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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,...

Amyloid Fibrils

Amyloid Fibrils

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Related Experiment Video

Updated: Apr 2, 2026

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

Published on: October 17, 2015

The Uppsala APP Mutation Promotes Wild-Type Amyloid-β Aggregation and Deposition In Vivo.

Junyue Ge¹, María Pagnon de la Vega², Silvia Zampar^3,4

¹Department of Psychiatry and Neurochemistry, University of Gothenburg, Gothenburg, Sweden.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)

|March 31, 2026

Summary

This summary is machine-generated.

Amyloid-beta Upp (AβUpp) accelerates the aggregation of wild-type amyloid-beta (Aβwt) in Alzheimer's disease models. This interaction leads to increased plaque formation and gliosis, mimicking human disease progression more closely.

Keywords:

Alzheimer's disease Uppsala mutation beta‐amyloid mass spectrometry imaging plaque pathology

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Last Updated: Apr 2, 2026

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

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Published on: October 17, 2015

Detecting Amyloid-β Accumulation via Immunofluorescent Staining in a Mouse Model of Alzheimer's Disease

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Published on: April 19, 2021

Stereotaxic Infusion of Oligomeric Amyloid-beta into the Mouse Hippocampus

Stereotaxic Infusion of Oligomeric Amyloid-beta into the Mouse Hippocampus

Published on: June 17, 2015

Area of Science:

Neuroscience
Molecular Biology
Genetics

Background:

Amyloid-beta (Aβ) aggregation is central to Alzheimer's disease (AD) pathogenesis.
Mutations in the amyloid precursor protein (APP) gene, like Uppsala APP (APPUpp), yield aggregation-prone Aβ variants.
APPUpp produces AβUpp42Δ19-24, a highly aggregation-prone mutant.

Purpose of the Study:

To investigate the pathological interplay between wild-type Aβ (Aβwt) and the AβUpp mutant.
To develop a more accurate mouse model for studying APPUpp-associated Alzheimer's disease.
To understand how AβUpp influences Aβwt aggregation and plaque formation.

Main Methods:

In vitro co-aggregation assays.
In vivo studies using a novel bitransgenic mouse model (tg-UppSwe x tg-Swe).
ELISA, immunohistochemistry, and MALDI mass spectrometry imaging.

Main Results:

Early deposition of AβUpp42Δ19-24 accelerates the aggregation and deposition of Aβwt species (Aβwt38, Aβwt40, Aβwt42).
A synergistic, seeding, or catalytic mechanism is proposed for AβUpp's effect on Aβwt.
Bitransgenic mice exhibited pronounced plaque-associated gliosis, unlike tg-UppSwe mice.

Conclusions:

AβUpp and Aβwt interact synergistically in Alzheimer's disease pathology.
This interaction influences the onset, progression, and structural characteristics of Aβ plaques.
The findings provide insights into the disease mechanisms in APPUpp mutation carriers.