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P2‐229: (Patho)physiological consequences of interactions of amyloid‐β with cellular and non‐cellular proteins; the role of “The Crossbeta Pathway”.
Author(s) -
Gebbink Martijn
Publication year - 2011
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.2011.05.1112
Subject(s) - amyloid (mycology) , chemistry , amyloid disease , factor xii , amyloidosis , prekallikrein , proteases , activator (genetics) , kallikrein , microbiology and biotechnology , protein folding , biochemistry , biology , amyloid fibril , enzyme , coagulation , disease , medicine , amyloid β , receptor , inorganic chemistry
Methods: In order to determine the relationship between ongoing neuronal activity, synaptic plasticity and isoform composition of extracellular Abeta, electrophysiologal and biochemical methods had been utilized. Results: Our results show that Abeta40 and Abeta42 isoforms were differentially affected by low-frequency single spikes versus high-frequency spike bursts. Dynamics of [Abeta40]o correlated to short-term plasticity of synaptic vesicle release, displaying facilitation during bursts. Ongoing neuronal activity negatively regulated burst-evoked facilitation of [Abeta40]o and long-term potentiation of vesicle release in hippocampal synapses. Notably, [Abeta42]o exhibited weaker dependency on the pattern of neuronal and synaptic activity. Conclusions: These results suggest that temporal pattern of activity critically controls Abeta40/Abeta42 ratio and propose that the history of synaptic activation regulates metaplasticity of Abeta40 and synaptic vesicle release in hippocampal networks.