Prion Diseases and Copper Metabolism. Bse, Scrapie and Cjd by D. Brown (Auth.)

By D. Brown (Auth.)

Foreign professionals right here examine learn into the prion ailments which come with Scrapie of sheep, BSE the "Mad Cow" disorder, and CJD one of many human ailments. The position of metals in those illnesses has develop into of significant significance, linking it with many of the alterations in Alzheimer's sickness. The publication makes a speciality of metabolism of copper and manganese that are present in those ailments. It stems from complaints of the overseas workshop at Christ's university, Cambridge college in 2001. After an advent at the background of analysis into the ailments, there are discussions at the results of copper on biochemical houses and prion proteins of mind cells, and more moderen strategies for his or her research. there's additionally a piece at the courting of Alzheimers disorder to prion diseases.

  • Focuses on metabolism of copper and manganese, that are present in Scrapie of sheep; BSE, the "Mad Cow" ailment; and CJD, one of many human prion diseases
  • Discusses the results of copper on biochemical homes, prion proteins of mind cells and new innovations for his or her study
  • Stems from the complaints of the foreign workshop at Christ's collage, Cambridge collage in 2001

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Moreover, the fact that Prn-pm mice do not, in our experiments, have reduced Cu-Zn SOD or cytochrome oxidase levels (Waggoner et al, 2000) suggests that PrPc is not involved in the specialized, chaperonemediated pathways involved in copper delivery to these two cuproenzymes (Valentine and Gralla, 1997). A. Harris et al. 35 from Prn-p mice are more susceptible to oxidative stress (Brown, 2001b), it is possible that PrPc-mediated copper uptake plays a role in delivery of the metal to other anti-oxidant enzymes.

As proposed by the "protein-only" hypothesis, the "prion" consists exclusively of a cellular host protein, PrP c , in its changed conformation (Griffith, 1967; Prusiner, 1982; Prusiner, 1991). , 1990). It consists of 209 amino acids and is covalently modified by the addition of several high mannose glycans (Endo et al. 1989). , 1996). It is clear that a full insight in prion propagation requires knowledge of the structure of PrP c and PrPSc and of the mechanism of conversion between them. , 2000) by nuclear magnetic resonance (NMR) structure determination was a first important event in this view.

To characterize the interaction of copper with biosynthetically produced PrP that contains its normal complement of posttranslational modifications, we have studied the effects of the metal on the biochemical properties of PrPc in detergent lysates of brain tissue and transfected cells (Quaglio et al, 2001). 3). 3 Cu2+ causes PrP to become PK resistant. Detergent extracts of mouse brain were incubated with the indicated concentrations of CuS04 for 30 minutes and then digested with different amounts of proteinase K (PK) for 30 min at 37°C.

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