Oxidative stress in Alzheimer's disease brain: New insights from redox proteomics
Abstract
Alzheimer's disease, an age-related neurodegenerative disorder, is characterized clinically by a progressive loss of memory and cognitive functions. Neuropathologically, Alzheimer's disease is defined by the accumulation of extracellular amyloid protein deposited senile plaques and intracellular neurofibrillary tangles made of abnormal and hyperphosphorylated tau protein, regionalized neuronal death, and loss of synaptic connections within selective brain regions. Evidence has suggested a critical role for amyloid-beta peptide metabolism and oxidative stress in Alzheimer's disease pathogenesis and progression. Among the other indices of oxidative stress in Alzheimer's disease brain are protein carbonyls and 3-nitrotyrosine, which are the markers of protein oxidation. Thus, in this review, we discuss the application of redox proteomics for the identification of oxidatively modified proteins in Alzheimer's disease brain and also discuss the functions associated with the identified oxidized proteins in relation to Alzheimer's disease pathology. The information obtained from proteomics may be helpful in understanding the molecular mechanisms involved in the development and progression of Alzheimer's disease as well as of other neurodegenerative disorders. Further, redox proteomics may provide potential targets for drug therapy in Alzheimer's disease.
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Nitro-oxidative modifications to mitochondrial proteins are associated with pathological changes in mitochondrial redox state, morphology, and bioenergetics in preclinical and early AD patients.
“Nitro-oxidative modifications to mitochondrial proteins are associated with pathological changes in mitochondrial redox state, morphology, and bioenergetics in preclinical and early AD patients”
From The mitochondria-targeted antioxidant MitoQ prevents loss of spatial memory retention and early neuropathology in a transgenic mouse model of Alzheimer’s disease (2011) · cites this paper as Butterfield et al., 2006
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- Authors
- Butterfield, D. A., Perluigi, M., & Sultana, R.
- Affiliations
- University of Kentucky (US)
- Corresponding author
- Butterfield, D. Allan
- Venue
- European Journal of Pharmacology
- Publisher
- Elsevier BV
- Published
- 2006-09
- Volume
- 545
- Issue
- 1
- Pages
- 39-50
- ISSN
- 0014-2999 (ISSN-L)
- OpenAlex
- W2154798120
- Cited by
- 363
- References
- 7
- Citations by year
- 2026: 5 · 2025: 8 · 2024: 7 · 2023: 7 · 2022: 8 · 2021: 14 · 2020: 20 · 2019: 11 · 2018: 12 · 2017: 8 · 2016: 17 · 2015: 17 · 2014: 32 · 2013: 27 · 2012: 31
- FWCI
- 3.28
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- European Journal of Pharmacology (publishedVersion)
- PubMed (publishedVersion)
- IRIS Research product catalog (Sapienza University of Rome) (submittedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (P01AG010836, P01AG005119, AG 10836, AG0 5119)
- 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, oxidative stress, redox proteomics, oxidized proteins, protein carbonyls, nitrotyrosine, amyloid-beta, tau hyperphosphorylation, neurofibrillary tangles, amyloid plaques, neurodegeneration, therapeutic target
- MeSH terms
- Actins, Alzheimer Disease, Humans, Hydrogen-Ion Concentration, Mitochondria, Nerve Tissue Proteins, Oxidation-Reduction, Phosphorylation, Mass Spectrometry, Synapses, Electrophoresis, Gel, Two-Dimensional, Neurites, tau Proteins, Long-Term Potentiation, Oxidative Stress, Proteome, Intercellular Signaling Peptides and Proteins, Proteomics, Ubiquitin Thiolesterase, Proteasome Endopeptidase Complex, Phosphatidylethanolamine Binding Protein
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