TURNOVER RATE OF PRP OLIGOMERS IN THE BRAIN

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 蛋白质聚集体的积累与许多神经退行性疾病有关。这些蛋白质聚集体的存在是正常蛋白质代谢被破坏的直接证据。Prion是这种效应的主要例子，因为它们是具有感染性的蛋白质颗粒。尽管已分离出不同孕育时间和不同病理类型的病毒株，但病毒粒子中没有核酸成分。感染只需要将正常的蛋白质周转转移到新的聚集体的形成上。要了解Pron疾病的传播以及这些聚集体如何导致神经退化，我们需要研究由于Pron感染而导致的蛋白质周转的变化。利用氮同位素标记，我们将在蛋白质组范围内测量蛋白质周转，以评估普里恩病期间全球蛋白质周转的扰动。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The accumulation of protein aggregates is associated with many neurodegenerative diseases. The presence of these protein aggregates is direct evidence that normal protein metabolism is disrupted. Prions are a primary example of this effect, as they are infectious proteinaceous particles. Although strains of prions have been isolated which differ in incubation time and pathology, there is no nucleic acid component of the prion particles. Infection requires only that normal protein turnover is diverted to the formation of new aggregates. Understanding the propagation of prion disease and how these aggregates cause neurodegeneration requires that we investigate changes in protein turnover due to prion infection. Using nitrogen isotope labeling we will measure protein turnover on a proteome-wide scale to assess perturbations in global protein turnover during prion disease.