NR APLO
AU Schneider,B.; Mutel,V.; Pietri,M.; Ermonval,M.; Mouillet-Richard,S.; Kellermann,O.
TI NADPH oxidase and extracellular regulated kinases 1/2 are targets of prion protein signaling in neuronal and nonneuronal cells
QU Proceedings of the National Academy of Sciences of the United States of America 2003 Nov 11; 100(23): 13326-31
PT journal article
AB Putative functions of the cellular prion protein, PrPc, include resistance to oxidative stress, copper uptake, cell adhesion, and cell signaling. Here, we report NADPH oxidase-dependent reactive oxygen species (ROS) production and extracellular regulated kinases 1/2 (ERK1/2) phosphorylation on PrPc stimulation in the 1C11 neuroectodermal precursor, in its neuronal differentiated progenies, and in GT1-7 neurohypothalamic and BW5147 lymphoid cells. In neuroprogenitor, hypothalamic, and lymphoid cells, ERK1/2 activation is fully controlled by the NADPH oxidase-dependent ROS production. In 1C11-derived bioaminergic cells, ROS signaling and ERK1/2 phosphorylation are both controlled by Fyn kinase activation, introducing some specificity in PrPc transduction associated with this neuronal context. These data argue for an ubiquitous function of PrPc in cell-redox homeostasis through ROS production.
MH Animals; Blotting, Western; Cell Line; Cytosol/metabolism; Dose-Response Relationship, Drug; Hypothalamus/metabolism; Mice; Microscopy, Fluorescence; Mitogen-Activated Protein Kinases/*metabolism; Models, Biological; NADPH Oxidase/*chemistry/metabolism/physiology; Neurons/*metabolism; Oxidation-Reduction; Phenotype; Phosphorylation; Precipitin Tests; Prions/*metabolism; Reactive Oxygen Species; Signal Transduction; Support, Non-U.S. Gov't; Time Factors; p42 MAP Kinase/*metabolism
AD Differenciation Cellulaire et Prions, Centre National de la Recherche Scientifique Unite Propre de Recherche 1983, Institut Andre Lwoff, 7 Rue Guy Moquet, BP8, 94 801 Villejuif Cedex, France.
SP englisch
PO USA