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Amyloid Fibrils03:03

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,...
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Amyloid Fibrils03:03

Amyloid Fibrils

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Alzheimer Disease ll: Pathophysiology01:23

Alzheimer Disease ll: Pathophysiology

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Alzheimer disease involves structural changes in the brain that begin long before symptoms appear. The most distinctive features are extracellular neuritic plaques and intracellular neurofibrillary tangles.Neuritic plaques form in the cerebral cortex and around blood vessels. These plaques contain a dense core of beta-amyloid (Aβ)—a toxic protein fragment that clumps outside neurons. The core is surrounded by damaged neuronal extensions, as well as reactive astrocytes and...
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Related Experiment Video

Updated: May 2, 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

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LECT2 makes the amyloid list.

Raymond L Comenzo1

  • 1TUFTS UNIVERSITY.

Blood
|March 15, 2014
PubMed
Summary

Leukocyte cell–derived chemotaxin 2 (LECT2) is now recognized as a cause of systemic amyloidosis. This protein deposition disease leads to organ damage and requires specific diagnostic methods for identification.

Area of Science:

  • Hematology
  • Protein Biochemistry
  • Pathology

Background:

  • Systemic amyloidosis is a group of diseases characterized by fibrillar protein deposition in tissues.
  • Diagnosis typically requires microscopic examination of Congo Red-stained tissue sections, showing apple-green birefringence.
  • Identifying the specific amyloid-forming protein is crucial for understanding disease mechanisms.

Purpose of the Study:

  • To identify novel proteins implicated in the pathogenesis of systemic amyloidosis.
  • To expand the list of known amyloidogenic proteins.

Main Methods:

  • Analysis of amyloid deposits from affected tissues.
  • Proteomic analysis of digested protein fragments.
  • Mass spectrometry to identify constituent proteins.

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Rapid Generation of Amyloid from Native Proteins In vitro
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A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation
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A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

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Related Experiment Videos

Last Updated: May 2, 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

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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

5.9K
A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation
06:34

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

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Main Results:

  • Leukocyte cell–derived chemotaxin 2 (LECT2) was identified as the primary amyloid-forming protein in a subset of systemic amyloidosis cases.
  • Amyloid deposits were characterized by the presence of chaperones like apolipoprotein E and serum amyloid P-component.

Conclusions:

  • LECT2 should be added to the list of proteins capable of causing systemic amyloidosis.
  • This finding expands the etiological spectrum of amyloidosis and may inform future diagnostic and therapeutic strategies.