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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: Jun 3, 2025

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Published on: November 30, 2018

Aβ40 Fibril Assembly on Human Cerebral Smooth Muscle Cells Impairs Cell Viability.

Brandon Irizarry¹, Judianne Davis², Jitika Rajpoot¹

¹Center for Structural Biology, Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York 11794-5215, United States.

|January 7, 2025

Summary

Cerebral amyloid angiopathy (CAA) involves amyloid-β (Aβ) peptide buildup in brain vessels. This study shows fibrillar Aβ seeds promote new amyloid formation on smooth muscle cells, causing cell death and advancing disease.

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Last Updated: Jun 3, 2025

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Published on: November 30, 2018

In Vitro Assays to Assess Blood-brain Barrier Mesh-like Vessel Formation and Disruption

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Published on: June 20, 2017

Visualizing Axonal Growth Cone Collapse and Early Amyloid β Effects in Cultured Mouse Neurons

Visualizing Axonal Growth Cone Collapse and Early Amyloid β Effects in Cultured Mouse Neurons

Published on: October 30, 2018

Area of Science:

Neuroscience
Biochemistry
Cell Biology

Background:

Cerebral amyloid angiopathy (CAA) is linked to brain hemorrhaging and cognitive decline in Alzheimer's disease (AD) and vascular cognitive impairment and dementia (VCID).
Familial mutations in amyloid-β (Aβ) peptide at positions 22 and 23 accelerate CAA pathology.
Human cerebral smooth muscle (HCSM) cells are key sites for amyloid deposition in cerebral blood vessels.

Purpose of the Study:

To investigate the impact of fibrillar Aβ peptides on HCSM cell viability.
To compare the effects of familial mutant Aβ40 (Dutch) with wild-type Aβ40 and Aβ42.

Main Methods:

Primary cultures of HCSM cells were treated with monomeric and fibrillar forms of Aβ peptides.
Cell viability was assessed after exposure to different Aβ variants and fibril seeds.
Intrathecal administration of Aβ40-Dutch fibrillar seeds was performed in a transgenic rat model of CAA.

Main Results:

Monomeric Aβ40-Dutch and Aβ42-WT significantly reduced HCSM cell viability, while Aβ40-WT was less toxic.
Aβ fibrils from sporadic or familial CAA did not significantly decrease HCSM cell viability upon direct binding.
Coincubation of Aβ40-WT monomers with sporadic CAA fibrils significantly reduced cell viability and increased cell surface fibril formation.
Intrathecal Aβ40-Dutch seeds promoted fibrillar amyloid accumulation in meningeal vessel smooth muscle in rats.

Conclusions:

Fibrillar Aβ seeds can propagate new amyloid fibril expansion on cerebral vascular smooth muscle.
This process leads to membrane disruption and HCSM cell death.
The findings suggest a mechanism for CAA progression involving seed-mediated amyloid expansion and vascular damage.