Cited by 2,120Alzheimer's disease research and treatmentsTrace Elements in HealthDementia and Cognitive Impairment Research

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Copper, iron and zinc in Alzheimer's disease senile plaques

Lovell, M.A, Robertson, J.D, Teesdale, W.J, Campbell, J.L, Markesbery, W.R·1998·Journal of the Neurological Sciences

DOI 10.1016/s0022-510x(98)00092-6

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Abstract

Concentrations of copper (Cu), iron (Fe) and zinc (Zn) were measured in the rims and cores of senile plaques (SP) and in the neuropil of the amygdala of nine Alzheimer's disease (AD) patients and in the neuropil of the amygdala of five neurologically normal control subjects using micro particle-induced X-ray emission (micro-PIXE). Comparison of SP rim and core values revealed no significant differences between levels of Cu, Fe or Zn. Zinc and Fe in SP rims and cores were significantly elevated in AD compared with AD neuropil (P<0.05). Copper was significantly elevated (P<0.05) in the rim of SP compared with AD neuropil. Comparison of AD and control neuropil revealed a significant (P<0.05) elevation of Zn in AD subjects. The elevation of these elements in SP in AD is of interest in light of the observation that Cu, Fe and particularly Zn, can accelerate aggregation of amyloid beta peptide.

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Clinical diagnosis of Alzheimer's disease: Report of the NINCDS‐ADRDA Work Group* under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease
McKhann, G., Drachman, D., Folstein, M., Katzman, R., Price, D., & Stadlan, E. M. (1984) · Neurology · doi:10.1212/wnl.34.7.939 · Cited by 27,915
The Consortium to Establish a Registry for Alzheimer's Disease (CERAD): Part II. Standardization of the neuropathologic assessment of Alzheimer's disease
Mirra, S. S., Heyman, A., McKeel, D., Sumi, S. M., Crain, B. J., Brownlee, L. M., Vogel, F. S., Hughes, J. P., Belle, G. V., Berg, L., et al. (1991) · Neurology · doi:10.1212/wnl.41.4.479 · Cited by 4,961
Consortium to Establish a Registry for Alzheimer's Disease (CERAD)
Fillenbaum, G., & Heyman, A. (2002) · doi:10.1002/0470846410.ch42(iii · Cited by 2,859
Diagnosis of Alzheimer's Disease
Khachaturian, Z. S. (1985) · Archives of Neurology · doi:10.1001/archneur.1985.04060100083029 · Cited by 2,499
Oxidative stress hypothesis in Alzheimer’s disease
Markesbery, W. R. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00629-6 · Cited by 2,383
Self-citation
Prevalence of Alzheimer's disease in a community population of older persons. Higher than previously reported
Evans, D. A. (1989) · JAMA · doi:10.1001/jama.262.18.2551 · Cited by 1,627
Rapid induction of Alzheimer A beta amyloid formation by zinc
Bush, A., Pettingell, W., Multhaup, G., d Paradis, M., Vonsattel, J., Gusella, J., Beyreuther, K., Masters, C., & Tanzi, R. (1994) · Science · doi:10.1126/science.8073293 · Cited by 1,522
Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease.
Smith, C. D., Carney, J. M., Starke-Reed, P. E., Oliver, C. N., Stadtman, E. R., Floyd, R. A., & Markesbery, W. R. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.23.10540 · Cited by 1,296
Self-citation
Release of endogenous Zn2+ from brain tissue during activity
Assaf, S. Y., & Chung, S. (1984) · Nature · doi:10.1038/308734a0 · Cited by 1,113
A model for beta-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease.
Hensley, K., Carney, J. M., Mattson, M. P., Aksenova, M., Harris, M., Wu, J. F., Floyd, R. A., & Butterfield, D. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.8.3270 · Cited by 1,086

Show all 72 references

Research works printed but not linked: 3

Ben-Shachar, 1987, Dopamine D2 receptor modulation by brain non-haem iron, Br J Pharmacol, 90, 2P
Hess, 1974, Chronische Bleivergiftung. Praxis, 63, 177
Markesbery WR, Ehmann WD. Brain trace elements in Alzheimer disease. In: Terry RD, Katzman R, Bick KL, editors. Alzheimer disease. New York: Raven Press, 1994:353–67.

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Amyloid-Beta (Aβ) D7H Mutation Increases Oligomeric Aβ42 and Alters Properties of Aβ-Zinc/Copper Assemblies
Chen, W.-T., Hong, C., Lin, Y.-T., Chang, W.-H., Huang, H.-T., Liao, J., Chang, Y.-J., Hsieh, Y.-F., Cheng, C.-Y., Liu, H.-C., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035807 · Cited by 119
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Migliorini, C., Porciatti, E., Łuczkowski, M., & Valensin, D. (2011) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2011.07.004 · Cited by 117
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Authors: Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R.
Affiliations: University of Kentucky (US)
University of Guelph (CA)
ORCID: Lovell, M.A
Robertson, J.D
Venue: Journal of the Neurological Sciences
Publisher: Elsevier BV
Published: 1998-06
Volume: 158
Issue: 1
Pages: 47-52
ISSN: 0022-510X (ISSN-L)
DOI: 10.1016/s0022-510x(98)00092-6
OpenAlex: W2083500052
Cited by: 2,120
References: 72
Citations by year: 2026: 38 · 2025: 52 · 2024: 69 · 2023: 82 · 2022: 100 · 2021: 92 · 2020: 95 · 2019: 103 · 2018: 80 · 2017: 94 · 2016: 87 · 2015: 82 · 2014: 89 · 2013: 96 · 2012: 116
FWCI: 18.64
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Journal of the Neurological Sciences (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute on Aging (2-PO1-AG05119, P01AG005119, 5-P50 AG0514)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: Alzheimer's disease, amyloid plaques, copper, iron, zinc, trace elements, amygdala, amyloid-beta aggregation, neuropil
MeSH terms: Alzheimer Disease, Amygdala, Copper, Humans, Iron, Spectrometry, X-Ray Emission, Zinc, Neuropil, Biotinylation, Plaque, Amyloid

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Copper, iron and zinc in Alzheimer's disease senile plaques

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