中文摘要：

prion 疾病的特点是错误褶层蛋白质 PrP ^{对 neuronal 房间有毒的 Sc} , 。proteasome 系统为快速、精确、及时的降级 ofproteins 负责并且在细胞的蛋白质质量控制起一个重要作用。增加的证据在 prion 疾病显示损害 activityof proteasomes。积累的 PrP ^Sc 能直接或间接地影响 proteasome 活动。错误褶层蛋白质可以影响 20S proteasome 的 19S regulatoryparticle，或 translational 以后修正的集会和活动，它可以不利地影响蛋白质降级 activityof proteasomes。在这评论，我们在 prionand 有关 proteasomes 的可能的规定总结了最近的调查结果另外的 neurodegenerative 疾病。proteasome 系统可以由改变它的结构提高它的降级活动，并且当 neuronal 房间服从于应力时，这项活动能被相关女伴也增加。当 proteasomesystem 被禁止时，经由 autophagy 的蛋白质总数的降级可以作为一个补偿系统增加。它是 possiblethat 平衡在 vivo 在 proteasome 和 autophagy 之间存在；当一个人被损害时，其它的活动可以增加维持动态平衡。然而，更多的研究是需要的 toelucidate 在 proteasome 系统和 autophagy 之间的关系。

英文摘要：

The hallmark of prion disease is the accumulation of mis folded protein PrPsc, which is toxic to neuronal cells. The proteasome system is responsible for the rapid, precise, and timely degradation of proteins and plays an important role in cellular protein quality control. Increasing evidence indi cates impaired activity of proteasomes in prion diseases. Accumulated PrPsc can directly or indirectly affect prote asome activity. Misfolded protein may influence the assem bly and activity of 19S regulatory particle, or post translational modification of 20S proteasome, which may adversely affect the protein degradation activity of protea somes. In this review, we summarized the recent findings concerning the possible regulation of proteasomes in prion and other neurodegenerative diseases. The proteasome system may enhance its degradation activity by changing its structure, and this activity can also be increased by related chaperones when neuronal cells are subject to stress. When the proteasome system is inhibited, degradation of protein aggregates via autophagy may increase as a compensatory system. It is possible that a balance exists between the prote asome and autophagy in vivo; when one is impaired, the ac tivity of the other may increase to maintain homeostasis. However, more studies are needed to elucidate the relation ship between the proteasome system and autophagy.