Normal prion protein has an activity like that of superoxide dismutase.
We show here that mouse prion protein (PrP(C)) either as recombinant protein or immunoprecipitated from brain tissue has superoxide dismutase (SOD) activity. SOD activity was also associated with recombinant chicken PrP(C) confirming the evolutionary conserved phenotype suggested by sequence similarity. Acquisition of copper by PrP(C) during protein folding endowed SOD activity on the protein but the addition of copper following refolding did not. PrP(C) dependent SOD activity was abolished by deletion of the octapeptide-repeat region involved in copper binding. These results describe an enzymic function for PrP(C) consistent with its cellular distribution and suggest it has a direct role in cellular resistance to oxidative stress.
Brown
D R
DR
Department of Biochemistry, Tennis Court Road, University of Cambridge, Cambridge CB2 1QW, U.K. drb33@cam.ac.uk
Wong
B S
BS
Hafiz
F
F
Clive
C
C
Haswell
S J
SJ
Jones
I M
IM
D000818:Animals; D001665:Binding Sites / Q000235:genetics; D001923:Brain Chemistry; D002645:Chickens; D003300:Copper / Q000737:chemistry; D066298:In Vitro Techniques; D051379:Mice; D018384:Oxidative Stress; D018621:PrPC Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017510:Protein Folding; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012091:Repetitive Sequences, Nucleic Acid; D017384:Sequence Deletion; D013045:Species Specificity; D013482:Superoxide Dismutase / Q000378:metabolism*
D018621:PrPC Proteins; D011993:Recombinant Fusion Proteins; D003300:Copper; D013482:Superoxide Dismutase