APP的胞质结构域及其在阿尔茨海默病发病机制中的可能作用。

The Italian journal of biochemistry Pub Date : 2006-09-01
Giuseppina Minopoli, Nicola Zambrano, Tommaso Russo
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引用次数: 0

摘要

APP是一种功能未知的I型膜蛋白,在β和γ分泌酶的驱动下,其蛋白水解过程产生β -淀粉样肽,这是阿尔茨海默病发病机制的标志之一。APP的短胞质结构域是一个复杂的蛋白质相互作用网络的中心。该网络似乎在APP加工的调控中起着至关重要的作用,反过来又在淀粉样肽的产生中起着至关重要的作用,从而为新的治疗方法提供了候选靶点。此外,APP的一些可能的功能可能只是从这个细胞结构域及其伴侣的研究中出现的。
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The cytosolic domain of APP and its possible role in the pathogenesis of Alzheimer's disease.

APP is a type I membrane protein of unknown function, whose proteolytic processing, driven by beta- and gamma-secretases, generates the beta-amyloid peptides, one of the hallmarks of the pathogenesis of Alzheimer's disease. The short cytosolic domain of APP is the center of a complex network of protein-protein interactions. This network appears to play a crucial role in the regulation of the APP processing and in turn in the generation of the amyloid peptides, thus suggesting candidate targets for new therapeutic approaches. Furthermore, some possible functions of APP could just emerge from the study of this cytodomain and its partners.

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