NR AMJV
AU Westaway,D.; Carlson,G.A.
TI Mammalian prion proteins: enigma, variation and vaccination.
QU Trends in Biochemical Sciences 2002 Jun; 27(6): 301-7
PT journal article; review; review, tutorial
AB Although misfolding of the cellular prion protein PrPc into an alternative form, denoted PrPsc, is a key event in prion infections, the normal function of PrPc remains to be clearly defined. Many PrPc-binding proteins have been identified, but authentication of these interactions in functional assays is incomplete. Doppel (Dpl), a recently discovered PrP-like protein, might provide a new avenue by which to explore physiological and pathological functions of PrP. For example, overexpression of Dpl causes apoptotic cerebellar cell death that is abrogated by PrPc, indicating that these two proteins can act in a common pathway. Despite our incomplete understanding of PrPc, immunological targeting of this PrPsc precursor has produced encouraging results, indicating a potential point of intervention against these fatal diseases.
ZR 56
MH Animal; Genomics; Human; Molecular Sequence Data; Prion Diseases/genetics/*immunology/prevention & control; Prions/chemistry/genetics/*immunology/*metabolism; Scrapie/genetics; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; *Vaccination
AD Centre for Research in Neurodegenerative Diseases, Dept of Laboratory Medicine and Pathobiology, University of Toronto, Tanz Neuroscience Building, 6 Queen's Park Crescent West, Toronto, Ontario M5S 3H2, Canada. david.westaway@utoronto.ca
SP englisch
PO England