NR ATVV
AU Laffont-Proust,I.; Faucheux,B.A.; Hässig,R.; Sazdovitch,V.; Simon,S.; Grassi,J.; Hauw,J.J.; Moya,K.L.; Haik,S.
TI The N-terminal cleavage of cellular prion protein in the human brain
QU FEBS Letters 2005 Nov 21; 579(28): 6333-7
PT journal article
AB Human brain cellular prion protein (PrPc) is cleaved within its highly conserved domain at amino acid 110/111/112. This cleavage generates a highly stable C-terminal fragment (C1). We examined the relative abundance of holo- and truncated PrPc in human cerebral cortex and we found important inter-individual variations in the proportion of C1. Neither age nor postmortem interval explain the large variability observed in C1 amount. Interestingly, our results show that high levels of C1 are associated with the presence of the active ADAM 10 suggesting this zinc metalloprotease as a candidate for the cleavage of PrPc in the human brain.
IN Die Autoren fanden beim Vergleich verschiedener Patienten in den Hirnen recht unterschiedliche Verhältnisse zwischen verkürztem und noch in voller Länge vorhandenem zellulärem Prionprotein PrPc. Wo ein großer Teil des Prionproteins proteolytisch verkürzt war, fanden die Autoren auch relativ hohe Konzentrationen der Zink-Metalloprotease ADAM 10.
MH ADAM Proteins/*metabolism; Age Factors; Cerebral Cortex/*enzymology/metabolism; Humans; Membrane Proteins/*metabolism; Oxidation-Reduction; PrPc Proteins/*metabolism; Protein Structure, Tertiary; Research Support, Non-U.S. Gov't
AD INSERM Avenir Team - Human Prion Diseases, IFR70, Neuropathology, Salpetriere Hospital, F-75013 Paris, France.
SP englisch
PO Niederlande