Redox proteomics and amyloid β-peptide: Insights into Alzheimer disease

Butterfield, D. Allan; Boyd‐Kimball, Debra

doi:10.1111/jnc.14589

Cited by 105Alzheimer's disease research and treatmentsRedox biology and oxidative stressDementia and Cognitive Impairment Research

Redox proteomics and amyloid β-peptide: Insights into Alzheimer disease

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Butterfield, D. Allan, Boyd‐Kimball, Debra·2019·Journal of Neurochemistry

DOI 10.1111/jnc.14589PMC PMC6417976

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Abstract

Alzheimer disease ( AD ) is a progressive neurodegenerative disorder associated with aging and characterized pathologically by the presence of senile plaques, neurofibrillary tangles, and neurite and synapse loss. Amyloid beta‐peptide (1–42) [Aβ(1–42)], a major component of senile plaques, is neurotoxic and induces oxidative stress in vitro and in vivo . Redox proteomics has been used to identify proteins oxidatively modified by Aβ(1–42) in vitro and in vivo . In this review, we discuss these proteins in the context of those identified to be oxidatively modified in animal models of AD , and human studies including familial AD , pre‐clinical AD ( PCAD ), mild cognitive impairment ( MCI ), early AD , late AD , Down syndrome ( DS ), and DS with AD ( DS / AD ). These redox proteomics studies indicate that Aβ(1–42)‐mediated oxidative stress occurs early in AD pathogenesis and results in altered antioxidant and cellular detoxification defenses, decreased energy yielding metabolism and mitochondrial dysfunction, excitotoxicity, loss of synaptic plasticity and cell structure, neuroinflammation, impaired protein folding and degradation, and altered signal transduction. Improved access to biomarker imaging and the identification of lifestyle interventions or treatments to reduce Aβ production could be beneficial in preventing or delaying the progression of AD . image This article is part of the special issue "Proteomics" .

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Altered glucose metabolism is associated with Aβ-mediated lipid peroxidation and protein oxidative damage to glycolytic and mitochondrial enzymes, ion-motive ATPases, opening of voltage-gated Ca2+ channels with Ca2+ elevation in endoplasmic reticulum and mitochondria, and consequent neuronal death.
“evidence was collected for altered glucose metabolism associated with Aβ-mediated lipid peroxidation and protein oxidative damage to glycolytic and mitochondrial enzymes, ion-motive ATPases, the opening of voltage-gated Ca2+ channels with resulting Ca2+ elevation in endoplasmic reticulum and mitochondria, and consequent neuronal death [8,35].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [35]
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The increased activity of MDH could be a compensatory mechanism in response to oxidative damage of other key energy-related proteins, including glycolytic enzymes.
“however, the increased activity could be a compensatory mechanism in response to the oxidative damage of other key energy-related proteins including a number of glycolytic enzymes [35].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [35]
The “Energy Yielding Metabolism and Mitochondrial Dysfunction” section (page unavailable) reports oxidative modification of several glycolytic enzymes and describes MDH’s role in supporting glycolytic activity. It does not report increased MDH activity or propose that such an increase compensates for oxidative damage to other proteins. (LLM, conf=0.83)
Experimental — accuracy not yet measured
Oxidative modification and decreased activity of several key glycolytic enzymes in MCI and AD brain are consistent with the observed glucose hypometabolism.
“Oxidative modification and the decreased activity of several key glycolytic enzymes in MCI and AD brain are consistent with the observed glucose hypometabolism [35].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [35]
The “Energy Yielding Metabolism and Mitochondrial Dysfunction” section (page unavailable) reports oxidative modification of multiple glycolytic enzymes in MCI and AD brain and documents reduced glucose catabolism during AD progression. It proposes that enzyme oxidation could contribute to hypometabolism, but the cited passages do not establish decreased activity of several glycolytic enzymes in MCI and AD brain. (LLM, conf=0.84)
Experimental — accuracy not yet measured
Evidence that oxidative damage is a critical part of AD pathology and progression is compelling.
“The evidence for oxidative damage being a critical component of the pathology and progression of AD is compelling8,11,115.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [115]
Many of the oxidized proteins identified are mitochondrial proteins involved in metabolism, protein synthesis and folding, ROS scavenging, transport, and apoptosis.
“Consistent with the hypothesis that both oxidative stress and mitochondrial dysfunction are early events in the progression of AD [12,35,53], many of the oxidized proteins identified are mitochondrial proteins involved in metabolism, protein synthesis and folding, ROS scavenging, transport, and apoptosis (Table 1).”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [35]

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Reed TT, Sultana R and Butterfield DA (2010) Redox proteomics of oxidatively modified brain proteins in Mild Cognitive Impairment, in Neuroproteomics, (Alzate O ed), CRC Press/Taylor & Frances, Boca Raton. 21882450

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Authors: Butterfield, D. A., & Boyd‐Kimball, D.
Affiliations: University of Kentucky (US)
Department of Chemistry and Biochemistry University of Mount Union Alliance Ohio USA
Corresponding author: Butterfield, D. Allan
ORCID: Butterfield, D. Allan
Venue: Journal of Neurochemistry
Publisher: Wiley
Published: 2018-11-27
Volume: 151
Issue: 4
Pages: 459-487
ISSN: 0022-3042 (ISSN-L)
1471-4159
DOI: 10.1111/jnc.14589
PMC: PMC6417976
OpenAlex: W2889848229
Cited by: 105
References: 315
Citations by year: 2026: 5 · 2025: 4 · 2024: 19 · 2023: 17 · 2022: 15 · 2021: 16 · 2020: 17 · 2019: 11 · 2018: 1
FWCI: 1.48
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: Journal of Neurochemistry (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute on Aging
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: Alzheimer's disease, amyloid-beta, amyloid-beta 42, oxidative stress, redox proteomics, protein oxidation, amyloid plaques, familial Alzheimer's disease, mild cognitive impairment, Down syndrome, mitochondrial dysfunction, neuroinflammation, excitotoxicity, synaptic plasticity, protein folding and degradation, signal transduction, antioxidant defense, biomarkers
MeSH terms: Alzheimer Disease, Animals, Brain, Humans, Oxidation-Reduction, Peptide Fragments, Amyloid beta-Peptides, Oxidative Stress, Disease Progression, Proteomics, Mice

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Redox proteomics and amyloid β-peptide: Insights into Alzheimer disease

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