NR ARQS
AU Kazlauskaite,J.; Pinheiro,T.J.T.
TI Aggregation and fibrillization of prions in lipid membranes
QU Biochemical Society Symposia 2005(72): 211-22
PT journal article; review; review, tutorial
AB A key molecular event in prion diseases is the conversion of PrP (prion protein) from its normal cellular form (PrPc) into the disease-specific form (PrPsc). The transition from PrPc to PrPsc involves a major conformational change, resulting in amorphous aggregates and/or fibrillar amyloid deposits. Here, we review several lines of evidence implicating membranes in the conversion of PrP, and summarize recent results from our own work on the role of lipid membranes in conformational transitions of prion proteins. By establishing new correlations between in vivo biological findings with in vitro biophysical results, we propose a role for lipid rafts in prion conversion, which takes into account the structural heterogeneity of PrP in different lipid environments.
ZR 52
MH Animals; Biological Transport, Active; Endoplasmic Reticulum/metabolism; Glycosylphosphatidylinositols/chemistry/metabolism; Golgi Apparatus/metabolism; Humans; In Vitro; Membrane Lipids/*chemistry/*metabolism; Membrane Microdomains/chemistry/metabolism; Models, Biological; Models, Molecular; Multiprotein Complexes; PrPc Proteins/chemistry/metabolism; PrPsc Proteins/chemistry/metabolism; Prions/*chemistry/*metabolism; Protein Conformation; Research Support, Non-U.S. Gov't
AD Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, U.K.
SP englisch
PO England