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Amyloid Fibrils

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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, normally used to...

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, normally used to...

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Methods for Detecting Cytotoxic Amyloids Following Infection of Pulmonary Endothelial Cells by Pseudomonas aeruginosa

Methods for Detecting Cytotoxic Amyloids Following Infection of Pulmonary Endothelial Cells by Pseudomonas aeruginosa

Published on: July 12, 2018

Systemic amyloidoses.

Luis M Blancas-Mejía¹, Marina Ramirez-Alvarado

¹Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905, USA. Blancasmejia.luis@mayo.edu

Annual Review of Biochemistry

|March 5, 2013

Summary

This summary is machine-generated.

Amyloidosis comprises protein misfolding diseases causing organ failure. This review details their pathophysiology, focusing on light chain amyloidosis and future research directions for systemic forms.

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Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

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Published on: September 28, 2019

Area of Science:

* Pathology and Medicine
* Biochemistry and Biophysics

Background:

* Amyloidoses are protein misfolding diseases characterized by amyloid fibril formation in tissues.
* These diseases can be localized or systemic, leading to cell death and organ failure.
* Understanding the complex pathophysiology is crucial for developing effective treatments.

Purpose of the Study:

* To review the proteins, cells, and pathophysiology of amyloidoses.
* To highlight light chain amyloidosis as a model for understanding pathogenesis.
* To discuss current models and future research opportunities for systemic amyloidoses.

Main Methods:

* Comprehensive literature review of amyloidosis research.
* Focus on biochemical and biophysical studies of light chain amyloidosis.
* Analysis of cellular, tissue, and animal models.

Main Results:

* Amyloidosis involves protein misfolding, conformational changes, and fibril formation.
* Systemic amyloidosis involves deposition distant from precursor protein synthesis.
* Biochemical and biophysical insights have advanced understanding of light chain amyloidosis pathogenesis.

Conclusions:

* Amyloidosis represents a significant challenge in medicine due to its complex pathophysiology.
* Light chain amyloidosis serves as a key model for studying disease mechanisms.
* Further research using diverse models is essential for addressing systemic amyloidoses.