KMID : 0578320190420010036
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Molecules and Cells 2019 Volume.42 No. 1 p.36 ~ p.44
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Effects of ¥ä-Catenin on APP by Its Interaction with Presenilin-1
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Dai Weiye
Ryu Tae-Yong Kim Han-Gun Jin Yun-Hye Cho Young-Chang Kim Kwon-Seop
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Abstract
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Alzheimer¡¯s disease (AD) is the most frequent age-related human neurological disorder. The characteristics of AD include senile plaques, neurofibrillary tangles, and loss of synapses and neurons in the brain. ¥â-Amyloid (A¥â) peptide is the predominant proteinaceous component of senile plaques. The amyloid hypothesis states that A¥â initiates the cascade of events that result in AD. Amyloid precursor protein (APP) processing plays an important role in A¥â production, which initiates synaptic and neuronal damage. ¥ä-Catenin is known to be bound to presenilin-1 (PS-1), which is the main component of the ¥ã-secretase complex that regulates APP cleavage. Because PS-1 interacts with both APP and ¥ä-catenin, it is worth studying their interactive mechanism and/or effects on each other. Our immunoprecipitation data showed that there was no physical association between ¥ä-catenin and APP. However, we observed that ¥ä-catenin could reduce the binding between PS-1 and APP, thus decreasing the PS-1 mediated APP processing activity. Furthermore, ¥ä-catenin reduced PS-1-mediated stabilization of APP. The results suggest that ¥ä-catenin can influence the APP processing and its level by interacting with PS-1, which may eventually play a protective role in the degeneration of an Alzheimer¡¯s disease patient.
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KEYWORD
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Alzheimer¡¯s disease, APP, ¥ä-catenin, presenilin
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