Amyloid-b suppresses XXXX -activated protein kinase (AMPK) signaling and contributes to @entity8095 -induced @entity137 .

@entity137 @entity8095 @entity4093 @entity1832 @entity179 @entity8582 @entity195 @entity2359 @entity2383
UNASSIGNED: @entity1832 ( @entity1832 ) is a @entity179 caused by abnormal accumulation of @entity1832 , which are intracellular deposits composed primarily of aggregated @entity8095 (aSyn). Although aSyn has been strongly implicated to induce @entity2359 , overexpression of wild-type aSyn is shown to be insufficient to trigger formation of protein aggregates by itself. Therefore, investigating the possible mechanism underlying aSyn aggregation is essential to understand the pathogenesis of @entity1832 . Previous studies have demonstrated that amyloid b (Ab), the primary cause of @entity195 ( @entity195 ), may promote the formation of aSyn inclusion bodies. However, it remains unclear how Ab contributes to the deposition and @entity2359 of aSyn. In the present study, we investigated the cytotoxic effects of Ab in aSyn-overexpressed neuronal cells. Our results showed that Ab inhibits autophagy and enhances aSyn aggregation in aSyn-overexpressed cells. Moreover, Ab also reduced @entity4093 ( @entity4093 ) and its downstream signaling, resulting in increased intracellular ROS accumulation and @entity2383 . Our in vitro and in vivo studies support that Ab-inhibition of @entity8582 -activated protein kinase (AMPK) signaling is involved in the @entity2359 effects of aSyn. Taken together, our findings suggest that Ab plays a synergistic role in aSyn aggregation and @entity137 , which may provide a novel understanding for exploring the underlying molecular mechanism of @entity1832 .
