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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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Updated: Jun 8, 2025

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

The Icelandic Mutation (APP-A673T) Is Protective against Amyloid Pathology In Vivo.

Sho Shimohama^1,2, Ryo Fujioka¹, Naomi Mihira¹

¹Dementia Pathophysiology Collaboration Unit, RIKEN Center for Brain Science, Wako, Saitama 351-0198, Japan.

The Journal of Neuroscience : the Official Journal of the Society for Neuroscience

|November 4, 2024

Summary

The Icelandic mutation (A673T) in amyloid precursor protein (APP) gene protects against Alzheimer's disease (AD) by reducing amyloid pathology in vivo. This finding suggests novel therapeutic strategies for AD prevention.

Keywords:

Alzheimer’s disease App knock-in mice Icelandic mutation amyloid pathology amyloid precursor protein protective mutation

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Last Updated: Jun 8, 2025

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

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

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Published on: October 17, 2015

Quantitative 3D In Silico Modeling q3DISM of Cerebral Amyloid-beta Phagocytosis in Rodent Models of Alzheimer's Disease

Quantitative 3D In Silico Modeling q3DISM of Cerebral Amyloid-beta Phagocytosis in Rodent Models of Alzheimer's Disease

Published on: December 26, 2016

Area of Science:

Neuroscience
Genetics
Molecular Biology

Background:

Epidemiological studies suggest the APP A673T mutation (Icelandic mutation) confers protection against Alzheimer's disease (AD).
Previous investigations into the A673T mutation's effect on APP processing were primarily in vitro, lacking in vivo validation.
Existing AD mouse models often carry the Swedish mutation, potentially interfering with studies on the Icelandic mutation due to opposing effects on APP β-cleavage.

Purpose of the Study:

To evaluate the in vivo impact of the A673T mutation on amyloid pathology and neuroinflammation in Alzheimer's disease.
To generate and characterize a novel mouse model carrying the A673T mutation in an App background free of the Swedish mutation.

Main Methods:

Introduced the A673T mutation into App knock-in mice lacking the Swedish mutation.
Assessed the effects of the A673T mutation on amyloid precursor protein (APP) processing, Aβ production, amyloid pathology, neuroinflammation, and neuritic alterations in vivo.
Studied both male and female mice to ensure comprehensive analysis.

Main Results:

The APP A673T mutation significantly downregulated APP β-cleavage, reducing Aβ production and amyloid pathology in the brain.
The Icelandic mutation demonstrated a protective effect against neuroinflammation and neuritic alterations.
This study provides the first in vivo evidence of the Icelandic mutation's protective role in amyloid pathology.

Conclusions:

The A673T Icelandic mutation offers in vivo protection against Alzheimer's disease pathology.
Targeting APP-BACE1 interaction or utilizing gene editing to introduce protective mutations like A673T are potential therapeutic strategies for AD.
These findings open avenues for novel treatments for individuals at high risk for Alzheimer's disease.