The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
A Specific Enzyme-Linked Immunosorbent Assay for Measuring β-Amyloid Protein Oligomers in Human Plasma and Brain Tissue of Patients With Alzheimer Disease
Open accessAbstract
OBJECTIVE: To examine in vivo levels of beta-amyloid (Abeta) oligomers (oAbeta) vs monomeric Abeta in plasma and brain tissue of patients with sporadic and familial Alzheimer disease (AD) using a new enzyme-linked immunosorbent assay (ELISA) specific for oAbeta. DESIGN: To establish the oAbeta ELISA, the same N-terminal Abeta antibody was used for antigen capture and detection. Plasma and postmortem brain tissue from patients with AD and control subjects were systematically analyzed by conventional monomeric Abeta and new oAbeta ELISAs. SUBJECTS: We measured oAbeta species in plasma samples from 36 patients with clinically well-characterized AD and 10 control subjects. In addition, postmortem samples were obtained from brain autopsies of 9 patients with verified AD and 7 control subjects. MAIN OUTCOME MEASURES: Oligomeric Abeta and 4 monomeric Abeta species in plasma samples from patients with AD and control subjects were measured by ELISA. RESULTS: The specificity of the oAbeta ELISA was validated with a disulfide-crossed-linked, synthetic Abeta(1-40)Ser26Cys dimer that was specifically detected before but not after the dissociation of the dimers in beta-mercaptoethanol. Plasma assays showed that relative oAbeta levels were closely associated with relative Abeta(42) monomer levels across all of the subjects. Analysis of sequential plasma samples from a subset of the patients with AD, including a patient with AD caused by a presenilin mutation, revealed decreases in both oAbeta and Abeta(42) monomer levels over a 1- to 2-year period. In brain tissue from 9 patients with AD and 7 control subjects, both oAbeta and monomeric Abeta(42) levels were consistently higher in the AD cases. CONCLUSIONS: An oAbeta-specific ELISA reveals a tight link between oAbeta and Abeta(42) monomer levels in plasma and brain. Both forms can decline over time in plasma, presumably reflecting their increasing insolubility in the brain.
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Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
Self-citationScheuner, 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
Self-citationJarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022
Deciphering the Molecular Basis of Memory Failure in Alzheimer's Disease
Walsh, D. M., & Selkoe, D. J. (2004) · Neuron · doi:10.1016/j.neuron.2004.09.010 · Cited by 1,207
Self-citationClassification and prediction of clinical Alzheimer's diagnosis based on plasma signaling proteins
Ray, S., Britschgi, M., Herbert, C., Takeda-Uchimura, Y., Boxer, A., Blennow, K., Friedman, L. F., Galasko, D. R., Jutel, M., Karydas, A., et al. (2007) · Nature Medicine · doi:10.1038/nm1653 · Cited by 1,048
Fagan, A. M., Roe, C. M., Xiong, C., Mintun, M. A., Morris, J. C., & Holtzman, D. M. (2007) · Archives of Neurology · doi:10.1001/archneur.64.3.noc60123 · Cited by 897
Plasma Aβ40 and Aβ42 and Alzheimer’s disease: Relation to age, mortality, and risk
Mayeux, R., Honig, L. S., Tang, M.-X., Manly, J., Stern, Y., Schupf, N., & Mehta, P. D. (2003) · Neurology · doi:10.1212/01.wnl.0000091890.32140.8f · Cited by 434
Portelius, E., Westman-Brinkmalm, A., Zetterberg, H., & Blennow, K. (2006) · Journal of Proteome Research · doi:10.1021/pr050475v · Cited by 206
Cited by
The Amyloid-β Pathway in Alzheimer’s Disease
Hampel, H., Hardy, J., Blennow, K., Chen, C., Perry, G., Kim, S. H., Villemagne, V. L., Aisen, P., Vendruscolo, M., Iwatsubo, T., et al. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01249-0 · Cited by 1,952
Is Alzheimer’s disease a type 3 diabetes? A critical appraisal
Kandimalla, R., Thirumala, V., & Reddy, P. H. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.08.018 · Cited by 621
The Alzheimer’s Disease Mitochondrial Cascade Hypothesis
Swerdlow, R. H., Burns, J. M., & Khan, S. M. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100339 · Cited by 562
“While a systemic increase in body Aβ levels could cause this, in AD Aβ levels actually drop in some tissues [27].”
BackgroundThe amyloid cascade-inflammatory hypothesis of Alzheimer disease: implications for therapy
McGeer, P. L., & McGeer, E. G. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1177-7 · Cited by 467
Synaptopathies: synaptic dysfunction in neurological disorders – A review from students to students
Lepeta, K., Lourenco, M. V., Schweitzer, B. C., Martino Adami, P. V., Banerjee, P., Catuara‐Solarz, S., de La Fuente Revenga, M., Guillem, A. M., Haidar, M., Ijomone, O. M., et al. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13713 · Cited by 386
Metadata
- Authors
- Xia, W., Yang, T., Shankar, G., Smith, I. M., Shen, Y., Walsh, D. M., & Selkoe, D. J.
- Venue
- Archives of Neurology
- Publisher
- American Medical Association (AMA)
- Published
- 2009-02-01
- Volume
- 66
- Issue
- 2
- Pages
- 190-9
- ISSN
- 0003-9942 (ISSN-L)
- OpenAlex
- W2169579980
- Cited by
- 216
- References
- 8
- FWCI
- 12.99
- Type
- journal article
- Language
- en
- Open access
- green
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