期刊
PROTEOMICS CLINICAL APPLICATIONS
卷 6, 期 3-4, 页码 201-211出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/prca.201100068
关键词
Alzheimer's disease; Membrane enrichment; Neurodegeneration
资金
- National Institutes of Health through the Emory NINDS [T32NS007480]
- Emory NINDS [NS055077]
- Emory Alzheimer's Disease Research Center [AG025688]
- National Institute of Aging [P01AG1449]
Purpose The present study is a discovery mode proteomics analysis of the membrane-enriched fraction of postmortem brain tissue from Alzheimer's disease (AD) and control cases. This study aims to validate a method to identify new proteins that could be involved in the pathogenesis of AD and potentially serve as disease biomarkers. Experimental design Liquid chromatography-tandem mass spectrometry (LC-MS/MS) was used to analyze the membrane-enriched fraction of human postmortem brain tissue from five AD and five control cases of similar age. Biochemical validation of specific targets was performed by immunoblotting. Results One thousand seven hundred and nine proteins were identified from the membrane-enriched fraction of frontal cortex. Label-free quantification by spectral counting and G-test analysis identified 13 proteins that were significantly changed in disease. In addition to Tau (MAPT), two additional proteins found to be enriched in AD, ubiquitin carboxy-terminal hydrolase 1 (UCHL1), and syntaxin-binding protein 1 (Munc-18), were validated through immunoblotting. Discussion and clinical relevance Proteomic analysis of the membrane-enriched fraction of postmortem brain tissue identifies proteins biochemically altered in AD. Further analysis of this subproteome may help elucidate mechanisms behind AD pathogenesis and provide new sources of biomarkers.
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