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Amyloid tracers binding sites in autosomal dominant and sporadic Alzheimer's disease
Author(s) -
Ni Ruiqing,
Gillberg PerGöran,
Bogdanovic Nenad,
Viitanen Matti,
Myllykangas Liisa,
Nennesmo Inger,
Långström Bengt,
Nordberg Agneta
Publication year - 2017
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.2016.08.006
Subject(s) - alzheimer's disease , disease , amyloid (mycology) , neuroscience , medicine , pathology , biology
Amyloid imaging has been integrated into diagnostic criteria for Alzheimer's disease (AD). How amyloid tracers binding differ for different tracer structures and amyloid‐β aggregates in autosomal dominant AD (ADAD) and sporadic AD is unclear. Methods Binding properties of different amyloid tracers were examined in brain homogenates from six ADAD with APPswe , PS1 M146V , and PS1 EΔ9 mutations, 13 sporadic AD, and 14 control cases. Results 3 H‐PIB, 3 H‐florbetaben, 3 H‐AZD2184, and BTA‐1 shared a high‐ and a varying low‐affinity binding site in the frontal cortex of sporadic AD. AZD2184 detected another binding site (affinity 33 nM) in the frontal cortex of ADAD. The 3 H‐AZD2184 and 3 H‐PIB binding were significantly higher in the striatum of ADAD compared to sporadic AD and control. Polyphenol resveratrol showed strongest inhibition on 3 H‐AZD84 binding followed by 3 H‐florbetaben and minimal on 3 H‐PIB. Discussion This study implies amyloid tracers of different structures detect different sites on amyloid‐β fibrils or conformations.