. Cell biology. Prion toxicity: all sail and no anchor. Science. 2005 Jun 3;308(5727):1420-1. PubMed.


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  1. I believe these are potentially very significant findings.

    View all comments by J. Lucy Boyd
  2. Prion disorders include Creutzfeldt Jakob disease in humans, bovine spongiform encephalopathy in cattle, and chronic wasting disease in the deer and elk population of North America. The underlying pathogenic and infectious particle in all prion disorders is the scrapie prion protein that arises from a change in conformation of the host-encoded prion protein to the pathogenic, scrapie form. Deposits of scrapie prion protein in the brain parenchyma have been considered hallmarks of prion disorders, until the recent report by Chesebro and colleagues that provides a new perspective on this much-debated question.

    By infecting transgenic mice expressing a soluble form of the prion protein, the authors demonstrate accumulation of scrapie plaques without clinical symptoms of prion disease. Although accumulated plaques resemble those observed in Alzheimer disease, lack of associated pathology provides a new perspective on the pathophysiology of prion disorders, and by extension, Alzheimer disease. This study demonstrates that, contrary to current belief, the plaques may in fact be neuroprotective, sequestering the more toxic molecules into an innocuous clump. This concept, though not totally novel, will change the therapeutic strategies that are currently aimed at reducing the plaque load in both prion and Alzheimer diseases.

    View all comments by Neena Singh

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This paper appears in the following:


  1. Anchors Aweigh—Making Amyloid out of Prions