Amyloid β binding proteins in vitro and in normal human cerebrospinal fluid
Open accessAbstract
A major neuropathological feature of Alzheimer's disease (AD) is the deposition of amyloid beta (A beta) in the form of senile plaques. The A beta peptide exists both in a beta-pleated sheet fibrillar form in amyloid deposits and as a normal soluble protein in biological fluids. Numerous proteins have been identified immunohistochemically to be associated with senile plaques, where A beta is the major constituent. Some of the latter have also been suggested to be carriers of the normal soluble A beta (sA beta) including apolipoprotein J (apoJ), apolipoprotein E (apoE) and transthyretin (TTR). We have found, using several different methods, that numerous proteins can bind synthetic A beta peptides when high concentrations are used; however, using an affinity anti-sA beta column we confirm that apoJ is the major binding protein in pooled human cerebrospinal fluid. On the other hand it is known that apoE co-purifies with A beta biochemically extracted from senile plaques. In AD tissue there may be a change in the major apolipoprotein binding A beta from apoJ to apoE.
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Clusterin interacts with soluble Aβ and forms complexes that cross the blood-brain barrier.
“It interacts with the soluble form of Aβ in animal models of disease and binds soluble Aβ in a specific and reversible manner, forming complexes that have been shown to cross the blood-brain barrier [21][22][23][24] .”
From Genome-wide association study identifies variants at CLU and PICALM associated with Alzheimer's disease (2009) · cites this paper as [23]
The paper reports that apoJ (clusterin) is the major binding protein for soluble Aβ in normal human cerebrospinal fluid (Abstract; page unavailable). It says soluble Aβ can cross the blood-brain barrier, but does not establish that apoJ–Aβ complexes cross it. The cited passages also do not establish binding in animal disease models or that the binding is specific and reversible. (LLM, conf=0.88)
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Ma, J., Yee, A., Brewer, H. B., Das, S., & Potter, H. (1994) · Nature · doi:10.1038/372092a0 · Cited by 871 · see citing works
Is Alzheimer's disease an apolipoprotein E amyloidosis?
Wisniewski, T., Lalowski, M., Golabek, A., Frangione, B., & Vogel, T. (1995) · The Lancet · doi:10.1016/s0140-6736(95)90701-7 · Cited by 155 · see citing works
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- Maggio, J.E., Stimson, E.R., Ghilardi, J.R., Allen, C.J., Dahl, C.E., Whitcomb, D.L., Vigna, S.R., Vinter, H.V., Labenski, M.E. and Mantyh, P.W., Reversible in vitro growth of Alzheimer's dis- ease p-amyloid plaques by deposition of labeled amyloid peptide, Proc. Natl. Acad. Sci. USA, 89 (1992) 5462-5466.
- Oda, T., Pasinetti, G.M., Stine, W.B., Snyder, S.W:, Holzman, T.F., Kraft, G.A., Osterburg, H.H., Johnson, S.A. and Finch, C.E., Clusterin inhibits the aggregation of amyloid B-peptide and forms a soluble complex that causes oxidative stress, Exp. Neurol., in press.
- Schwarzman, A.L., Gregori, L., Vitek, M.P., Lyubski, S., Strittmatter, W.J., Enghilde, J.J., Bhasin, R., Silverman, J., Weis- braber, K.H., Coyle, P.K., Zagorski, M.G., Taiafous, J., Eisen- berg, M., Saunders, A.M., Roses, A.D. and Goldgaber, D., Transthyretin sequesters amyloid j3 protein and prevents amyloid formation, Proc. Natl. Acad. Sci. USA, 91 (1994) 8368-8372.
- Strittmatter, W. J., Saunders, A. M., Schmechel, D., Pericak- Vance, M., Enghild, J., Salvesen, G.S. and Roses, A.D., Apolipo- protein E: high-avidity binding to p-amyloid and increased he- quency of type 4 allele in late-onset familial Alzheimer disease, Proc. Natl. Acad. Sci. USA, 90 (1993) 1977-1981.
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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 · see citing works
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Regland, B., Lehmann, W., Abedini, I., Blennow, K., Jonsson, M., Karlsson, I., Sjögren, M., Wallin, A., Xilinas, M., & Gottfries, C.-G. (2001) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000051288 · Cited by 220 · see citing works
Replication of CLU, CR1, and PICALM Associations With Alzheimer Disease
Carrasquillo, M. M., Belbin, O., Hunter, T. A., Ma, L., Bisceglio, G. D., Zou, F., Crook, J. E., Pankratz, V. S., Dickson, D. W., Graff-Radford, N. R., et al. (2010) · Archives of Neurology · doi:10.1001/archneurol.2010.147 · Cited by 208 · see citing works
Tai, L. M., Bilousova, T., Jungbauer, L., Roeske, S. K., Youmans, K. L., Yu, C., Poon, W. W., Cornwell, L. B., Miller, C. A., Vinters, H. V., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.442103 · Cited by 165 · see citing works
Sadowski, M., Pankiewicz, J., Scholtzova, H., Ripellino, J. A., Li, Y., Schmidt, S. D., Mathews, P. M., Fryer, J. D., Holtzman, D. M., Sigurdsson, E. M., et al. (2004) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63355-x · Cited by 154 · see citing works
Nilselid, A.-M., Davidsson, P., Nägga, K., Andreasen, N., Fredman, P., & Blennow, K. (2006) · Neurochemistry International · doi:10.1016/j.neuint.2005.12.005 · Cited by 104 · see citing works
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Bishop, G. M., & Robinson, S. R. (2004) · Drugs & Aging · doi:10.2165/00002512-200421100-00001 · Cited by 94 · see citing works
Han, S.-H., Park, J.-C., & Mook-Jung, I. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.12.004 · Cited by 67 · see citing works
- Authors
- Golabek, A., Marques, M. A., Lalowski, M., & Wisniewski, T.
- Affiliations
- NYU Langone Health (US)
- ORCID
- Lalowski, Maciej
- Venue
- Neuroscience Letters
- Publisher
- Elsevier BV
- Published
- 1995-05
- Volume
- 191
- Issue
- 1-2
- Pages
- 79-82
- ISSN
- 0304-3940 (ISSN-L)
- OpenAlex
- W2079330864
- Cited by
- 99
- References
- 2
- Citations by year
- 2025: 1 · 2021: 1 · 2020: 6 · 2019: 5 · 2018: 3 · 2017: 1 · 2016: 1 · 2015: 4 · 2014: 4 · 2013: 2 · 2012: 4
- FWCI
- 3.22
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Neuroscience Letters (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (AG00542, AG10953, R35AG010953)
- Topics
- Health Sciences › Medicine › Physiology › 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, Alzheimer's disease, cerebrospinal fluid, clusterin, apolipoprotein E, prealbumin, amyloid plaques
- MeSH terms
- Amino Acid Sequence, Animals, Antibodies, Monoclonal, Apolipoproteins E, Cattle, Glycoproteins, Humans, Immunohistochemistry, Iodine Radioisotopes, Molecular Sequence Data, Nerve Tissue Proteins, Prealbumin, Precipitin Tests, Protein Binding, Blotting, Western, Amyloid beta-Peptides, Molecular Chaperones, Clusterin
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