Characterizing the symmetry of amyloid beta protein retention in Alzheimer's disease using florbetapir positron emission tomography - a study using data from the Alzheimer's disease neuroimaging initiative
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Progression of Alzheimer's disease has been associated with the deposition of aggregated amyloid beta (Aβ) protein in the brain. Though first described in post-mortal tissue, the development of Aβ specific tracers for positron emission tomography (PET) permits in-vivo mapping of its distribution in the brain. One of the well-known and early-developed tracers is the Pittsburgh Compound B (PiB) (Klunk et al., 2004). However, the challenge with PiB lies in the stability of the radioisotope 11C. 11C's short half-life of only 20 minutes hinders its transportation and usage at imaging facilities that are not in close proximity with the radioisotopes manufacturer. Recently, an alternative Aβ tracer has been developed, Florbetapir (Wong et al, 2010.), with a half-life of 110 minutes that should allow wider accessibility to imaging sites while improve the detection of Aβ. To define better the specificity and utility of Florbetapir, we propose to utilize existing PET data acquired with the radioactive tracer Florbetapir from the Alzheimer's disease Neuroimaging Initiative (ADNI). Our goal is to characterize the symmetry of Aβ protein deposition in the brain of patients with Alzheimer's disease. While a previous study has investigated this issue using PiB, Florbetapir has not been used. Our project will involve data post-processing by segmenting out non-brain tissues. Segmented data is then normalized by the pixel intensity and a distribution curve is created using MathCad program. In addition, we will calculate the asymmetry score for Regions of Interest. This will permit comparison of the uptakes of tracer between brain hemispheres to be made. Results from our project can provide insight into Florbetapir's binding affinity for Aβ. In addition, Florbetapir's potential as a better alternative to PiB can also be evaluated.