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Mol Cell Proteomics. 2014 Oct;13(10):2584-92. doi: 10.1074/mcp.M114.040113. Epub 2014 Jun 27.

Targeting synaptic pathology with a novel affinity mass spectrometry approach.

Author information

1
From the ‡Department of Psychiatry and Neurochemistry, Institute of Neuroscience and Physiology, Sahlgrenska Academy at the University of Gothenburg, S43180 Mölndal, Sweden; ann.brinkmalm@neuro.gu.se.
2
From the ‡Department of Psychiatry and Neurochemistry, Institute of Neuroscience and Physiology, Sahlgrenska Academy at the University of Gothenburg, S43180 Mölndal, Sweden;
3
¶Department of Psychiatry, University of British Columbia, Vancouver V6H3Z6, British Columbia, Canada;
4
‖MRC Toxicology Unit, Hodgkin Building, University of Leicester, LE19HN Leicester, UK;
5
From the ‡Department of Psychiatry and Neurochemistry, Institute of Neuroscience and Physiology, Sahlgrenska Academy at the University of Gothenburg, S43180 Mölndal, Sweden; **UCL Institute of Neurology, Queen Square WC1N3BG, London, UK.

Abstract

We report a novel strategy for studying synaptic pathology by concurrently measuring levels of four SNARE complex proteins from individual brain tissue samples. This method combines affinity purification and mass spectrometry and can be applied directly for studies of SNARE complex proteins in multiple species or modified to target other key elements in neuronal function. We use the technique to demonstrate altered levels of presynaptic proteins in Alzheimer disease patients and prion-infected mice.

PMID:
24973420
PMCID:
PMC4188988
DOI:
10.1074/mcp.M114.040113
[Indexed for MEDLINE]
Free PMC Article

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