TURNOVER RATE OF PRP OLIGOMERS IN THE BRAIN

该子项目是利用 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 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。 朊病毒是这种效应的主要例子，因为它们是感染性蛋白质颗粒。 虽然朊病毒株已被分离出来，其在孵育时间和病理学上不同，但朊病毒颗粒中没有核酸成分。 感染只需要正常的蛋白质周转被转移到新的聚集体的形成。 了解朊病毒疾病的传播以及这些聚集体如何导致神经变性，需要我们研究朊病毒感染引起的蛋白质周转的变化。 使用氮同位素标记，我们将在蛋白质组范围内测量蛋白质周转，以评估朊病毒疾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.