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cPLA2 and desaturases underlie the tau hyperphosphorylation offset induced by BACE knock-down in neuronal primary cultures.

Biochim Biophys Acta Mol Basis Dis. 2018 Nov;1864(11):3696-3707. Epub 2018 Aug 24
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摘要


Inflammation has been suggested to play early and perhaps causative roles in Alzheimer's disease (AD) pathogenesis possibly in part by the overactivation of the aspartic acid protease named β-site amyloid precursor protein (APP) cleaving enzyme 1 (BACE1), which is responsible for the β-amyloid cascade. We have described that BACE1 is involved in the lysophosphatidylethanolamine (LPE) (18:1/20:4/22:6) upregulation associated with tauopathy and inflammation signaling (cPLA2/arachidonic acid/COX2) in a triple transgenic model of Alzheimer's disease, where BACE1 silencing reversed the imbalanced profile and produced cognitive function improvement. In this study, we analyze the role of cPLA2 and desaturases (SCD1, FAD6) in the BACE1 knockdown-induced protective action under a glutamate excitotoxicity model. Glutamate (125 μM) produced hyperphosphorylation of tau in cortical primary cultures along with increased apoptotic nuclei, LDH release, and cPLA2 expression, which were all reversed by BACE1-KD. This beneficial effect was reinforced by the silencing of cPLA2 but attenuated by the reduction in SCD1 and partially attenuated by the reduction in FAD6. Inversely, overexpression SCD1 and FAD6 recovered the neuroprotective effect produced by BACE1-KD, which was not achieved by the overexpression of each desaturase alone. These findings suggest that the hyperphosphorylation of tau and the creation of a pro-inflammatory cell environment are blocked in a desaturase-dependent manner by targeting BACE1.

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