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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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Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...

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Related Experiment Video

Updated: May 21, 2026

Neurodegeneration in an Animal Model of Chronic Amyloid-beta Oligomer Infusion Is Counteracted by Antibody Treatment Infused with Osmotic Pumps
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Neurodegeneration in an Animal Model of Chronic Amyloid-beta Oligomer Infusion Is Counteracted by Antibody Treatment Infused with Osmotic Pumps

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Amyloid-β peptide: Dr. Jekyll or Mr. Hyde?

Daniela Puzzo1, Ottavio Arancio

  • 1Department of Bio-Medical Sciences, Section of Physiology, University of Catania, Catania, Italy.

Journal of Alzheimer'S Disease : JAD
|June 28, 2012
PubMed
Summary

Amyloid-beta (Aβ) peptides, often linked to Alzheimer's disease, are essential for healthy brain function, synaptic plasticity, and memory. Lowering Aβ levels impairs cognitive functions, highlighting its physiological role.

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Stereotaxic Infusion of Oligomeric Amyloid-beta into the Mouse Hippocampus
08:16

Stereotaxic Infusion of Oligomeric Amyloid-beta into the Mouse Hippocampus

Published on: June 17, 2015

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Pathology

Background:

  • Amyloid-beta (Aβ) peptides are implicated in Alzheimer's disease (AD) pathogenesis due to neurotoxicity and plaque formation.
  • Aβ originates from the amyloid-beta protein precursor (AβPP), whose processing yields various Aβ fragments.
  • The physiological function of AβPP and its fragments, particularly Aβ, is not well understood, with Aβ often considered a toxic byproduct.

Purpose of the Study:

  • To investigate the potential physiological role of Aβ in the healthy brain.
  • To determine if Aβ concentrations are necessary for normal synaptic plasticity and memory.
  • To explore the mechanisms underlying Aβ's effects on neurotransmission and cognitive function.

Main Methods:

  • Administered picomolar concentrations of human Aβ42 to mice to assess effects on synaptic plasticity and memory.
  • Utilized an anti-rodent Aβ antibody and siRNA against murine AβPP to reduce endogenous Aβ levels in healthy mice.
  • Investigated the role of neurotransmitter release and α7-nicotinic receptors in mediating Aβ's effects.

Main Results:

  • Picomolar Aβ42 enhanced synaptic plasticity and memory in mice.
  • Inhibition of endogenous Aβ production in mice impaired synaptic plasticity and memory.
  • Administration of human Aβ42 rescued deficits caused by reduced endogenous Aβ.
  • Aβ's effects were mediated by modulating neurotransmitter release and α7-nicotinic receptors.

Conclusions:

  • Physiological concentrations of Aβ are necessary for normal synaptic plasticity and memory in the healthy brain.
  • Aβ is not merely a toxic "garbage" fragment but plays a crucial physiological role.
  • Findings necessitate re-evaluation of therapeutic strategies for Alzheimer's disease, considering Aβ's normal function.