Prion diseases articles within Nature

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  • Brief Communications Arising |

    • John Collinge
    • , Zane Jaunmuktane
    •  & Sebastian Brandner

  • Letter |

    Treatment of children with human cadaver-derived growth hormone (c-hGH) contaminated with prions resulted in transmission of Creutzfeldt–Jakob disease (CJD); unexpectedly, in an autopsy study of eight such iCJD patients, the authors found amyloid-β deposition in the grey matter typical of that seen in Alzheimer's disease and amyloid-β in the blood vessel walls characteristic of cerebral amyloid angiopathy, consistent with iatrogenic transmission of amyloid-β pathology in addition to CJD and suggests that healthy c-hGH-exposed individuals may also be at risk of Alzheimer's disease and cerebral amyloid angiopathy.

    • Zane Jaunmuktane
    • , Simon Mead
    •  & Sebastian Brandner

  • Letter |

    Accumulation of prion protein during prion replication causes persistent translational repression of global protein synthesis, which is mediated by eIF2α-P and is associated with synaptic failure and neuronal loss in prion-diseased mice; promoting translational recovery in hippocampi of prion-infected mice is neuroprotective.

    • Julie A. Moreno
    • , Helois Radford
    •  & Giovanna R. Mallucci

  • News & Views |

    Prions are infectious proteins that can cause deadly diseases in mammals. Detailed measurements of infectivity suggest that there may be distinct infectious and toxic versions of this protein. See Letter p.540

    • Reed B. Wickner

  • Letter |

    Here it is shown that during the silent phase of prion infection, prions first exponentially propagate until a defined limit is reached. Then a plateau phase follows. Prion propagation is independent of prion concentration, whereas in the plateau phase the time to clinical onset is inversely correlated to prion concentration. The similar levels of infectivity at the end of the first and second phase suggests that there is a separation between prion infectivity and toxicity. Moreover, something seems to limit prion production. It is suggested that the prions are not neurotoxic themselves but catalyse the formation of such species from PrPC. Production of neurotoxic species is triggered when prion propagation saturates, leading to a switch from autocatalytic production of infectivity to a toxic pathway.

    • Malin K. Sandberg
    • , Huda Al-Doujaily
    •  & John Collinge

  • News Feature |

    Almost every human protein has segments that can form amyloids, the sticky aggregates known for their role in disease. Yet cells have evolved some elaborate defences, finds Jim Schnabel.

    • Jim Schnabel

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