Simultaneous Live Imaging of Multiple Endogenous Proteins Reveals a Mechanism for Alzheimer's-Related Plasticity Impairment.
作者： Sarah G Cook , Dayton J Goodell , Susana Restrepo , Don B Arnold , K Ulrich Bayer
DOI: 10.1016/J.CELREP.2019.03.041
关键词:
摘要: CaMKIIα is a central mediator of bidirectional synaptic plasticity, including long-term potentiation (LTP) and depression (LTD). To study how movement during plasticity affected by soluble amyloid-β peptide oligomers (Aβ), we used FingR intrabodies to simultaneously image endogenous markers for excitatory versus inhibitory synapses in live neurons. Aβ blocks LTP-stimulus-induced accumulation at synapses. This block requires CaMKII activity, dose time dependent, also occurs without detectable Aβ; it specific LTP, as LTD not reduced. As required normal its impairment can mechanistically explain Aβ-induced LTP. LTP binding the NMDA receptor, induces internalization receptors. However, surprisingly, this does cause observed extrasynaptic, but synaptic,
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