Wednesday, June 13, 2018 6:25:07 PM
https://eurekalert.org/pub_releases/2018-06/c-adh061118.php
"The molecule, called CamKII, usually orchestrates synaptic plasticity, an aspect of neuronal adaptability that enables neurons to reinforce their responses to the signals they exchange. Groups of neurons that code for an information to be memorized are connected by synapses, which are themselves under the control of mechanisms of synaptic plasticity. When the connection between two neurons must be reinforced in order to memorize information, for instance during intense stimulation, CamKII is activated and leads to a chain of reactions that strengthen the capacity to transmit messages between these neurons. Synaptic plasticity is central to memory and learning. Amyloid peptides prevent CamKII from participating to this process of synaptic plasticity, and this blockage eventually leads to the disappearance of the synapse. This discovery could find an application in early phases of Alzheimer's disease when initial cognitive deficiencies are observed, which could be linked to this synaptic malfunction"
Their research shows that the amyloid damages a mechanism that is critical to synaptic plasticity Camkii, which in turn causes synaptic loss. Bryostatin has been proven to aid this mechanism in a neuroprotective way. Just another modality that proves beneficial.
http://www.jbc.org/content/291/32/16462.full.pdf
http://www.jbc.org/content/early/2016/06/21/jbc.M116.730440
"Abstract
Protein kinase C epsilon (PKCe) promotes synaptic maturation and synaptogenesis via activation of synaptic growth factors such as BDNF, NGF, and IGF. However, many of the detailed mechanisms by which PKCe induces synaptogenesis are not fully understood. Accumulation of PSD-95 to the postsynaptic density (PSD) is known to lead to synaptic maturation and strengthening of excitatory synapses. Here we investigated the relationship between PKCe and PSD-95.We show that the PKCe activators DCPLA-ME and bryostatin 1 induce phosphorylation of PSD-95 at the serine-295 residue, increase the levels of PSD-95, and enhance its membrane localization. Elimination of the serine-295 residue in PSD-95 abolished PKCe-induced membrane accumulation. Knockdown of either PKCe or JNK1 prevented PKCe activator-mediated membrane accumulation of PSD-95. PKCe directly phosphorylated PSD-95 and JNK1 in vitro. Inhibiting PKCe, JNK, or CaMKII activity prevented the effects of PKCe activators on PSD-95 phosphorylation. Increase in membrane accumulation of PKCe and phosphorylated PSD-95 (p-PSD-95S295) coincided with increased number of synapses and increased amplitudes of excitatory post-synaptic potentials (EPSPs) in adult rat hippocampal slices. Knockdown of PKCe also reduced the synthesis of PSD-95 and the presynaptic protein synaptophysin by 30% and 44% respectively. Prolonged activation of PKCe increased synapse number by 2-fold, increased presynaptic vesicle density, and greatly increased PSD-95 clustering.These results indicate that PKCe promotes synaptogenesis by activating PSD-95 phosphorylation directly, through JNK1 and CaMKII, and also by inducing expression of PSD-95 and synaptophysin.
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