Protein misfolding and disease: the case of prion disorders |
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Authors: | C Hetz C Soto |
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Institution: | (1) Serono Pharmaceutical Research Institute, 14 Chemin des Aulx, 1228 Plan les Ouates (Switzerland), CH;(2) Instituto de Ciencias Biomédicas, Universidad de Chile, Santiago (Chile), CL |
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Abstract: | Recent findings strongly support the hypothesis that diverse human disorders, including the most common neurodegenerative
diseases, arise from misfolding and aggregation of an underlying protein. Despite the good evidence for the involvement of
protein misfolding in disease pathogenesis, the mechanism by which protein conformational changes participate in the disease
is still unclear. Among the best-studied diseases of this group are the transmissible spongiform encephalopathies or prion-related
disorders, in which misfolding of the normal prion protein plays a key role in the disease. In this article we review recent
data on the link between prion protein misfolding and the pathogensis of spongiform encephalopathies.
Received 15 July 2002; received after revision 19 August 2002; accepted 23 August 2002
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ID="*"Corresponding author. |
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Keywords: | , Protein conformational disorders, prion protein misfolding, transmissible spongiform encephalopathies, neuronal,,,,,apoptosis, brain inflammation, prion protein function, |
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