Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

Monica Bucciantini, Elisa Giannoni, Fabrizio Chiti, Fabiana Baroni, Lucia Formigli, Jesús Zurdo, Niccolò Taddei, Giampietro Ramponi, Christopher M. Dobson () and Massimo Stefani ()
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Monica Bucciantini: Universitá degli Studi di Firenze
Elisa Giannoni: Universitá degli Studi di Firenze
Fabrizio Chiti: Universitá degli Studi di Firenze
Fabiana Baroni: Universitá degli Studi di Firenze
Lucia Formigli: Universitá degli Studi di Firenze
Jesús Zurdo: University of Cambridge
Niccolò Taddei: Universitá degli Studi di Firenze
Giampietro Ramponi: Universitá degli Studi di Firenze
Christopher M. Dobson: University of Cambridge
Massimo Stefani: Universitá degli Studi di Firenze

Nature, 2002, vol. 416, issue 6880, 507-511

Abstract: Abstract A range of human degenerative conditions, including Alzheimer's disease, light-chain amyloidosis and the spongiform encephalopathies, is associated with the deposition in tissue of proteinaceous aggregates known as amyloid fibrils or plaques. It has been shown previously that fibrillar aggregates that are closely similar to those associated with clinical amyloidoses can be formed in vitro from proteins not connected with these diseases, including the SH3 domain from bovine phosphatidyl-inositol-3′-kinase and the amino-terminal domain of the Escherichia coli HypF protein. Here we show that species formed early in the aggregation of these non-disease-associated proteins can be inherently highly cytotoxic. This finding provides added evidence that avoidance of protein aggregation is crucial for the preservation of biological function and suggests common features in the origins of this family of protein deposition diseases.

Date: 2002
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DOI: 10.1038/416507a

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