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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 >Prion protein expression alters APP cleavage without interaction with BACE-1
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Prion protein expression alters APP cleavage without interaction with BACE-1

机译：Prion蛋白表达可改变APP裂解而不与BACE-1相互作用

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摘要

The prion protein (PrP) and the beta-site amyloid precursor protein (APP) cleaving enzyme 1 (BACE-1) are both copper binding proteins, but are associated with two separate neurodegenerative diseases. The role of BACE-1 in the formation of beta-amyloid has made it a major target in attempts to reduce the formation of beta-amyloid in Alzheimer's diseases. However, the suggestion that PrP, normally associated with prion diseases, binds to BACE-1 and reduces its activity has led to the suggestion that the study of this interaction could be of considerable importance to Alzheimer's disease. We therefore undertook to investigate the possible interaction of these two proteins physically and at the level of transcription, translation and APP cleavage. Our findings suggest that mature PrP and BACE-1 do not physically interact, but that altered PrP expression results in altered BACE-1 protein expression and promoter activity. Additionally, overexpression of PrP results in increased cleavage of APP in contrast to previous datas suggesting a reduction. Our findings suggest that any relation between PrP and BACE-1 is indirect. Altered expression of PrP causes changes in the expression of many other proteins which may be as a result of altered copper metabolism.
机译：ion病毒蛋白（PrP）和β位淀粉样蛋白前体蛋白（APP）裂解酶1（BACE-1）都是铜结合蛋白，但与两种单独的神经退行性疾病有关。 BACE-1在β-淀粉样蛋白形成中的作用使其成为减少阿尔茨海默氏病中β-淀粉样蛋白形成的主要目标。然而，通常与病毒疾病有关的PrP与BACE-1结合并降低其活性的建议导致了这种相互作用的研究对于阿尔茨海默氏病可能具有相当重要的意义。因此，我们承诺在物理上以及在转录，翻译和APP裂解水平上研究这两种蛋白的可能相互作用。我们的发现表明，成熟的PrP和BACE-1不会发生物理相互作用，但是PrP表达的改变会导致BACE-1蛋白表达和启动子活性的改变。另外，与先前的数据表明减少的情况相比，PrP的过表达导致APP的切割增加。我们的发现表明PrP和BACE-1之间的任何关系都是间接的。 PrP的表达改变导致许多其他蛋白质表达的改变，这可能是铜代谢改变的结果。

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