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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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Lysosomal Hydrolases

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Related Experiment Video

Updated: Jun 13, 2026

Genetic Analysis of Hereditary Transthyretin Ala97Ser Related Amyloidosis
06:33

Genetic Analysis of Hereditary Transthyretin Ala97Ser Related Amyloidosis

Published on: June 9, 2018

LECT2 amyloidosis.

Merrill D Benson1

  • 1Department of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, Indiana 46202 - 5126, USA. mdbenson@iupui.edu

Kidney International
|April 16, 2010
PubMed
Summary
This summary is machine-generated.

New LECT2 amyloidosis, a systemic disease, affects kidneys causing nephrotic syndrome and renal failure. Early clinical and pathological signs of this amyloidosis remain unknown.

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

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Rapid Generation of Amyloid from Native Proteins In vitro
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Rapid Generation of Amyloid from Native Proteins In vitro

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Last Updated: Jun 13, 2026

Genetic Analysis of Hereditary Transthyretin Ala97Ser Related Amyloidosis
06:33

Genetic Analysis of Hereditary Transthyretin Ala97Ser Related Amyloidosis

Published on: June 9, 2018

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

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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:

  • Nephrology
  • Pathology
  • Genetics

Background:

  • LECT2 amyloidosis is a recently identified systemic amyloidosis.
  • It is characterized by amyloid deposition in the glomeruli, renal vessels, and interstitium.
  • This condition has been observed in patients presenting with nephrotic syndrome and renal failure.

Discussion:

  • The discovery of LECT2 amyloidosis expands the spectrum of systemic amyloidoses.
  • Renal involvement is a key feature, manifesting as nephrotic syndrome and renal failure.
  • Understanding the specific mechanisms of LECT2 protein aggregation and deposition is crucial.

Key Insights:

  • LECT2 amyloidosis is a distinct systemic amyloidosis.
  • Kidney pathology is central to its presentation.
  • Early diagnostic markers and disease progression are currently undefined.

Outlook:

  • Further research is needed to elucidate the early clinical and pathological manifestations of LECT2 amyloidosis.
  • Investigating the genetic and molecular underpinnings of LECT2 amyloid formation will be essential.
  • Developing diagnostic tools and therapeutic strategies for LECT2 amyloidosis is a future priority.