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Amyloid Fibrils

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...

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Related Experiment Video

Updated: Oct 15, 2025

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Published on: April 28, 2022

Evolutionary conservation of systemic and reversible amyloid aggregation.

Emma Lacroix^1,2, Lionel Pereira^1,2, Byoungjoo Yoo¹

¹Department of Molecular Biology and Biochemistry, Simon Fraser University, 8888 University Drive, Burnaby, BC V5A 1S6, Canada.

Journal of Cell Science

|October 27, 2021

Summary

Functional amyloids called amyloid bodies (A-bodies) are conserved across species as a stress response. These reversible protein aggregates are crucial for cell survival under harsh conditions.

Keywords:

A-body Amyloid aggregation Cellular stress Evolutionary conservation Subnuclear structures

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Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Published on: August 28, 2012

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Last Updated: Oct 15, 2025

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Published on: April 28, 2022

Neurodegeneration in an Animal Model of Chronic Amyloid-beta Oligomer Infusion Is Counteracted by Antibody Treatment Infused with Osmotic Pumps

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Published on: August 14, 2016

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Published on: August 28, 2012

Area of Science:

Cell Biology
Molecular Biology
Biophysics

Background:

Human cells form reversible nuclear amyloid aggregates (amyloid bodies or A-bodies) under environmental stress.
These structures share biophysical traits with pathological amyloids linked to neurodegenerative diseases like Alzheimer's and Parkinson's.

Purpose of the Study:

To investigate the evolutionary conservation and physiological role of amyloid bodies (A-bodies) across diverse eukaryotic species.
To identify the molecular mechanisms, including regulatory RNAs, involved in A-body formation.

Main Methods:

Induction of amyloid bodies (A-bodies) under various stress conditions in different species (e.g., Drosophila melanogaster, Saccharomyces cerevisiae).
Biophysical characterization of A-bodies.
RNA-sequencing to identify regulatory RNAs involved in A-body aggregation.

Main Results:

Amyloid bodies (A-bodies) are evolutionarily conserved across eukaryotes, with formation triggered by species-specific severe, sublethal stress.
Regulatory long non-coding RNAs driving A-body aggregation are conserved and essential in human, mouse, and chicken cells.
A-body formation represents a tailored, protective stress response pathway.

Conclusions:

The identification of functional, reversible amyloids in diverse species underscores their physiological importance.
Understanding A-bodies provides insights into both functional protein aggregation and the mechanisms underlying pathological amyloid diseases.