Prion proteins and ECTO-NOX proteins exhibit similar oscillating redox activities.
Both recombinant full-length mouse prion protein expressed in Escherichia coli and native prion protein (PrPsc) from mouse brain exhibited NADH oxidase and protein disulfide-thiol interchange activities similar to those formerly thought to be properties exclusive to the growth-related, cell surface ECTO-NOX proteins. The two activities exhibited the complex 2+3 pattern of oscillations characteristic of ECTO-NOX proteins where the two activities alternate to generate a period length of 24 min. The oscillations were augmented by copper and diminished by addition of the copper chelator bathocuproene. That the activity might be attributable to a contaminating protein was ruled out by experiments where the purified recombinant prion-containing extracts were resolved by SDS-PAGE and the activity was restricted to a single band corresponding to the predicted Mr of the recombinant prion as verified by Western blot analyses.
Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47907-2064, USA.
Chinpal
C
Kim
D James
DJ
Morré
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D002614:Chelating Agents / Q000494:pharmacology; D002853:Chromatography, Liquid / Q000379:methods; D003300:Copper / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D051379:Mice; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D010084:Oxidation-Reduction; D010507:Periodicity; D018620:PrPSc Proteins / Q000378:metabolism; D011328:Prions / Q000235:genetics / Q000378:metabolism*; D019704:Protein Disulfide-Isomerases / Q000378:metabolism; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D013053:Spectrophotometry / Q000379:methods
D002614:Chelating Agents; D018620:PrPSc Proteins; D011328:Prions; D011994:Recombinant Proteins; D003300:Copper; D009247:NADH, NADPH Oxidoreductases; D019704:Protein Disulfide-Isomerases