Redox proteomics identification of oxidatively modified brain proteins in inherited Alzheimer's disease

An initial assessment

D. Allan Butterfield*, Anastazija Gnjec, H. Fai Poon, Alessandra Castegna, William M. Pierce, Jon B. Klein, Ralph N. Martins

*Corresponding author for this work

Research output: Contribution to journalArticle

96 Citations (Scopus)

Abstract

Objective: To identify oxidatively modified proteins in brains of persons with inherited Alzheimer's disease. Methods: Redox proteomics was used to identify oxidatively modified brain proteins in persons with mutations in the genes for presenilin-1 (PS-1). Results: An initial redox proteomics assessment of oxidatively modified proteins from brains of individuals with PS-1 mutations was performed. These PS1 mutations, Q222H and M233T, are completely penetrant causing early-onset familial AD as previously reported in these Australian families. We show that oxidative modifications of ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1), γ-enolase, actin, and dimethylarginine dimethylaminohydrolase 1 (DMDMAH-1) are present in the brain of familial AD subjects. Conclusions: These initial results suggest that oxidatively modified proteins are important common features in both familial and sporadic AD.

Original languageEnglish
Pages (from-to)391-397
Number of pages7
JournalJournal of Alzheimer's Disease
Volume10
Issue number4
Publication statusPublished - 2006
Externally publishedYes

Keywords

  • Familial Alzheimer's disease
  • Oxidatively modified brain proteins
  • Redox proteomics

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