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Moreover, the intracellular Ser-326-dependent changes in Syn cleavage caused by the FAD PSEN1 M146L mutation were suggested via ERK/MAPK-mediated activation of Stress-induced-phosphatase (STOP1) which led to enhanced processing of APP by beta-secretase, downregulated activity of the amyloidogenic APP variant by decreasing its APP-cleavage by alpha-secretase, and downregulation of the intracellular Syn levels by increased activity of the non-amyloidogenic PS1 M148V mutant [203]. More recently, studies indicated that Syn-activity inhibitors could reduce the plaque-size in APP/PS1 transgenic mice [204]. However, Tiezu Chen’s group reported that Syn over-expression in Apppsyn mice could increase the number of plaques and CAA. On the contrary, Syn knockdown could reduce the number of plaques and CAA in PS1J20 mice [205].
In terms of synaptic plasticity, Syn knockout mice have a significant decrease in LTP, whereas Syn overexpression causes a significant LTP increase [206]. To date, many published findings have demonstrated an association between the implicated genes: PSEN1, PSEN2, APP, and MAPT and the risk of dementia in AD, which may increase with age and correlated with the total Abeta burden ( Figure 3 ). In AD patients, the accumulation of Abeta is known to occur first in the hippocampus, followed by changes in the cortex [207].
Syn also modulates the expression levels of the other gene that encodes for Abeta precursor protein in neurons: amyloid beta precursor protein (APP), and the APP levels are regulated by Syn as well as other closely related proteins. As indicated, Syn decreases APP levels. Curiously, Syn can also influence APP processing, levels and protein trafficking in presynaptic vesicles, resulting in altered levels Aβ [208].
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