Format

Send to

Choose Destination
See comment in PubMed Commons below
J Biol Chem. 2001 Jan 19;276(3):2286-91. Epub 2000 Nov 1.

Cleavage of the amino terminus of the prion protein by reactive oxygen species.

Author information

1
Institut de Génétique Humaine, CNRS U.P.R. 1142, 141 Rue de la Cardonille, 34396 Montpellier Cedex 5, France.

Abstract

Relatively limited information is available on the processing and function of the normal cellular prion protein, PrP(C). Here it is reported for the first time that PrP(C) undergoes a site-specific cleavage of the octapeptide repeat region of the amino terminus on exposure to reactive oxygen species. This cleavage was both copper- and pH-dependent and was retarded by the presence of other divalent metal ions. The oxidative state of the cell also decreased detection of full-length PrP(C) and increased detection of amino-terminally fragmented PrP(C) within cells. Such a post-translational modification has vast implications for PrP(C), in its processing, because such cleavage could alter further proteolysis, and in the formation of the scrapie isoform of the prion protein, PrP(Sc), because abnormal cleavage of PrP(Sc) occurs into the octapeptide repeat region.

PMID:
11060296
DOI:
10.1074/jbc.M007243200
[Indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire
    Loading ...
    Support Center