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conferenceseries
.com
Volume 7, Issue 4 (Suppl)
J Clin Exp Pathol, an open access journal
ISSN: 2161-0681
Euro Pathology 2017
August 02-03, 2017
13
th
EUROPEAN PATHOLOGY CONGRESS
August 02-03, 2017 Milan, Italy
Peering into the iron window of Alzheimer’s disease MR imaging and pathophysiology
Jonathan J Wisco
Brigham Young University, USA
T
he severity of pathological protein deposition and concomitant iron presence distinguishes neurological disorders. Tissues
with high amounts of protein or iron deposits have a characteristically rapid T2* MRI signal decay. Therefore, these
tissue components do not appear on traditional MRI, as the NMR signal has already gone through multiple time constants
of decay before any signal can be acquired. Ultra-short Echo Time (UTE) imaging, however, significantly reduces the time
between the appearance of an NMR signal and its sampling, allowing for the measurement of iron-related pathology. We
used a novel UTE sequence with a 3D cones k-space trajectory in a 3T Siemens scanner to image short T2* tissues in the
amygdala and hippocampus in
ex vivo
, 20 mm thick coronal human brain slabs, each with known Alzheimer’s disease (AD)
Braak VI tauopathy or with cerebrovascular disease (CVD). We quantified the MR signal from tissues with T2* values of
less than 1 ms at TEs of 0.25, 0.5, 0.8, 1.0, 2.0, 3.0, and 5.0 ms and TR of 12.1 ms (1 mm ISO, FA=15 degree, FOV=15 cm
2
).
Different images were then formed by subtracting the TE=5 ms images from the images acquired at the other TEs, effectively
suppressing longer T2* tissues. T2* value in the AD amygdala and hippocampus as 4.8+/-1.9 ms (mean+/-SD), and T2* values
in anatomically matching regions of the CVD brain was 2.2+/-1.1 ms. We analyzed tissue sections in these regions for the
presence of Abeta-42, tau, and CD-68 immunohistochemical reactivity, and enhanced Perl’s staining. We noted that the T2*
signal decreased with the additive presence of amyloid plaques, tau tangles, non-heme iron, and activated microglia. UTE
imaging may be a feasible method to visualize iron-related protein pathology. Future work will further examine the individual
contributions of pathological proteins, non-heme iron, and inflammation to the T2* decay.
Biography
Jonathan J Wisco is an Associate Professor and Director of the Laboratory for Translational Anatomy of Degenerative Disease and Developmental Disorders,
College of Life Sciences, Department of Physiology and Developmental Biology, and Neuroscience Center at Brigham Young University, Provo, UT. He is also
an Associate Director of the BYU MRI Research Facility. He holds an Adjunct Associate Professor position in the Department of Neurobiology and Anatomy at
University of Utah School of Medicine, USA.
jjwisco@byu.eduJonathan J Wisco, J Clin Exp Pathol 2017, 7:4(Suppl)
DOI: 10.4172/2161-0681-C1-037