Cited by 1,009Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchPrion Diseases and Protein Misfolding

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Dramatic Aggregation of Alzheimer Aβ by Cu(II) Is Induced by Conditions Representing Physiological Acidosis

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Atwood, Craig S., Moir, Robert D., Huang, Xudong, Scarpa, Richard C., Bacarra, N. Michael E., Romano, Donna M., Hartshorn, Mariana A., Tanzi, Rudolph E., Bush, Ashley I.·1998·Journal of Biological Chemistry

DOI 10.1074/jbc.273.21.12817

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Abstract

The cortical deposition of Abeta is an event that occurs in Alzheimer's disease, Down's syndrome, head injury, and normal aging. Previously, in appraising the effects of different neurochemical factors that impact upon the solubility of Abeta, we observed that Zn2+ was the predominant bioessential metal to induce the aggregation of soluble Abeta at pH 7.4 in vitro and that this reaction is totally reversible with chelation. We now report that unlike other biometals tested at maximal biological concentrations, marked Cu2+-induced aggregation of Abeta1-40 emerged as the solution pH was lowered from 7.4 to 6.8 and that the reaction was completely reversible with either chelation or alkalinization. This interaction was comparable to the pH-dependent effect of Cu2+ on insulin aggregation but was not seen for aprotinin or albumin. Abeta1-40 bound three to four Cu2+ ions when precipitated at pH 7.0. Rapid, pH-sensitive aggregation occurred at low nanomolar concentrations of both Abeta1-40 and Abeta1-42 with submicromolar concentrations of Cu2+. Unlike Abeta1-40, Abeta1-42 was precipitated by submicromolar Cu2+ concentrations at pH 7.4. Rat Abeta1-40 and histidine-modified human Abeta1-40 were not aggregated by Zn2+, Cu2+, or Fe3+, indicating that histidine residues are essential for metal-mediated Abeta assembly. These results indicate that H+-induced conformational changes unmask a metal-binding site on Abeta that mediates reversible assembly of the peptide. Since a mildly acidic e…

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“The avidity with which A β 42 binds Cu(II) [9] and the potency of this reaction in pre-cipitating the peptide as non-ﬁbrillar aggregates [5,10] suggested to us that Cu(II) might be bound by ﬁbril-lar A β 42 and that such an interaction could reverse the β -sheet conformation of the amyloid.”
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Authors: Atwood, C. S., Moir, R. D., Huang, X., Scarpa, R. C., Bacarra, N. M. E., Romano, D. M., Hartshorn, M. A., Tanzi, R. E., & Bush, A. I.
Affiliations: Harvard University (US)
Corresponding author: Bush, Ashley I.
ORCID: Atwood, Craig S.
Moir, Robert D.
Huang, Xudong
Tanzi, Rudolph E.
Bush, Ashley I.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1998-05
Volume: 273
Issue: 21
Pages: 12817-12826
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.273.21.12817
OpenAlex: W2018333394
Cited by: 1,009
References: 97
Citations by year: 2026: 13 · 2025: 15 · 2024: 12 · 2023: 16 · 2022: 14 · 2021: 22 · 2020: 26 · 2019: 28 · 2018: 26 · 2017: 33 · 2016: 24 · 2015: 40 · 2014: 38 · 2013: 39 · 2012: 59
FWCI: 20.04
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 8188 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institute on Aging (1R29AG1268601)
National Cancer Institute
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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
Keywords: amyloid-beta aggregation, copper(II), acidosis, pH-dependent aggregation, Alzheimer's disease, Aβ40, amyloid-beta 42, zinc, histidine residues, metal ion binding, amyloid plaques, metal chelation, inflammation, neurodegeneration
MeSH terms: Acidosis, Alzheimer Disease, Animals, Copper, Humans, Hydrogen-Ion Concentration, Peptide Fragments, Protein Binding, Zinc, Amyloid beta-Peptides, Rats

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Dramatic Aggregation of Alzheimer Aβ by Cu(II) Is Induced by Conditions Representing Physiological Acidosis

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