NR AQML
AU Mange,A.; Beranger,F.; Peoc'h,K.; Onodera,T.; Frobert,Y.; Lehmann,S.
TI Alpha- and beta- cleavages of the amino-terminus of the cellular prion protein
QU Biology of the Cell 2004 Mar; 96(2): 125-32
PT journal article
AB It is commonly assumed that the physiological isoform of prion protein, PrPc, is cleaved during its normal processing between residues 111/112, whereas the pathogenic isoform, PrPsc, is cleaved at an alternate site in the octapeptide repeat region around position 90. Here we demonstrated both in cultured cells and in vivo, that PrPc is subject to a complex set of post-translational processing with the molecule being cleaved upstream of position 111/112, in the octapeptide repeat region or at position 96. PrP has therefore two main cleavage sites that we decided to name alpha and beta. Cleavage of PrPc at these sites leads us to re-evaluate the function of both N- and C-terminus fragments thus generated.
MH Amino Acid Sequence; Animals; Cell Line; Cell Survival; Hamsters; Humans; Mice; Peptide Fragments/chemistry/metabolism/secretion; PrPc Proteins/*chemistry/genetics/*metabolism; *Protein Processing, Post-Translational; Research Support, Non-U.S. Gov't; Sequence Deletion/genetics; Spectrum Analysis, Mass; Transfection
AD Institut de Genetique Humaine, CNRS U.P.R. 1142, 141, rue de la Cardonille, 34396 Montpellier Cedex 5, France.
SP englisch
PO Frankreich