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

Authors

Allan Butterfield, Edith Cowan University
Anastazija Gnjec, Edith Cowan University
Hannah Fai Poon, University of Kentucky, USA
Alessandra Castegna, University of Kentucky, USA
William M. Pierce, University of Louisville, USA
Jon B. Klein, University of Louisville, USA
Ralph Martins, Edith Cowan University

Document Type

Journal Article

Keywords

Redox proteomics, familial Alzheimer's disease, oxidatively modified brain proteins

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.