By D. Brown (Auth.)
Overseas gurus right here examine examine into the prion illnesses which come with Scrapie of sheep, BSE the "Mad Cow" ailment, and CJD one of many human ailments. The function of metals in those ailments has turn into of serious significance, linking it with the various adjustments in Alzheimer's disorder. The publication makes a speciality of metabolism of copper and manganese that are present in those illnesses. It stems from complaints of the overseas workshop at Christ's collage, Cambridge collage in 2001. After an creation at the heritage of analysis into the illnesses, there are discussions at the results of copper on biochemical homes and prion proteins of mind cells, and more moderen thoughts for his or her learn. there's additionally a bit at the courting of Alzheimers affliction to prion diseases.
- Focuses on metabolism of copper and manganese, that are present in Scrapie of sheep; BSE, the "Mad Cow" illness; and CJD, one of many human prion diseases
- Discusses the results of copper on biochemical houses, prion proteins of mind cells and new ideas for his or her study
- Stems from the lawsuits of the overseas workshop at Christ's collage, Cambridge college in 2001
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Additional info for Prion Diseases and Copper Metabolism. Bse, Scrapie and Cjd Research
Harris, Lesley R. Brown, Elena Quaglio, Bettina Drisaldi and Roberto Chiesa. 1 ABSTRACT Prion diseases are fatal neurological disorders that result from conformational conversion of PrPc, a neuronal glycoprotein of uncertain function, into PrPSc, the primary protein component of infectious prions. During the past several years, several lines of evidence have led to the surprising conclusion that copper ions may play an important role in the biology of both PrPc and PrPSc. It was find that binding of copper to PrPc profoundly alters its cellular trafficking, and dramatically changes its biochemical properties.
R. Giockshuber (Institute of Molecular Biology and Biophysics, ETH Zurich) for their participation in the research and the many helpful discussions. We also thank Willi Groth for his technical support. This project was supported by the Swiss National Science Foundation, Project 438-050285. 5 Co-ordinate Binding of Copper to Prion Protein David R. 1 INTRODUCTION The prion protein (PrPc) is a copper binding protein. However, such a simple statement leads to several questions. There are many known copper binding proteins.
These observations suggest the hypothesis that PrPc functions as a recycling receptor for the cellular uptake or efflux of copper ions. In an uptake model, PrPc on the plasma membrane binds Cu+2 via the peptide repeats, and then delivers the metal by endocytosis to an acidic, endosomal compartment. A. Harris et al. 29 ions then dissociate from PrP c by virtue of the low endosomal pH and, after reduction to Cu+1 , are transported into the cytoplasm by a transmembrane transporter. PrP c subsequently returns to the cell surface to bind additional copper, and the cycle is repeated.