title: Copper-dependent degradation of recombinant ovine prion protein. Phosphatidylinositol stimulates aggregation and copper-driven disappearance of prion protein.
abstract: 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.
authors.affiliation: FIPL, BIA, Institut National de la Recherche Agronomique, Nantes, France.
authors.forename: Kirill
authors.initials: K
authors.lastname: Tsiroulnikov
authors.forename: Jean-Marc
authors.initials: JM
authors.lastname: Chobert
authors.forename: Thomas
authors.initials: T
authors.lastname: Haertlé
mesh_terms: D000818:Animals; D003300:Copper / Q000737:chemistry* / Q000378:metabolism*; D010716:Phosphatidylinositols / Q000494:pharmacology*; D011328:Prions / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012756:Sheep; D013997:Time Factors
chemical_list: D010716:Phosphatidylinositols; D011328:Prions; D011994:Recombinant Proteins; D003300:Copper