Proteomics changes of brain tissues have been described in different
neurodegenerative diseases including
Alzheimer's disease and
Parkinson's disease. However, the brain proteomics of human
prion disease remains less understood. In the study, the proteomics patterns of cortex and cerebellum of brain tissues of
sporadic Creutzfeldt-Jakob disease,
fatal familial insomnia, and G114V genetic CJD were analyzed with isobaric tags for relative and absolute quantitation combined with multidimensional liquid chromatography and MS analysis, with the brains from three normal individuals as controls. Global
protein profiling, significant pathway, and functional categories were analyzed. In total, 2287
proteins were identified with quantitative information both in cortex and cerebellum regions. Cerebellum tissues appeared to contain more up- and down-regulated
proteins (727
proteins) than cortex regions (312
proteins) of
Creutzfeldt-Jakob disease,
fatal familial insomnia, and G114V genetic CJD. Viral
myocarditis,
Parkinson's disease,
Alzheimer's disease, lysosome, oxidative phosphorylation,
protein export, and
drug metabolism-
cytochrome P450 were the most commonly affected pathways of the three kinds of diseases. Almost coincident
biological functions were identified in the brain tissues of the three diseases. In all, data here demonstrate that the brain tissues of
Creutzfeldt-Jakob disease,
fatal familial insomnia, and G114V genetic CJD have obvious proteomics changes at their terminal stages, which show the similarities not only among human
prion diseases but also with other neurodegeneration diseases. This is the first study to provide a reference
proteome map for human
prion diseases and will be helpful for future studies focused on potential
biomarkers for the diagnosis and
therapy of human
prion diseases.