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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: Jun 27, 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

Amyloidosis-recent developments.

Tom Pettersson1, Yrjö T Konttinen

  • 1Department of Medicine, Helsinki University Central Hospital, Helsinki, Finland. tom.pettersson@helsinki.fi

Seminars in Arthritis and Rheumatism
|November 22, 2008
PubMed
Summary
This summary is machine-generated.

Amyloidosis is a complex disease with 27 human types, diagnosed via tissue microscopy and precursor identification. Treatment focuses on managing the underlying cause and precursor production for better prognosis.

More Related Videos

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

Related Experiment Videos

Last Updated: Jun 27, 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

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

Area of Science:

  • Medical Science
  • Pathology
  • Genetics

Background:

  • Amyloidosis involves abnormal protein deposits causing organ damage.
  • Early suspicion is key, especially in patients with inflammatory diseases or genetic predispositions.
  • Understanding pathomechanisms is crucial for diagnosis and treatment.

Purpose of the Study:

  • To comprehensively review amyloidosis, covering clinical presentation, diagnosis, classification, grading, prognosis, and treatment.
  • To integrate pathomechanistic insights with clinical management strategies.
  • To highlight the evolving understanding and classification of amyloidosis.

Main Methods:

  • Literature search of PubMed and MEDLINE (1990-2007) using the keyword "amyloidosis".
  • Evaluation based on authors' clinical experience and existing research.
  • Review of diagnostic techniques including microscopy, immunohistochemistry, sequencing, proteomics, and genetic testing.

Main Results:

  • Clinical suspicion arises from specific syndromes in patients with chronic inflammatory diseases, plasma cell dyscrasias, or hereditary amyloidosis.
  • Diagnosis confirmed by Congo red microscopy showing birefringent amyloid, with typing via precursor identification (immunohistochemistry, sequencing, proteomics).
  • Amyloidosis encompasses 27 human and 9 animal types; grading (mild, moderate, severe) and prognosis are linked to precursor synthesis and concentration. Treatment requires accurate underlying disease diagnosis and precursor production inhibition, often with organ-specific interventions.

Conclusions:

  • Continued research into pathogenesis and protein structure-function is vital.
  • Development of novel therapies targeting protein misfolding, aggregation, and clearance is anticipated.
  • Advancements in understanding amyloidosis will drive new therapeutic strategies.