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Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis

Charles G Glabe1, Rakez Kayed

  • 1Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, USA. cglabe@uci.edu

Neurology
|January 25, 2006
PubMed

Insights

Soluble amyloid oligomers are key in degenerative diseases, causing cell damage by permeabilizing membranes. This leads to common downstream effects like calcium imbalance and mitochondrial dysfunction, impacting diseases such as inclusion-body myositis.

Area of Science:

  • Neuroscience
  • Cell Biology
  • Pathology

Background:

  • Soluble amyloid oligomers are increasingly recognized as central players in various degenerative diseases.
  • These oligomers exhibit shared structural characteristics and membrane-disrupting capabilities.

Purpose of the Study:

  • To elucidate the common pathogenic mechanism initiated by amyloid oligomers.
  • To connect membrane permeabilization by oligomers to downstream cellular dysfunction in diseases like sporadic inclusion-body myositis.

Main Methods:

  • The study reviews recent findings on amyloid oligomer structure and function.
  • It synthesizes evidence linking membrane permeabilization to specific cellular events.

Main Results:

  • Amyloid oligomers share common structural features and membrane-permeabilizing activity.
  • Membrane permeabilization triggers a cascade of cellular dysfunctions, including calcium dyshomeostasis, oxidative stress, and mitochondrial impairment.

Conclusions:

  • A common pathogenic pathway initiated by amyloid oligomers involves membrane permeabilization.
  • This pathway contributes significantly to cellular dysfunction and death in amyloid-associated degenerative conditions, exemplified by sporadic inclusion-body myositis.

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