Literature DB >> 17183150

Redox proteomics identification of oxidatively modified brain proteins in inherited Alzheimer's disease: an initial assessment.

D Allan Butterfield1, Anastazija Gnjec, H Fai Poon, Alessandra Castegna, William M Pierce, Jon B Klein, Ralph N Martins.   

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), gamma-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.

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Year:  2006        PMID: 17183150     DOI: 10.3233/jad-2006-10407

Source DB:  PubMed          Journal:  J Alzheimers Dis        ISSN: 1387-2877            Impact factor:   4.472


  43 in total

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6.  Redox proteomics identification of 4-hydroxynonenal-modified brain proteins in Alzheimer's disease: Role of lipid peroxidation in Alzheimer's disease pathogenesis.

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Review 8.  Neuroproteomics as a promising tool in Parkinson's disease research.

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Review 10.  Amyloid β-peptide (1-42)-induced oxidative stress in Alzheimer disease: importance in disease pathogenesis and progression.

Authors:  D Allan Butterfield; Aaron M Swomley; Rukhsana Sultana
Journal:  Antioxid Redox Signal       Date:  2013-02-14       Impact factor: 8.401

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