Abstract
We have examined the effects of the beta-amyloid peptide (Aβ25-35) on fibroblasts derived from subjects with Alzheimer's disease (AD) and from age-matched controls. The peptide was significantly more cytotoxic to the AD-derived fibroblasts. The level of protein oxidation was also greater in the cells from AD subjects. Two-dimensional electrophoresis (2-DE) coupled with immunostaining for protein carbonylation revealed specific oxidation-sensitive proteins (OSPs) in both the control and AD-derived cells. Two specific OSPs were identified by mass spectrometry as heat shock protein 60 (HSP 60) and vimentin. Exposure of the cells to Aβ25-35 resulted in a twofold increase in the level of oxidation of these two OSPs in the cells derived from controls, but a ninefold increase in their level of oxidation in the fibroblasts from AD subjects. These observations are of particular interest because of the proposed anti-apoptotic roles of both HSP 60 and vimentin and our recent observation that these same two proteins are particularly susceptible to oxidation in neuronally derived cells.
Original language | English (US) |
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Pages (from-to) | 135-141 |
Number of pages | 7 |
Journal | Biochimica et Biophysica Acta - Molecular Basis of Disease |
Volume | 1637 |
Issue number | 2 |
DOIs | |
State | Published - Mar 20 2003 |
Keywords
- Alzheimer's disease
- Anti-apoptotic protein
- Heat shock protein 60
- Protein oxidation
- Two-dimensional gel electrophoresis
- Vimentin
ASJC Scopus subject areas
- Molecular Medicine
- Molecular Biology