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P1‐011: SUBJECTIVE MEMORY COMPLAINTS, CORTICAL THINNING, AND COGNITIVE DYSFUNCTION IN MIDDLE‐AGED ADULTS AT RISK FOR AD: FINDINGS FROM THE WISCONSIN REGISTRY FOR ALZHEIMER'S PREVENTION
Author(s) -
Schultz Stephanie,
Oh Jennifer,
Koscik Rebecca L.,
Dowling N. Maritza,
Gallagher Catherine,
Carlsson Cynthia,
Bendlin Barbara B.,
LaRue Asenath,
Hermann Bruce,
Rowley Howard,
Asthana Sanjay,
Sager Mark A.,
Johnson Sterling,
Okonkwo Ozioma
Publication year - 2014
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2014.05.246
Subject(s) - cognition , neuropsychology , psychology , posterior cingulate , cohort , cognitive decline , effects of sleep deprivation on cognitive performance , memory clinic , medicine , audiology , dementia , neuroscience , cognitive impairment , disease
Background: In vivo tau imaging would be useful for early and differential diagnosis of neurodegenerative diseases 18 F-THK5117 is a PET tracer which binds to tau pathology in Alzheimer’s disease (AD) brain with high affinity and selectivity. However, the binding ability of 18 F-THK5117 to tau lesions in non-AD brains has not been fully investigated. In this study, the binding ability of THK5117 to several forms of protein aggregates were evaluated using the brain sections from various non-AD neurodegenerative diseases. Methods: Postmortem brain sections from AD, tangle-predominant senile dementia (TPSD), corticobasal degeneration (CBD), progressive supranuclear palsy (PSP), frontotemporal lobar degeneration (FTLD), and dementia with Lewy bodies (DLB) were used for this study. Binding ability of THK5117 to protein deposits was evaluated by autofluorescence staining and autoradiography. Brain sections were additionally immunostained with tau, A b, a -synuclein, and TDP-43 antibodies. Results: Neurofibrillary tangles in the brain sections from TPSD as well as AD were clearly labeled with THK5117. In AD brain sections, THK5117 bound to both 3 repeat and 4 repeat tau lesions. In CBD brain sections, THK5117 intensely labeled argyrophilic threads and coiled bodies containing 4 repeat tau. THK5117 additionally labeled tau lesions in PSP brain sections. However, THK5117 failed to label the inclusion bodies of tau in FTLD, senile plaques, Lewy bodies, and TDP-43 deposits. Conclusions: THK5117 labels a certain forms of tau protein deposits in non-AD tauopathies. These binding were independent of tau isoforms and may depend on the protein conformation.