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J. Biol. Chem., Vol. 276, Issue 3, 2286-2291, January 19, 2001
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From the Relatively limited information is available on
the processing and function of the normal cellular prion protein,
PrPC. Here it is reported for the first time that
PrPC 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
PrPC and increased detection of amino-terminally fragmented
PrPC within cells. Such a post-translational modification
has vast implications for PrPC, in its processing, because
such cleavage could alter further proteolysis, and in the
formation of the scrapie isoform of the prion protein,
PrPSc, because abnormal cleavage of
PrPSc occurs into the octapeptide repeat region.
Cleavage of the Amino Terminus of the Prion Protein by Reactive
Oxygen Species*
,§,¶,
,, and**
Institut de Génétique Humaine,
CNRS U.P.R. 1142, 141 Rue de la Cardonille,
34396 Montpellier Cedex 5, France and the Commissariat
à l'Energie Atomique (Saclay, France), Service de Pharmacologie
et d'Immunologie, Saclay, 91191 Gif Sur Yvette Cedex, France
*
This work was supported by grants from the Cellule de
Coordination Interorganismes sur les Prions and the CNRS.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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