Tsiroulnikov Kirill, Chobert Jean-Marc, Haertlé Thomas
FIPL, BIA, Institut National de la Recherche Agronomique, Nantes, France.
FEBS J. 2006 May;273(9):1959-65. doi: 10.1111/j.1742-4658.2006.05209.x.
Prion protein (PrP) plays an important role in cell protection from oxidative stress due to its action as copper-chelating protein. The present study demonstrates that PrP participates in reductions of Cu2+ to Cu+ ions, and that this process results in fragmentation of protein. The interaction with phosphatidylinositol, a natural phospholipid moiety bound to PrP, strongly enhances recombinant PrP aggregation and degradation. The copper-dependent PrP degradation could promote the formation of amyloid structures, destabilizing the PrP soluble form by the cleavage of the N-terminal part.
朊病毒蛋白（PrP）作为一种铜螯合蛋白，在细胞抵御氧化应激中发挥重要作用。本研究表明，PrP参与将Cu2+还原为Cu+离子的过程，且该过程会导致蛋白质片段化。与磷脂酰肌醇（一种与PrP结合的天然磷脂部分）的相互作用，强烈增强了重组PrP的聚集和降解。铜依赖性的PrP降解可能促进淀粉样结构的形成，通过切割N端部分使PrP可溶性形式不稳定。
