Proteomic identification of HNE-bound proteins in early Alzheimer disease: Insights into the role of lipid peroxidation in the progression of AD
Abstract
Early Alzheimer's disease (EAD) is the intermediary stage between mild cognitive impairment (MCI) and late-stage Alzheimer's disease (AD). The symptoms of EAD mirror the disease advancement between the two phases. Dementia, memory deficits, and cognitive decline are more pronounced as the disease progresses. Oxidative stress in brain is reported in MCI and AD, including lipid peroxidation indexed by protein-bound 4-hydroxy-2-nonenal (HNE). There are limited data regarding the proteomics analysis of brain from subjects with EAD and even less concerning the possible relationship of EAD HNE-modified brain proteins with HNE-modified proteins in MCI and AD. Proteomics was utilized to investigate excessively HNE-bound brain proteins in EAD compared to those in control. These new results provide potentially valuable insight into connecting HNE-bound brain proteins in EAD to those previously identified in MCI and AD, since EAD is a transitional stage between MCI and late-stage AD. In total, six proteins were found to be excessively covalently bound by HNE in EAD inferior parietal lobule (IPL) compared to age-related control brain. These proteins play roles in antioxidant defense (manganese superoxide dismutase), neuronal communication and neurite outgrowth (dihydropyriminidase-related protein 2), and energy metabolism (alpha-enolase, malate dehydrogenase, triosephosphate isomerase, and F1 ATPase, alpha subunit). This study shows that there is an overlap of brain proteins in EAD with previously identified oxidatively modified proteins in MCI and late-stage AD. The results are consistent with the hypothesis that oxidative stress, in particular lipid peroxidation, is an early event in the progression of AD, and is the first to identify in EAD identical brain proteins previously identified as HNE-modified in MCI and late-state AD.
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MDH is oxidatively modified by HNE in early AD inferior parietal lobule and its carbonylation is induced by Aβ in vitro and in vivo.
“MDH is oxidatively modified by HNE in early AD inferior parietal lobule (IPL) [55] and its carbonylation is induced by Aβ in vitro and in vivo [63,65,66].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [55]
The activities of LDH, aconitase, and ATP synthase are significantly decreased as a result of oxidation.
“The activities of LDH, aconitase, and ATP synthase are significantly decreased as a result of oxidation [54,55,56,61]”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [55]
ATP synthase is carbonylated in vivo by Aβ, significantly modified by HNE in MCI hippocampus and IPL, early AD IPL, and late AD IPL, and significantly nitrated in late AD hippocampus.
“The carbonylation of ATP synthase is induced in vivo by Aβ [73], and it is significantly modified by HNE in MCI hippocampus and IPL [56], early AD IPL [55], and late AD IPL [54] in addition to being significantly nitrated in late AD hippocampus [57].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [55]
The activity of MDH is significantly increased.
“however, the activity of MDH is significantly increased [55].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [55]
MnSOD is oxidatively modified by HNE in early AD IPL, resulting in a significant decrease in enzyme activity.
“MnSOD is oxidatively modified by HNE in early AD IPL, resulting in a significant decrease in enzyme activity [55]”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [55]
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- Authors
- Reed, T. T., Pierce, W. M., Markesbery, W. R., & Butterfield, D. A.
- Affiliations
- University of Kentucky (US)
- University of Louisville (US)
- Corresponding author
- Butterfield, D. Allan
- Venue
- Brain Research
- Publisher
- Elsevier BV
- Published
- 2009-06
- Volume
- 1274
- Pages
- 66-76
- ISSN
- 0006-8993 (ISSN-L)
- OpenAlex
- W2076534507
- Cited by
- 190
- References
- 79
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 1 · 2023: 8 · 2022: 7 · 2021: 13 · 2020: 12 · 2019: 9 · 2018: 11 · 2017: 8 · 2016: 14 · 2015: 13 · 2014: 14 · 2013: 16 · 2012: 16
- FWCI
- 13.03
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Brain Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (AG-0288383, P01AG010836, P01AG005119, AG 10836, AG0 5119)
- Topics
- Health Sciences › Medicine › Physiology › 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 › Redox biology and oxidative stress
- Keywords
- early Alzheimer's disease, 4-hydroxynonenal, lipid peroxidation, oxidative stress, protein oxidation, brain proteomics, inferior parietal lobule, manganese superoxide dismutase, alpha-enolase, malate dehydrogenase, triosephosphate isomerase, F1-ATPase, antioxidant defense, energy metabolism, neural communication, disease progression
- MeSH terms
- Aged, Aged, 80 and over, Aldehydes, Alzheimer Disease, Brain, Female, Humans, Male, Proteins, Blotting, Western, Lipid Peroxidation, Oxidative Stress, Disease Progression, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Proteomics
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Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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