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Author Notes:

Corresponding Authors: Nicholas T. Seyfried, Departments of Neurology and Biochemistry, nseyfri@emory.edu; Allan I. Levey, Department of Neurology, alevey@emory.edu, and James J. Lah, Department of Neurology, jlah@emory.edu


Research Funding:

Funding was provided through the National Institutes of Health through the Emory NINDS T32 Training in translational neurology grant (T32NS007480), Emory NINDS Neuroscience Core Facilities (NS055077), Emory Alzheimer’s Disease Research Center (AG025688), and National Institute of Aging (P01AG1449).


  • Alzheimer’s disease
  • membrane enrichment
  • proteomics
  • neurodegeneration

Analysis of a membrane enriched proteome from post-mortem human brain tissue in Alzheimer's disease


Journal Title:

Proteomics - Clinical Applications


Volume 6, Number 3-4


, Pages 201-211

Type of Work:

Article | Post-print: After Peer Review


Purpose The present study is a discovery mode proteomics analysis of the membrane enriched fraction of post-mortem 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 post-mortem brain tissue from five AD and five control cases of similar age. Biochemical validation of specific targets was performed by immunoblotting. Results 1709 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 post-mortem brain tissue identifies proteins biochemically altered in AD. Further analysis of this sub-proteome may help elucidate mechanisms behind AD pathogenesis and provide new sources of biomarkers.

Copyright information:

© 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim

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