Cited by 259Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchAluminum toxicity and tolerance in plants and animals

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Metal-associated amyloid-β species in Alzheimer's disease

Pithadia, Amit S, Lim, Mi Hee·2012·Current Opinion in Chemical Biology

DOI 10.1016/j.cbpa.2012.01.016

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Abstract

Highly concentrated metals such as Cu, Zn, and Fe are found in amyloid-β (Aβ) plaques within the brain of Alzheimer's disease (AD). In vitro and in vivo studies have suggested that metal binding to Aβ could facilitate Aβ aggregation and generate reactive oxygen species (ROS), which could contribute to the neuropathogenesis of AD. The connection between metal-Aβ interaction/reactivity and AD development, however, has not been clearly revealed owing to the complexity of the disease. In this review, metal-Aβ interaction/reactivity and its relation to neurotoxicity are briefly discussed. Additionally, our review illustrates the recent progress of small molecules, capable of targeting metal-Aβ species and modulating their interaction/reactivity, which could offer a promising approach to interrogate their role in AD.

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Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
Treatment with a Copper-Zinc Chelator Markedly and Rapidly Inhibits β-Amyloid Accumulation in Alzheimer's Disease Transgenic Mice
Cherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., Barnham, K. J., Volitakis, I., Fraser, F. W., Kim, Y.-S., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00317-8 · Cited by 1,447
Alzheimer's Disease: From Pathology to Therapeutic Approaches
Jakob‐Roetne, R., & Jacobsen, H. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200802808 · Cited by 626
The redox chemistry of the Alzheimer's disease amyloid β peptide
Smith, D. G., Cappai, R., & Barnham, K. J. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.02.002 · Cited by 608
Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide
Faller, P., & Hureau, C. (2009) · Dalton Trans. · doi:10.1039/b813398k · Cited by 530
The chemistry of Alzheimer’s disease
Rauk, A. (2009) · Chemical Society Reviews · doi:10.1039/b807980n · Cited by 417
Alzheimer's disease, metal ions and metal homeostatic therapy
Zatta, P., Drago, D., Bolognin, S., & Sensi, S. L. (2009) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2009.05.002 · Cited by 369
Causes of oxidative stress in Alzheimer disease
Zhu, X., Su, B., Wang, X., Smith, M. A., & Perry, G. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7218-4 · Cited by 336
Medicinal Inorganic Chemistry Approaches to Passivation and Removal of Aberrant Metal Ions in Disease
Scott, L. E., & Orvig, C. (2009) · Chemical Reviews · doi:10.1021/cr9000176 · Cited by 332
Design of small molecules that target metal-Aβ species and regulate metal-induced Aβ aggregation and neurotoxicity
Choi, J.-S., Braymer, J. J., Nanga, R. P. R., Ramamoorthy, A., & Lim, M. H. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1006091107 · Cited by 264
Self-citation

