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O2‐06‐05: Synaptic activity reduces intraneuronal Aβ, alters APP transport and protects against Alzheimer's disease‐like synaptic alterations
Author(s) -
Tampellini Davide,
Rahman Nawreen,
Gallo Eduardo F.,
CapetilloZarate Estibaliz,
Lin Michael T.,
Gouras Gunnar K.
Publication year - 2009
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.2009.05.365
Subject(s) - synaptic plasticity , neuroscience , synaptic fatigue , hippocampal formation , depolarization , synaptic cleft , hippocampus , synaptic augmentation , chemistry , biology , microbiology and biotechnology , neurotransmitter , inhibitory postsynaptic potential , endocrinology , biochemistry , central nervous system , excitatory postsynaptic potential , receptor
species around 56kD; dimer/trimer bands are strong in 2-3 cases. The cterminal antibody CT20 detects a c-terminal fragment at w17kD in AD cases. P-tau aggregates and fragments are detected in the same samples with a series of tau antibodies. Conclusions: These results indicate that multiple APP processing pathways are active in AD synapses and multiple oligomeric assemblies, particularly a 56kD assembly, may contribute to synaptic dysfunction.