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Licensed Unlicensed Requires Authentication Published by De Gruyter June 1, 2005

No Superoxide Dismutase Activity of Cellular Prion Protein in vivo

  • G. Hutter , F.L. Heppner and A. Aguzzi
From the journal Biological Chemistry

Abstract

Prion diseases are characterized by the deposition of PrPSc, an abnormal form of the cellular prion protein PrPc, which is encoded by the Prnp gene. PrPc is highly expressed on neurons and its function is unknown. Recombinant PrPc was claimed to possess superoxide dismutase (SOD) activity, and it was hypothesized that abrogation of this function may contribute to neurodegeneration in prion diseases. We tested this hypothesis in vivo by studying copper/zinc and manganese SOD activity in genetically defined crosses of mice lacking the Sod1 gene with mice lacking PrPc, and with hemizygous or homozygous tga20 transgenic mice overexpressing various levels of PrPc. We failed to detect any influence of the Prnp genotype and gene dosage on SOD1 or SOD2 activity in heart, spleen, brain, and synaptosomeenriched brain fractions. Control experiments included crosses of mice lacking or overexpressing PrP with mice overexpressing human Cu[2+]/Zn[2+]-superoxide dismutase, and confirmed that SOD enzymatic activity correlated exclusively with the gene dosage of bona fide human or murine SOD. We conclude that PrPc in vivo does not discernibly contribute to total SOD activity and does not possess an intrinsic dismutase activity.

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Published Online: 2005-06-01
Published in Print: 2003-09-28

Copyright © 2003 by Walter de Gruyter GmbH & Co. KG

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