Normal prion protein has an activity like that of superoxide dismutase

Citation
Dr. Brown et al., Normal prion protein has an activity like that of superoxide dismutase, BIOCHEM J, 344, 1999, pp. 1-5
Citations number
31
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL JOURNAL
ISSN journal
0264-6021 → ACNP
Volume
344
Year of publication
1999
Part
1
Pages
1 - 5
Database
ISI
SICI code
0264-6021(19991115)344:<1:NPPHAA>2.0.ZU;2-N
Abstract
We show here that mouse prion protein (PrPC) either as recombinant protein or immunoprecipitated from brain tissue has superoxide dismutase (SOD) acti vity. SOD activity was also associated with recombinant chicken PrPC confir ming the evolutionary conserved phenotype suggested by sequence similarity. Acquisition of copper by PrPC during protein folding endowed SOD activity on the protein but the addition of copper following refolding did not. PrPC dependent SOD activity was abolished by deletion of the octapeptide-repeat region involved in copper binding. These results describe an enzymic funct ion for PrPC consistent with its cellular distribution and suggest it has a direct role in cellular resistance to oxidative stress.