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 Aβ(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 Aβ(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.
Original language | English |
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Pages (from-to) | 1239-1249 |
Number of pages | 11 |
Journal | Neurobiology of Aging |
Volume | 27 |
Issue number | 9 |
DOIs | |
State | Published - Sep 2006 |
Bibliographical note
Funding Information:This work was supported in part by NIH grants to D.A.B. [AG-05119; AG-10836] and C.D.L [AG12423, AG21037]. We are indebted to Creg Darby for providing the XA1440 strain.
Keywords
- Alzheimer's disease
- Amyloid β-peptide
- C. elegans
- Protein oxidation
- Proteomics
ASJC Scopus subject areas
- General Neuroscience
- Aging
- Clinical Neurology
- Developmental Biology
- Geriatrics and Gerontology