NR AUPW
AU Tsiroulnikov,K.; Chobert,J.M.; Haertle,T.
TI Copper-dependent degradation of recombinant ovine prion protein. Phosphatidylinositol stimulates aggregation and copper-driven disappearance of prion protein.
QU The FEBS Journal 2006 May; 273(9): 1959-65
PT journal article
AB 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.
MH Animals; Copper/*chemistry/*metabolism; Phosphatidylinositols/*pharmacology; Prions/*chemistry/genetics/*metabolism; Recombinant Proteins/chemistry/genetics/metabolism; Research Support, Non-U.S. Gov't; Sheep; Time Factors
AD Kirill Tsiroulnikov, Jean-Marc Chobert and Thomas Haertlé (haertle@nantes.inra.fr), FIPL, BIA, Institut National de la Recherche Agronomique, Nantes, France.
SP englisch
PO England