NR ANXS
AU Ermonval,M.; Mouillet-Richard,S.; Codogno,P.; Kellermann,O.; Botti,J.
TI Evolving views in prion glycosylation: functional and pathological implications.
QU Biochimie 2003 Jan-Feb; 85(1-2): 33-45
PT journal article; review; review, tutorial
AB Prion diseases form a group of neurodegenerative disorders with the unique feature of being transmissible. These diseases involve a pathogenic protein, called PrPsc for the scrapie isoform of the cellular prion protein (PrPc) which is an abnormally-folded counterpart of PrPc. Many questions remain unresolved concerning the function of PrPc and the mechanisms underlying prion replication, transmission and neurodegeneration. PrPc is a glycosyl-phosphatidylinositol-anchored glycoprotein expressed at the cell surface of neurons and other cell types. PrPc may be present as distinct isoforms depending on proteolytic processing (full length and truncated), topology(GPI-anchored, transmembrane or soluble) and glycosylation (non- mono- and di-glycosylated). The present review focuses on the implications of PrPc glycosylation as to the function of the normal protein, the cellular pathways of conversion into PrPsc, the diversity of prion strains and the related selective neuronal targeting.
ZR 161
MH Animals; Glycosylation; Humans; PrPc Proteins/chemistry/metabolism; PrPsc Proteins/chemistry/metabolism; Prion Diseases/*metabolism; Prions/chemistry/*metabolism/pathogenicity; Protein Processing, Post-Translational; Research Support, Non-U.S. Gov't
AD Laboratoire de Differenciation Cellulaire et Prions, UPR1983 CNRS, 7, rue Guy-Moquet, 94800 Villejuif, France. ermonval@vjf.cnrs.fr
SP englisch
PO Frankreich