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Copper‐dependent degradation of recombinant ovine prion protein
Author(s) -
Tsiroulnikov Kirill,
Chobert JeanMarc,
Haertlé Thomas
Publication year - 2006
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2006.05209.x
Subject(s) - recombinant dna , chemistry , prion protein , copper , chelation , cleavage (geology) , liposome , fragmentation (computing) , moiety , phosphatidylinositol , protein aggregation , biochemistry , amyloid (mycology) , biophysics , stereochemistry , biology , signal transduction , organic chemistry , medicine , paleontology , ecology , disease , pathology , fracture (geology) , gene , inorganic chemistry
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 Cu 2+ 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.