Anti-apoptotic proteins are oxidized by Aβ25-35 in Alzheimer's fibroblasts

Joungil Choi, Christina A. Malakowsky, John M. Talent, Craig C. Conrad, Christopher A. Carroll, Susan T. Weintraub, Robert W. Gracy

Research output: Contribution to journalArticlepeer-review

48 Scopus citations


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 languageEnglish (US)
Pages (from-to)135-141
Number of pages7
JournalBiochimica et Biophysica Acta - Molecular Basis of Disease
Issue number2
StatePublished - Mar 20 2003


  • 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


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