The Relationship Between Copper, Manganese, and Bovine Brain Prion Proteins: Implications for Trace Mineral Nutrition and Bovine Spongiform Encephalopathy

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dc.contributor.advisor J. Odle, Committee Member en_US
dc.contributor.advisor H. C. Liu, Committee Member en_US
dc.contributor.advisor D. Hanson, Committee Member en_US
dc.contributor.advisor J. Spears, Committee Member en_US Legleiter, Leon R. en_US 2010-04-02T19:16:20Z 2010-04-02T19:16:20Z 2006-11-08 en_US
dc.identifier.other etd-11032006-085510 en_US
dc.description.abstract The purpose of this research was to evaluate the relationship between dietary copper and manganese and bovine brain prion proteins. Aberrant prion proteins are the causative infective agent in bovine spongiform encephalopathy and other transmissible spongiform encephalopathies. While the cellular prion protein is purported to bind copper ions, a substitution of copper with manganese on the prion protein causes alterations in the biochemical properties of the prion that are similar to the infective prion. An imbalance in brain copper and manganese that allows for prion bound copper to be replaced by manganese has been implicated in the spontaneous conversion of cellular prions to aberrant prions and the subsequent sporadic forms of transmissible spongiform encephalopathies. Until now these findings have not been tested in the bovine. Thus, the studies reported here were designed to test the hypothesis that a copper deficiency, alone or coupled with high dietary manganese, would result in decreased brain copper and increased brain manganese and subsequently alter the biochemical properties of prion proteins. Considerations were given to animal age and length of exposure as well as imbalances in dietary copper and manganese. We report that brain copper is decreased in copper deficient cattle and brain manganese is slightly increased when exposed to high dietary manganese. The perturbations in brain copper and manganese did not alter prion biochemical properties. Most notably there was no apparent manganese for copper substitution on prion proteins that resulted in increased protease resistance or decreased superoxide dismutase-like activity. Also, the prion associated copper and superoxide dismutase-like activities were significantly lower than values reported from in vitro research. Taken together, these results do not support the hypothesis that perturbations in brain copper and manganese induce biochemical changes to prion proteins. Additionally, these data suggest the relationship between brain prions and copper need to be revaluated in the context of whole animal biology. en_US
dc.rights I hereby certify that, if appropriate, I have obtained and attached hereto a written permission statement from the owner(s) of each third party copyrighted matter to be included in my thesis, dis sertation, or project report, allowing distribution as specified below. I certify that the version I submitted is the same as that approved by my advisory committee. I hereby grant to NC State University or its agents the non-exclusive license to archive and make accessible, under the conditions specified below, my thesis, dissertation, or project report in whole or in part in all forms of media, now or hereafter known. I retain all other ownership rights to the copyright of the thesis, dissertation or project report. I also retain the right to use in future works (such as articles or books) all or part of this thesis, dissertation, or project report. en_US
dc.subject bovine en_US
dc.subject prion en_US
dc.subject copper en_US
dc.subject manganese en_US
dc.title The Relationship Between Copper, Manganese, and Bovine Brain Prion Proteins: Implications for Trace Mineral Nutrition and Bovine Spongiform Encephalopathy en_US PhD en_US dissertation en_US Nutrition en_US

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