Proteomic identification of proteins specifically oxidized in Caenorhabditis elegans expressing human Aβ(1–42): Implications for Alzheimer's disease

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 Ca 2+ homeostaisis, and cell death. There is increasing evidence that protein oxidation is involved...

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Bibliographic Details
Published in:Neurobiology of aging 2006-09, Vol.27 (9), p.1239-1249
Main Authors: Boyd-Kimball, Debra, Poon, H. Fai, Lynn, Bert C., Cai, Jian, Pierce Jr, William M., Klein, Jon B., Ferguson, Jmil, Link, Christopher D., Butterfield, D. Allan
Format: Article
Language:English
Subjects:
Alzheimer's disease
Amyloid β-peptide
C. elegans
Caenorhabditis elegans
Protein oxidation
Proteomics
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Summary: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 Ca 2+ 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.
ISSN:0197-4580
1558-1497
DOI:10.1016/j.neurobiolaging.2005.07.001