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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...
Alzheimer Disease ll: Pathophysiology01:23

Alzheimer Disease ll: Pathophysiology

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 microglia. Abnormal...

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Related Experiment Video

Updated: Jun 3, 2026

Correlative Light and Electron Microscopy to Study Microglial Interactions with β-Amyloid Plaques
10:52

Correlative Light and Electron Microscopy to Study Microglial Interactions with β-Amyloid Plaques

Published on: June 1, 2016

Microglia demonstrate age-dependent interaction with amyloid-β fibrils.

Angela Marie Floden1, Colin Kelly Combs

  • 1Department of Pharmacology, Physiology and Therapeutics, University of North Dakota School of Medicine and Health Sciences, Grand Forks, ND 58203-9037, USA.

Journal of Alzheimer'S Disease : JAD
|March 16, 2011
PubMed
Summary

Microglia in Alzheimer's disease (AD) lose their ability to clear amyloid-beta (Aβ) plaques with age. This study reveals a critical developmental window around 6 months where this phagocytic function is lost, impacting AD progression.

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Immunofluorescence Staining Using IBA1 and TMEM119 for Microglial Density, Morphology and Peripheral Myeloid Cell Infiltration Analysis in Mouse Brain
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Immunofluorescence Staining Using IBA1 and TMEM119 for Microglial Density, Morphology and Peripheral Myeloid Cell Infiltration Analysis in Mouse Brain

Published on: October 27, 2019

Quantitative 3D In Silico Modeling (q3DISM) of Cerebral Amyloid-beta Phagocytosis in Rodent Models of Alzheimer's Disease
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Quantitative 3D In Silico Modeling (q3DISM) of Cerebral Amyloid-beta Phagocytosis in Rodent Models of Alzheimer's Disease

Published on: December 26, 2016

Related Experiment Videos

Last Updated: Jun 3, 2026

Correlative Light and Electron Microscopy to Study Microglial Interactions with β-Amyloid Plaques
10:52

Correlative Light and Electron Microscopy to Study Microglial Interactions with β-Amyloid Plaques

Published on: June 1, 2016

Immunofluorescence Staining Using IBA1 and TMEM119 for Microglial Density, Morphology and Peripheral Myeloid Cell Infiltration Analysis in Mouse Brain
10:40

Immunofluorescence Staining Using IBA1 and TMEM119 for Microglial Density, Morphology and Peripheral Myeloid Cell Infiltration Analysis in Mouse Brain

Published on: October 27, 2019

Quantitative 3D In Silico Modeling (q3DISM) of Cerebral Amyloid-beta Phagocytosis in Rodent Models of Alzheimer's Disease
09:33

Quantitative 3D In Silico Modeling (q3DISM) of Cerebral Amyloid-beta Phagocytosis in Rodent Models of Alzheimer's Disease

Published on: December 26, 2016

Area of Science:

  • Neuroscience
  • Immunology
  • Aging Research

Background:

  • Alzheimer's disease (AD) is characterized by amyloid-beta (Aβ) plaque accumulation and microglial activation.
  • Microglia, the brain's immune cells, appear dysfunctional in AD, with reduced ability to clear Aβ.
  • Previous studies suggest an age-associated decline in microglial phagocytosis of Aβ.

Purpose of the Study:

  • To define the temporal profile of microglial interaction with amyloid-beta (Aβ) fibrils.
  • To investigate the age-dependent changes in microglial phagocytic capacity for Aβ.
  • To identify critical developmental periods influencing microglial Aβ clearance.

Main Methods:

  • Acutely isolated microglia from mice at postnatal day 0, 2 months, and 6 months were used.
  • Microglial phagocytosis of Aβ fibrils and bacterial bioparticles was assessed in vitro.
  • The ability of microglia to reduce Aβ plaque load in AD brain sections was evaluated.

Main Results:

  • Postnatal day 0 microglia effectively phagocytosed Aβ fibrils in a CD47-dependent manner.
  • This phagocytic ability was lost by 6 months of age in mice.
  • Adult microglia retained phagocytic function for bacterial bioparticles but showed impaired Aβ uptake, despite adhering to Aβ plaques.

Conclusions:

  • There is a specific age-associated decline in microglial phagocytosis of Aβ fibrils.
  • A critical developmental window around 6 months of age exists where microglia lose Aβ phagocytic function.
  • Understanding this temporal profile is crucial for developing therapeutic strategies targeting microglial function in Alzheimer's disease.