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F2‐07‐01: BLOOD AMYLOID‐BETA PREDICTS AMYLOID PET CONVERSION
Author(s) -
Bateman Randall,
Schindler Suzanne E.,
Bollinger James G.,
Ovod Vitaliy,
Mawuenyega Kwasi G.,
Li Yan,
Gordon Brian A.,
Holtzman Dave M.,
Morris John C.,
Benzinger Tammie L.S.,
Xiong Chengjie,
Fagan Anne M.
Publication year - 2019
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.2019.06.4440
Subject(s) - amyloid (mycology) , concordance , medicine , amyloidosis , beta (programming language) , pathology , computer science , programming language
Progressive supranuclear palsy and Lewy body dementia. and performed systematic biochemical analyses which suggest that these oligomers represent disease specific tau oligomeric strains. Finally, we investigated their propagation in vivo by injecting Intravitreally in hTau mice. Results: Our findings suggest that occurrence of soluble aggregates of a-synuclein, Amyloid-b and others, not only synergize with tau and aggravate its toxicity, but also play a role in tau soluble aggerates polymorphism and the formation of oligomeric strains. These distinct tau oligomeric prion-like tau strains can induce different phenotypes. Conclusions: Recent studies of amyloid polymorphisms (strains) and the toxic interactions between amyloidogenic proteins represent important first steps to elucidate the toxic interplay between soluble aggregates and lay the groundwork for the development of multi-panel biomarkers and perhaps more successful therapeutic interventions by targeting multiple candidate and personalized therapeutics.