NR ASRB
AU Roucou,X.; LeBlanc,A.C.
TI Cellular prion protein neuroprotective function: implications in prion diseases.
QU Journal of Molecular Medicine 2005 Jan; 83(1): 3-11
PT journal article; review; review, tutorial
AB Prion protein can display two conformations: a normal cellular conformation (PrP) and a pathological conformation associated with prion diseases (PrPsc). Three complementary strategies are used by researchers investigating how PrP is involved in the pathogenesis of prion diseases: elucidation of the normal function of PrP, determination of how PrPsc is toxic to neurons, and unraveling the mechanism for the conversion of PrP to PrPsc. We review the normal function of PrP as an antioxidant and an antiapoptotic protein in vivo and in vitro. This review also addresses contrasting evidence that PrP is cytotoxic. Finally, we discuss the implication of the neuroprotective role of PrP in prion diseases.
ZR 87
MH Animals; Apoptosis/genetics/physiology; Brain/metabolism; Breast Neoplasms/metabolism; Cell Survival/physiology; Humans; Mice; Neurons/*metabolism; Oxidative Stress/physiology; Prion Diseases/*metabolism; Prions/*metabolism; Proto-Oncogene Proteins c-bcl-2/physiology; Tumor Necrosis Factor-alpha/metabolism
AD Bloomfield Center for Research in Aging, Lady Davis Institute for Medical Research, 3755 Ch. Cote Ste-Catherine, Montreal, QC, H3T 1E2, Canada.
SP englisch
PO Deutschland