Copper‐dependent degradation of recombinant ovine prion protein
Open Access
- 10 April 2006
- journal article
- Published by Wiley in The FEBS Journal
- Vol. 273 (9), 1959-1965
- https://doi.org/10.1111/j.1742-4658.2006.05209.x
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.Keywords
This publication has 32 references indexed in Scilit:
- Sequential Generation of Two Structurally Distinct Ovine Prion Protein Soluble Oligomers Displaying Different Biochemical ReactivitiesJournal of Molecular Biology, 2005
- Synthetic Mammalian PrionsScience, 2004
- Copper induces increased beta-sheet content in the scrapie-susceptible ovine prion protein PrPVRQ compared with the resistant allelic variant PrPARRBiochemical Journal, 2004
- Prion Infection Impairs Copper Binding of Cultured CellsPublished by Elsevier ,2003
- Copper and Zinc Binding Modulates the Aggregation and Neurotoxic Properties of the Prion Peptide PrP106−126Biochemistry, 2001
- The N-Terminal Tandem Repeat Region of Human Prion Protein Reduces Copper: Role of Tryptophan ResiduesBiochemical and Biophysical Research Communications, 2000
- Prion Protein Selectively Binds Copper(II) IonsBiochemistry, 1998
- Metal‐dependent α‐helix formation promoted by the glycine‐rich octapeptide region of prion proteinFEBS Letters, 1996
- Natural scrapie in a closed flock of Cheviot sheep occurs only in specific PrP genotypesArchiv für die gesamte Virusforschung, 1996
- The Amyloid Precursor Protein of Alzheimer's Disease in the Reduction of Copper(II) to Copper(I)Science, 1996