Abstract #3371
Chemical Exchange Saturation Transfer on a prototype model of neurodegeneration.
Eleni Demetriou 1 , Andreia C Silva 1 , Marilena Rega 1 , Francisco Torrealdea 1 , James E M Fairney 1,2 , Mohamed Tachrount 1 , Mark Farrow 3 , and Xavier Golay 1
1
Brain repair and rehabilitation, Institute
of Neurology, London, United Kingdom,
2
Medical
Physics &Biomedical engineering, University College of
London, London, United Kingdom,
3
MRC
prion unit, UCL Institute of Neurology, London, United
Kingdom
In this study, we apply Chemical Exchange Saturation
Transfer (CEST) to examine changes related to protein
folding and aggregation occurring in a terminal mouse
model of prion disease. A trend towards increased amide
proton transfer in the Prion mice was found in the
cortex and basal ganglia but was not statistically
significant .However, this was also accompanied by a
significant reduction found in the magnetization
transfer asymmetry at 10μT power in both basal ganglia
and cortex of the diseased animals, suggestive of
changes happening in the local proteasome possibly
indicating cell death at this late stage of this
disease, in addition to a reduced number of exposed
amine groups due to PrP misfolding.
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