The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Apolipoprotein J and Alzheimer's amyloid β solubility
Open accessAbstract
Apolipoprotein J (apoJ) has been found associated with soluble amyloid β (sAβ) in plasma and cerebrospinal fluid in normal individuals and co-deposited with fibrillar Aβ in Alzheimer's cerebrovascular and parenchymal lesions. Although studies in vitro and in vivo indicate that apoJ is a major carrier protein for sAβ, its role in the fibrillogenesis process is not known. We report herein that apoJ in its native high-density lipoprotein lipidic environment is fully active to interact with Aβ peptides. Furthermore, apoJ prevents aggregation and polymerization of synthetic Aβ in vitro. The interaction was stable for at least 14 days at 37 °C in physiologic buffers, and the peptide retrieved after complex dissociation at low pH retained its inherent aggregation properties. In addition, the binding to apoJ protects synthetic Aβ from proteolytic degradation; both Aβ1–42 and Aβ1–40 were more resistant to proteolysis by trypsin and chymotrypsin when complexed to apoJ. The data suggest that the interaction may preclude sAβ aggregation in biological fluids and point to a protecting role of apoJ for complexed Aβ species.
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Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids
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Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs.
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Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
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
Alzheimer’s Disease Risk Genes and Mechanisms of Disease Pathogenesis
Karch, C. M., & Goate, A. M. (2015) · Biological Psychiatry · doi:10.1016/j.biopsych.2014.05.006 · Cited by 1,357
ApoE and Clusterin Cooperatively Suppress Aβ Levels and Deposition
DeMattos, R. B., Cirrito, J. R., Parsadanian, M., May, P. C., O'Dell, M. A., Taylor, J. W., Harmony, J. A. K., Aronow, B. J., Bales, K. R., Paul, S. M., et al. (2004) · Neuron · doi:10.1016/s0896-6273(03)00850-x · Cited by 459
Clusterin in Alzheimer’s Disease: Mechanisms, Genetics, and Lessons From Other Pathologies
Foster, E. M., Dangla-Valls, A., Lovestone, S., Ribe, E. M., & Buckley, N. J. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00164 · Cited by 381
Metadata
- Authors
- MATSUBARA, E., SOTO, C., GOVERNALE, S., FRANGIONE, B., & GHISO, J.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1996-06-01
- Volume
- 316
- Issue
- 2
- Pages
- 671-679
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1755584404
- Cited by
- 190
- References
- 7
- FWCI
- 4.46
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Apolipoprotein J and Alzheimer's amyloid β solubility. https://app.cochat.ai/papers/10.1042/bj3160671
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- MATSUBARA, E., SOTO, C., GOVERNALE, S., FRANGIONE, B., & GHISO, J. (1996). Apolipoprotein J and Alzheimer's amyloid β solubility. Biochemical Journal. https://doi.org/10.1042/bj3160671
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
