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首页> 外文期刊>Neurochemistry International: The International Journal for the Rapid Publication of Critical Reviews, Preliminary and Original Research Communications in Neurochemistry >Reversible and irreversible acetylcholinesterase inhibitors cause changes in neuronal amyloid precursor protein processing and protein kinase C level in vitro.
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Reversible and irreversible acetylcholinesterase inhibitors cause changes in neuronal amyloid precursor protein processing and protein kinase C level in vitro.

机译：可逆和不可逆的乙酰胆碱酯酶抑制剂在体外引起神经元淀粉样前体蛋白加工和蛋白激酶C水平的变化。

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摘要

The alternative routes of cleavage of the amyloid precursor protein (APP) result in the generation and secretion of both soluble APP and beta-amyloid, the latter being the main component of the amyloid deposits in the brains of individuals with Alzheimer's disease (AD). This study examined the question of whether acetylcholinesterase (AChE) inhibitors can alter the processing of APP and the level of protein kinase C (PKC) in primary rat basal forebrain cultures. Western blotting was used to test two AChE inhibitors (reversible and irreversible) for their ability to enhance the release of APP and PKC content. These inhibitors were ambenonium (AMB) and metrifonate (MTF), at different concentrations. A significant increase was found in the cell-associated APP level in a basal forebrain neuronal culture, and there was an elevation of the APP release into the medium. Increases were similarly observed in the PKC levels after AMB or MTF treatment. The results suggest that these AChE inhibitors promote the non-amyloidogenic route of APP processing, which may be due to their stimulatory effects on PKC. The PKC activation may enhance the alpha-secretase activity and consequently the production of the N-terminal APP. Since both a decreased level of APP secretion and a low activity and level of PKC may be involved in the pathogenesis of AD, it is concluded that the administration of AChE inhibitors to AD patients may facilitate the memory processes and exert a neuroprotective effect.
机译：淀粉样蛋白前体蛋白（APP）裂解的替代途径导致可溶性APP和β-淀粉样蛋白的产生和分泌，β-淀粉样蛋白是阿尔茨海默氏病（AD）患者大脑中淀粉样蛋白沉积的主要成分。这项研究探讨了乙酰胆碱酯酶（AChE）抑制剂是否可以改变原代大鼠基础前脑培养物中APP的加工和蛋白激酶C（PKC）的水平。蛋白质印迹法用于测试两种AChE抑制剂（可逆和不可逆）增强APP和PKC含量释放的能力。这些抑制剂分别是不同浓度的eno烯（AMB）和美甲酸酯（MTF）。在基底前脑神经元培养物中，与细胞相关的APP水平显着增加，并且APP向培养基中的释放有所增加。在AMB或MTF处理后，同样观察到PKC水平增加。结果表明，这些AChE抑制剂促进了APP加工过程的非淀粉样生成途径，这可能是由于它们对PKC的刺激作用。 PKC激活可以增强α分泌酶的活性，从而增强N末端APP的产生。由于APP分泌​​的降低水平和PKC的低活性和低水平都可能与AD的发病有关，因此可以得出结论，向AD患者施用AChE抑制剂可以促进记忆过程并发挥神经保护作用。

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