Proteomic identification of proteins specifically oxidized in Caenorhabditis elegans expressing human Aβ(1-42): Implications for Alzheimer’s Disease
Abstract
Protein oxidation has been shown to lead to loss of protein function, increased protein aggregation, decreased protein turnover, decreased membrane fluidity, altered cellular redox poteintial, loss of Ca2+ homeostaisis, and cell death. There is increasing evidence that protein oxidation is involved in the pathogenesis of Alzheimer's disease and amyloid beta-peptide (1-42) has been implicated as a mediator of oxidative stress in AD. However, the specific implications of the oxidation induced by Abeta(1-42) on the neurodegeneration evident in AD are unknown. In this study, we used proteomic techniques to identify specific targets of oxidation in transgenic Caenorhabditis elegans (C. elegans) expressing human Abeta(1-42). We identified 16 oxidized proteins involved in energy metabolism, proteasome function, and scavenging of oxidants that are more oxidized compared to control lines. These results are discussed with reference to Alzheimer's disease.
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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 [66]
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- Authors
- Boyd-Kimball, D., Poon, H. F., Lynn, B. C., Cai, J., Pierce Jr., W. M., Klein, J. B., Ferguson, J., Link, C. D., & Butterfield, D. A.
- Affiliations
- University of Kentucky (US)
- University of Louisville (US)
- University of Colorado Boulder (US)
- Corresponding author
- Butterfield, D. Allan
- Venue
- Neurobiology of Aging
- Publisher
- Elsevier BV
- Published
- 2006-09
- Volume
- 27
- Issue
- 9
- Pages
- 1239-1249
- ISSN
- 0197-4580 (ISSN-L)
- OpenAlex
- W2167590630
- Cited by
- 98
- References
- 58
- Citations by year
- 2024: 2 · 2023: 2 · 2022: 2 · 2021: 4 · 2020: 3 · 2019: 4 · 2018: 4 · 2017: 1 · 2016: 2 · 2015: 5 · 2014: 4 · 2013: 8 · 2012: 7
- FWCI
- 5.79
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neurobiology of Aging (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (P01AG010836, P01AG005119, AG21037, R01AG021037, AG 10836, AG12423, AG0 5119, R01AG012423)
- 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
- protein oxidation, amyloid-beta, Alzheimer's disease, Caenorhabditis elegans, transgenic Caenorhabditis elegans, oxidative stress, oxidized proteins, energy metabolism, proteasome function, antioxidant scavenging, neurodegeneration, protein aggregation
- MeSH terms
- Analysis of Variance, Animals, Humans, Oxidation-Reduction, Peptide Fragments, Mass Spectrometry, Blotting, Western, Electrophoresis, Gel, Two-Dimensional, Gene Expression, Amyloid beta-Peptides, Caenorhabditis elegans, Oxidative Stress, Sequence Analysis, Protein, Caenorhabditis elegans Proteins, Animals, Genetically Modified, Proteomics
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