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Related Concept Videos

Amyloid Fibrils03:03

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...
Amyloid Fibrils03:03

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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Related Experiment Video

Updated: May 16, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

β(2)-microglobulin amyloidosis.

Dorthe B Corlin1, Niels H H Heegaard

  • 1Department of Clinical Biochemistry and Immunology, Division of Microbiology and Diagnostics, Statens Serum Institut, Bldg. 85/240, Artillerivej 5, 2300, Copenhagen S, Denmark, dbcw@novonordisk.com.

Sub-Cellular Biochemistry
|December 11, 2012
PubMed
Summary

Dialysis-related amyloidosis (DRA) occurs in long-term hemodialysis patients. This review explores how beta(2)-microglobulin (β(2)m) forms amyloid, causing pain and dysfunction in DRA.

Area of Science:

  • Biochemistry
  • Nephrology
  • Rheumatology

Background:

  • Dialysis-related amyloidosis (DRA) is a complication of long-term hemodialysis.
  • It involves the deposition of beta(2)-microglobulin (β(2)m) amyloid in the musculoskeletal system, causing pain and functional loss.
  • The exact mechanisms of β(2)m amyloid formation in DRA patients remain unclear.

Purpose of the Study:

  • To review current knowledge on the mechanisms of β(2)m amyloid formation in dialysis-related amyloidosis.
  • To elucidate the factors contributing to the development of DRA syndrome.

Main Methods:

  • Literature review of existing studies on β(2)m amyloidosis.
  • Analysis of proposed molecular mechanisms and contributing factors.

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Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry
09:31

Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry

Published on: March 7, 2019

Related Experiment Videos

Last Updated: May 16, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry
09:31

Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry

Published on: March 7, 2019

Main Results:

  • β(2)m amyloid formation involves conformational changes, particularly around the D-strand, DE-loop, and Pro32 peptide bond.
  • High circulating β(2)m levels, post-translational modifications in a pro-inflammatory uremic environment, metal ions (Cu2+), uremic toxins, and redox processes are crucial.
  • Domain-swapped β(2)m dimers likely form the building blocks of amyloid fibrils.
  • Activated complement and cellular pathways perpetuate the process, leading to DRA.

Conclusions:

  • DRA pathogenesis is multifactorial, involving protein misfolding, biochemical modifications, and inflammatory processes.
  • Understanding these mechanisms is key to developing strategies for preventing or treating DRA.