Show all 14 references

Research works printed but not linked: 31

Alzheimer's Association, 2011, Alzheimer's disease facts and figures, Alzheimers Dement, 7, 208, 10.1016/j.jalz.2011.02.004 · DOI
Hardy, 1992, Alzheimer's disease: the amyloid cascade hypothesis, Science, 256, 184, 10.1126/science.1566067 · DOI · Paper page
Wang, 2006, Clearance of amyloid-beta in Alzheimer's disease: progress, problems and perspectives, Drug Discov Today, 11, 931, 10.1016/j.drudis.2006.08.004 · DOI
Kurz, 2011, Amyloid clearance as a treatment target against Alzheimer's disease, J Alzheimers Dis, 24, 61, 10.3233/JAD-2011-102139 · DOI
Maynard, 2005, Metals and amyloid-β in Alzheimer's disease, Int J Exp Pathol, 86, 147, 10.1111/j.0959-9673.2005.00434.x · DOI
Bonda, 2011, Role of metal dyshomeostasis in Alzheimer's disease, Metallomics, 3, 267, 10.1039/c0mt00074d · DOI
Jomova, 2011, Advances in metal-induced oxidative stress and human diseases, Toxicology, 283, 65, 10.1016/j.tox.2011.03.001 · DOI
DeToma, 2012, Misfolded proteins in Alzheimer's disease and type II diabetes, Chem Soc Rev, 41, 608, 10.1039/C1CS15112F · DOI
Burdette, 2003, Meeting of the minds: metalloneurochemistry, Proc Natl Acad Sci USA, 100, 3605, 10.1073/pnas.0637711100 · DOI
Que, 2008, Metals in neurobiology: probing their chemistry and biology with molecular imaging, Chem Rev, 108, 1517, 10.1021/cr078203u · DOI
Bush, 2008, Therapeutics for Alzheimer's disease based on the metal hypothesis, Neurotherapeutics, 5, 421, 10.1016/j.nurt.2008.05.001 · DOI
Frederickson, 2005, The neurobiology of zinc in health and disease, Nat Rev Neurosci, 6, 449, 10.1038/nrn1671 · DOI
Faller, 2009, Copper and zinc binding to amyloid-β: coordination, dynamics, aggregation, reactivity and metal-ion transfer, ChemBioChem, 10, 2837, 10.1002/cbic.200900321 · DOI · Paper page
Gaggelli, 2006, Copper homeostasis and neurodegenerative disorders (Alzheimer's, prion, and Parkinson's diseases and amyothrophic lateral sclerosis), Chem Rev, 106, 1995, 10.1021/cr040410w · DOI · Paper page
Drew, 2011, The heterogeneous nature of Cu2+ interactions with Alzheimer's amyloid-β peptide, Acc Chem Res, 44, 1146, 10.1021/ar200014u · DOI
Karr, 2008, Cu(II) binding to monomeric, oligomeric, and fibrillar forms of the Alzheimer's disease amyloid-β peptide, Biochemistry, 47, 5006, 10.1021/bi702423h · DOI
Dorlet, 2009, Pulse EPR spectroscopy reveals the coordination sphere of copper(II) ions in the 1–16 amyloid-β peptide: a key role of the first two N-terminus residues, Angew Chem Int Ed, 48, 9273, 10.1002/anie.200904567 · DOI
Shearer, 2008, The amyloid-β peptide of Alzheimer's disease binds CuI in a linear bis-His coordination environment: insight into a possible neuroprotective mechanism for the amyloid-β peptide, J Am Chem Soc, 130, 17826, 10.1021/ja805940m · DOI
Himes, 2008, Structural studies of copper(I) complexes of amyloid-β peptide fragments: formation of two-coordinate bis(histidine) complexes, Angew Chem Int Ed, 47, 9084, 10.1002/anie.200803908 · DOI
Shearer, 2010, Cu K-edge X-ray absorption spectroscopy reveals differential copper coordination within amyloid-β oligomers compared to amyloid-β monomers, Chem Commun, 46, 9137, 10.1039/c0cc02446e · DOI
Feaga, 2011, Affinity of Cu+ for the copper-binding domain of amyloid-β peptide of Alzheimer's disease, Inorg Chem, 50, 1614, 10.1021/ic100967s · DOI
Bousejra-ElGarah, 2011, Iron(II) binding to amyloid-β, the Alzheimer's peptide, Inorg Chem, 50, 9024, 10.1021/ic201233b · DOI
Noy, 2008, Zinc-amyloid β interactions on a millisecond time-scale stabilize non-fibrillar Alzheimer-related species, J Am Chem Soc, 130, 1376, 10.1021/ja076282l · DOI
Chen, 2011, Distinct effects of Zn2+, Cu2+, Fe3+, and Al3+ on amyloid-β stability, oligomerization, and aggregation, J Biol Chem, 286, 9646, 10.1074/jbc.M110.177246 · DOI
Pramanik, 2011, Active site environment of heme-bound amyloid β peptide associated with Alzheimer's disease, J Am Chem Soc, 133, 81, 10.1021/ja1084578 · DOI
Atamna, 2006, Amyloid-β peptide binds with heme to form a peroxidase: relationship to the cytopathologies of Alzheimer's disease, Proc Natl Acad Sci USA, 103, 3381, 10.1073/pnas.0600134103 · DOI
Atamna, 2006, Heme binding to amyloid β peptide: mechanistic role in Alzheimer's disease, J Alzheimers Dis, 10, 255, 10.3233/JAD-2006-102-310 · DOI
Adlard, 2008, Rapid restoration of cognition in Alzheimer's transgenic mice with 8-hydroxy quinoline analogs is associated with decreased interstitial Aβ, Neuron, 59, 43, 10.1016/j.neuron.2008.06.018 · DOI · Paper page
Kung, 2001, Novel stilbenes as probes for amyloid plaques, J Am Chem Soc, 123, 12740, 10.1021/ja0167147 · DOI
Ono, 2004, Curcumin has potent anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro, J Neurosci Res, 75, 742, 10.1002/jnr.20025 · DOI · Paper page
Wu, 2008, Sequestration of copper from β-amyloid promotes selective lysis by cyclen-hybrid cleave agents, J Biol Chem, 283, 31657, 10.1074/jbc.M804722200 · DOI

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“E C metals such as Fe, Cu, and Zn play important roles in Aβ aggregate deposition [11,16–19] and neurotoxicity as well as inducing formation of reactive oxygen species (ROS) [20–23].”
Background
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“Metal ion dyshomeostasis is a well-acknowledged feature of AD [90].”
Background
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Self-citation

Authors: Pithadia, A. S., & Lim, M. H.
Affiliations: University of Michigan (US)
Corresponding author: Lim, Mi Hee
ORCID: Lim, Mi Hee
Venue: Current Opinion in Chemical Biology
Publisher: Elsevier BV
Published: 2012-04
Volume: 16
Issue: 1-2
Pages: 67-73
ISSN: 1367-5931 (ISSN-L)
DOI: 10.1016/j.cbpa.2012.01.016
OpenAlex: W1984223653
Cited by: 259
References: 48
Citations by year: 2026: 3 · 2025: 12 · 2024: 10 · 2023: 14 · 2022: 11 · 2021: 17 · 2020: 21 · 2019: 28 · 2018: 30 · 2017: 25 · 2016: 16 · 2015: 18 · 2014: 26 · 2013: 20 · 2012: 8
FWCI: 2.48
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Current Opinion in Chemical Biology (publishedVersion)
PubMed (publishedVersion)
Scholarworks@UNIST (Ulsan National Institute of Science and Technology) (submittedVersion)
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 › Agricultural and Biological Sciences › Plant Science › Aluminum toxicity and tolerance in plants and animals
Keywords: Alzheimer's disease, amyloid-beta, metal ion binding, copper, zinc, iron, amyloid plaques, amyloid-beta aggregation, reactive oxygen species, neurotoxicity, metal chelators
MeSH terms: Alzheimer Disease, Amyloid, Humans, Metals, Reactive Oxygen Species

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Metal-associated amyloid-β species in Alzheimer's disease

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