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      The transcellular spread of cytosolic amyloids, prions, and prionoids.

      1 ,
      Neuron
      Elsevier BV

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          Abstract

          Recent reports indicate that a growing number of intracellular proteins are not only prone to pathological aggregation but can also be released and "infect" neighboring cells. Therefore, many complex diseases may obey a simple model of propagation where the penetration of seeds into hosts determines spatial spread and disease progression. We term these proteins prionoids, as they appear to infect their neighbors just like prions--but how can bulky protein aggregates be released from cells and how do they access other cells? The widespread existence of such prionoids raises unexpected issues that question our understanding of basic cell biology.

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          Author and article information

          Journal
          Neuron
          Neuron
          Elsevier BV
          1097-4199
          0896-6273
          Dec 24 2009
          : 64
          : 6
          Affiliations
          [1 ] Institute of Neuropathology, University Hospital of Zürich, Schmelzbergstrasse 12, CH-8091 Zürich, Switzerland. adriano.aguzzi@usz.ch
          Article
          S0896-6273(09)01006-X
          10.1016/j.neuron.2009.12.016
          20064386
          5de43e41-436c-4cfc-a18b-bd8f5380542b
          2009 Elsevier Inc. All rights reserved.
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