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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 8, 2026

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging
10:04

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

Published on: October 20, 2017

How to diagnose amyloidosis.

P Mollee1, P Renaut, D Gottlieb

  • 1Haematology Department, Pathology Queensland, Princess Alexandra Hospital, Brisbane, Queensland, Australia; School of Medicine, University of Queensland, Brisbane, Queensland, Australia.

Internal Medicine Journal
|September 13, 2013
PubMed
Summary
This summary is machine-generated.

Amyloidosis diagnosis requires high clinical suspicion and accurate identification of the amyloid protein. This review outlines diagnostic strategies and limitations, particularly in Australia and New Zealand, for effective patient management.

Keywords:
amyloidosisdiagnosisgenetic testingimmunohistochemistryproteomics

More Related Videos

Performing and Processing FNA of Anterior Fat Pad for Amyloid
09:41

Performing and Processing FNA of Anterior Fat Pad for Amyloid

Published on: October 30, 2010

Related Experiment Videos

Last Updated: May 8, 2026

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging
10:04

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

Published on: October 20, 2017

Performing and Processing FNA of Anterior Fat Pad for Amyloid
09:41

Performing and Processing FNA of Anterior Fat Pad for Amyloid

Published on: October 30, 2010

Area of Science:

  • Medicine
  • Pathology
  • Genetics

Background:

  • Amyloidosis involves misfolded protein deposition, impairing organ function.
  • Early diagnosis and correct protein identification are vital for management, prognosis, and genetic counseling.
  • High clinical suspicion is essential for timely detection.

Purpose of the Study:

  • To review current evidence for amyloidosis diagnosis and subtyping.
  • To outline limitations of diagnostic techniques in Australia and New Zealand.
  • To discuss optimal diagnostic strategies and provide recommendations.

Main Methods:

  • Literature review of diagnostic techniques for amyloidosis.
  • Analysis of diagnostic approaches in the Australian and New Zealand context.
  • Synthesis of evidence for clinical suspicion and investigation.

Main Results:

  • Current diagnostic techniques have limitations.
  • Accurate amyloid protein identification is crucial for patient care.
  • Optimal diagnostic strategies are needed for effective management.

Conclusions:

  • A systematic approach to diagnosis and subtyping is essential for amyloidosis.
  • Understanding diagnostic limitations improves patient outcomes.
  • Recommendations are provided for suspecting and investigating amyloidosis.