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Background g-Secretase cleaves amyloid precursor protein (APP) to produce Ab peptide, and the secretase is a critical factor in the pathogenesis of Alzheimer’s Disease (AD), whereas acetylcholinesterase (AChE) is a key factor for maintaining normal nerve impulses. However, there has been no published research that focuses on the relationship between these two factors. g-Secretase cleaves various substrates, and loss of function of g-secretase is lethal. Thus, the mechanism by which g-secretase cleaves APP is a key factor in AD pathogenesis. AChE is one of the main targets in the treatment of AD, and AChE inhibitors are commonly used for AD. Currently there is agreement that AChE inhibitors stabilizes acetylcholine (ACh) levels in the brain, which ensures ACh transport among neurons. However, the actual effect is limited. It has been reported that AChE interacts with PS1 and affects its glycosylation. This result suggests a link between AChE and g-secretase. Here, we have tested the effects of AChE on cleavage of APP by g-secretase.

Acetylcholinesterase blocks cleavage of APP by γ-secretase in 293 cells and mouse brain