Wechselberger Christian, Wurm Susanne, Pfarr Werner, Höglinger Otmar
Center for Biomedical Nanotechnology, Upper Austrian Research GmbH, Linz, Austria.
Exp Cell Res. 2002 Nov 15;281(1):1-8. doi: 10.1006/excr.2002.5655.
Prion proteins are mentioned predominantly as unprecedented infectious pathogens in the context of transmissible spongiform encephalopathies. Since prions are devoid of nucleic acids, disease transmission must be mediated by an entirely novel mechanism. The general accepted theory proposes the conversion of cellular prion protein (PrP(C)) into the pathological isoform solely through conformational changes. This process favors the development of insoluble protein aggregates in the central nervous system typical for prion diseases. However, progress to elucidate the physiological functions of PrP(C) is still slow besides recent indications of a multifaceted network, in which PrP(C) seems to play a fundamental role. Possible contributions of interrupted or disturbed physiological signaling events due to the pathological prion protein isoform are presented in terms of recent findings.
在可传播性海绵状脑病的背景下，朊病毒蛋白主要被视为前所未有的传染性病原体。由于朊病毒不含核酸，疾病传播必定由一种全新的机制介导。普遍接受的理论认为，细胞朊病毒蛋白（PrP(C)）仅通过构象变化转化为病理异构体。这一过程有利于在朊病毒疾病典型的中枢神经系统中形成不溶性蛋白质聚集体。然而，除了最近表明PrP(C)似乎在一个多方面的网络中发挥重要作用外，阐明PrP(C)生理功能的进展仍然缓慢。根据最近的研究结果，介绍了病理性朊病毒蛋白异构体导致的生理信号事件中断或紊乱可能产生的影响。
