Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?

Hilal A. Lashuel, Peter T. Lansbury

Research output: Contribution to journalReview article

306 Citations (Scopus)

Abstract

Protein fibrillization is implicated in the pathogenesis of most, if not all, age-associated neurodegenerative diseases, but the mechanism(s) by which it triggers neuronal death is unknown. Reductionist in vitro studies suggest that the amyloid protofibril may be the toxic species and that it may amplify itself by inhibiting proteasome-dependent protein degradation. Although its pathogenic target has not been identified, the properties of the protofibril suggest that neurons could be killed by unregulated membrane permeabilization, possibly by a type of protofibril referred to here as the 'amyloid pore'. The purpose of this review is to summarize the existing supportive circumstantial evidence and to stimulate further studies designed to test the validity of this hypothesis.

Original languageEnglish
Pages (from-to)167-201
Number of pages35
JournalQuarterly Reviews of Biophysics
Volume39
Issue number2
DOIs
Publication statusPublished - 1 May 2006

ASJC Scopus subject areas

  • Biophysics

Fingerprint Dive into the research topics of 'Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?'. Together they form a unique fingerprint.

  • Cite this