Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA.
Int J Biol Macromol. 2010 Mar 1;46(2):275-9. doi: 10.1016/j.ijbiomac.2009.12.017. Epub 2010 Jan 7.
Chaperones assist in maintenance of functional proteome in vivo. However, they seem to be either ineffective or overwhelmed in the case of protein misfolding diseases like Parkinson's, Huntington's or Alzheimer's. Studies involving one or two chaperones from Hsp70 system cannot provide comprehensive information about the involvement of whole system. We present for the first time, in vitro characterization of the effect of each component of Hsp70 system on alpha-synuclein (involved in Parkinson's) using SEC and ThT assay. Our results show while some components enhance the aggregation others seem to stabilize alpha-synuclein against aggregation. Keeping whole Hsp70 system intact, the factor responsible for triggering aggregation seemed to be initial alpha-synuclein conformation.
伴侣蛋白协助维持体内蛋白质功能组的稳定性。然而，在帕金森病、亨廷顿病或阿尔茨海默病等蛋白质错误折叠疾病中，伴侣蛋白似乎要么无效，要么力不从心。涉及 HSP70 系统中的一两种伴侣蛋白的研究不能提供有关整个系统参与情况的全面信息。我们首次在体外使用 SEC 和 ThT 分析方法对 HSP70 系统的每个成分对参与帕金森病的α-突触核蛋白的影响进行了表征。我们的结果表明，虽然一些成分增强了聚集，但其他成分似乎稳定了α-突触核蛋白，使其不易聚集。保持 HSP70 系统完整，引发聚集的因素似乎是初始α-突触核蛋白构象。
