cerebral and Systemic Amyloid
Picken, M. M., Larrondo-Lillo, M., Coria, F., Gallo, G. R., Shelanski, M. L., & Frangione, B. (1990) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199001000-00005 · Cited by 65
Developmental expression of α1-antichymotrypsin in brain may be related to astrogliosis
Koo, E. H., Abraham, C. R., Potter, H., Cork, L. C., & Price, D. L. (1991) · Neurobiology of Aging · doi:10.1016/0197-4580(91)90079-y · Cited by 49
Self-citationPotter, H., Nelson, R. B., Das, S., Siman, R. G., Kayyali, U. S., & Dressler, D. (1992) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1992.tb27485.x · Cited by 29
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Research works printed but not linked: 3
- Pasternack, J. M., Abraham, C. R., Van Dyke, B., Potter, H. & Younkin, S. G. Am. J. Pathol. 135, 827–834 (1989).
- Das, S. & Potter, H. Neuron (in the press).
- Wisniewski, T. et al. Am. J. Path. (in the press).
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Selkoe, D. J., & Hardy, J. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606210 · Cited by 6,164
Alzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063
Inflammation and Alzheimer’s disease
Akiyama, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00124-x · Cited by 4,514
Harold, D., Abraham, R., Hollingworth, P., Sims, R., Gerrish, A., Hamshere, M. L., Pahwa, J. S., Moskvina, V., Dowzell, K., Williams, A., et al. (2009) · Nature Genetics · doi:10.1038/ng.440 · Cited by 3,326
Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W., et al. (1996) · Nature Medicine · doi:10.1038/nm0896-864 · Cited by 2,599
Metadata
- Authors
- Ma, J., Yee, A., Brewer, H. B., Das, S., & Potter, H.
- Affiliations
- Harvard University (US)
- National Institutes of Health (US)
- Venue
- Nature
- Published
- 1994-11
- Volume
- 372
- Issue
- 6501
- Pages
- 92-94
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2021333248
- Cited by
- 871
- References
- 29
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 8 · 2023: 5 · 2022: 20 · 2021: 17 · 2020: 21 · 2019: 16 · 2018: 13 · 2017: 20 · 2016: 17 · 2015: 12 · 2014: 17 · 2013: 13 · 2012: 18
- FWCI
- 47.73
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- 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
- alpha-1-antichymotrypsin, apolipoprotein E, amyloid-beta, Alzheimer's disease, APOE isoforms, APOE ε4, protease inhibitors, lipid transfer proteins, amyloidosis
- MeSH terms
- alpha 1-Antichymotrypsin, Alzheimer Disease, Apolipoproteins E, Biopolymers, Humans, Peptide Fragments, Amyloid beta-Peptides, Molecular Chaperones, Apolipoprotein E3, Apolipoprotein E4, Apolipoprotein E2, In Vitro Techniques
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