Brain copper content and cuproenzyme activity do not vary with prion protein expression level.

@article{Waggoner2000BrainCC,
  title={Brain copper content and cuproenzyme activity do not vary with prion protein expression level.},
  author={Darrel J. Waggoner and Bettina Drisaldi and Thomas B. Bartnikas and Ruby Leah B. Casareno and Joseph R. Prohaska and Jonathan D. Gitlin and David A Harris},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 11},
  pages={
          7455-8
        }
}
Prion diseases are neurodegenerative disorders that result from conformational transformation of a normal cell surface glycoprotein, PrP(C), into a pathogenic isoform, PrP(Sc). Although the normal physiological function of PrP(C) has remained enigmatic, the recent observation that the protein binds copper ions with micromolar affinity suggests a possible role in brain copper metabolism. In this study, we have used mice that express 0, 1, and 10 times the normal level of PrP to assess the effect… CONTINUE READING
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