Redox Proteomics Identification of Oxidatively Modified Brain Proteins in Inherited Alzheimer's Disease: An Initial Assessment

Document Type

Journal Article

Publisher

IOS Press

Faculty

Faculty of Computing, Health and Science

School

School of Exercise, Biomedical and Health Science

RAS ID

4449

Comments

Butterfield, A. , Gnjec, A. , Poon, H., Castegna, A., Pierce, W., Klein, J., & Martins, R. N. (2006). Redox proteomics identification of oxidatively modified brain proteins in inherited Alzheimer's disease: An initial assessment. Journal of Alzheimer's Disease, 10(4), 391-397. Available here

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.

DOI

10.3233/JAD-2006-10407

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Link to publisher version (DOI)

10.3233/JAD-2006-10407