NR AYEK
AU Westergard,L.; Christensen,H.M.; Harris,D.A.
TI The cellular prion protein (PrPc): its physiological function and role in disease.
QU Biochimica et Biophysica Acta - Molecular Basis of Disease 2007 Jun; 1772(6): 629-44
PT journal article; research support, n.i.h., extramural; review
AB Prion diseases are caused by conversion of a normal cell-surface glycoprotein (PrPc) into a conformationally altered isoform (PrPsc) that is infectious in the absence of nucleic acid. Although a great deal has been learned about PrPsc and its role in prion propagation, much less is known about the physiological function of PrPc. In this review, we will summarize some of the major proposed functions for PrPc, including protection against apoptotic and oxidative stress, cellular uptake or binding of copper ions, transmembrane signaling, formation and maintenance of synapses, and adhesion to the extracellular matrix. We will also outline how loss or subversion of the cytoprotective or neuronal survival activities of PrPc might contribute to the pathogenesis of prion diseases, and how similar mechanisms are probably operative in other neurodegenerative disorders.
ZR 173
MH Animals; Apoptosis/physiology; Humans; Models, Biological; PrPc Proteins/metabolism/*physiology; Prion Diseases/metabolism/pathology/*physiopathology; Signal Transduction/physiology
AD Department of Cell Biology and Physiology, Washington University School of Medicine, St Louis, MO 63110, USA.
SP englisch
PO Niederlande