Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

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...
Alzheimer's Disease: Overview01:26

Alzheimer's Disease: Overview

Alzheimer's Disease (AD) is a continually advancing neurodegenerative disorder, distinguished by escalating memory loss, cognitive dysfunction, and dementia. The disease unfolds in three stages: preclinical, mild cognitive impairment (MCI), and dementia. Its onset is insidious, and the progression gradual, with the cause not well explained by other disorders.
The clinical diagnosis of AD hinges on the presence of memory and other cognitive impairments. Biomarkers, such as changes in Aβ and tau...
Alzheimer's Disease: Treatment01:22

Alzheimer's Disease: Treatment

Alzheimer's Disease (AD), a neurodegenerative disorder, is pathologically identified by amyloid plaques and neurofibrillary tangles composed of tau protein. AD pharmacotherapy aims to manage cognitive symptoms, delay disease progression, and treat behavioral symptoms. The treatment is primarily symptomatic and palliative, with no definitive disease-modifying therapy available. Cholinesterase inhibitors, including donepezil (Aricept), rivastigmine (Exelon), and galantamine (Razadyne), are...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

IgG Glycosylation Analysis in Patients with Ring14 Syndrome Unveils Novel Pathomechanisms and New Therapy Perspectives.

Biomolecules·2026
Same author

Printing to Fight Antimicrobial Resistance Through Nano/Microstructured Platforms.

Chemical record (New York, N.Y.)·2026
Same author

A splice-altering intronic variant in two multiplex families refines autosomal recessive COG4-related congenital disorder of glycosylation.

Molecular genetics and metabolism·2026
Same author

Aberrant Cell Cycle Gene Expression in a Transgenic Mouse Model of Alzheimer's Disease.

Cells·2026
Same author

Protective Functions of β-Alanyl-L-Histidine and Glycyl-L-Histidyl-L-Lysine Glycoconjugates and Copper in Concert.

Antioxidants (Basel, Switzerland)·2025
Same author

(±)-2-Cyclohexyl-5-methoxy-2H-chromene, a Synthetic 5-Methoxyflavone Derivative, Is a Selective DNA Polymerase-β Inhibitor with Neuroprotective Activity against β-Amyloid Toxicity.

ACS chemical neuroscience·2025

Related Experiment Video

Updated: Jun 20, 2026

Neurodegeneration in an Animal Model of Chronic Amyloid-beta Oligomer Infusion Is Counteracted by Antibody Treatment Infused with Osmotic Pumps
10:19

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

Published on: August 14, 2016

Beta-amyloid monomers are neuroprotective.

Maria Laura Giuffrida1, Filippo Caraci, Bruno Pignataro

  • 1Department of Pharmaceutical Sciences, University of Catania, Catania 95125, Italy.

The Journal of Neuroscience : the Official Journal of the Society for Neuroscience
|August 28, 2009
PubMed
Summary

Beta-amyloid (Abeta) monomers protect neurons from death, suggesting a loss-of-function mechanism in Alzheimer's disease. Therapies reducing Abeta burden should consider this protective role.

More Related Videos

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
06:17

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

Published on: May 22, 2018

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices
04:41

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices

Published on: July 14, 2010

Related Experiment Videos

Last Updated: Jun 20, 2026

Neurodegeneration in an Animal Model of Chronic Amyloid-beta Oligomer Infusion Is Counteracted by Antibody Treatment Infused with Osmotic Pumps
10:19

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

Published on: August 14, 2016

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
06:17

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

Published on: May 22, 2018

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices
04:41

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices

Published on: July 14, 2010

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Beta-amyloid (Abeta) protein, specifically Abeta(1-42), is implicated in Alzheimer's disease (AD) pathogenesis.
  • Abeta(1-42) oligomers are considered neurotoxic, but the function of its monomeric form is unknown.
  • The presence of Abeta(1-42) in normal individuals suggests a potential physiological role.

Purpose of the Study:

  • To investigate the function of monomeric Abeta(1-42) in neuronal survival and protection.
  • To elucidate the molecular mechanisms underlying the neuroprotective effects of Abeta(1-42) monomers.
  • To explore the implications of Abeta(1-42) monomer function for Alzheimer's disease pathology.

Main Methods:

  • Utilized synthetic Abeta(1-42) monomers and Arctic mutation variants.
  • Assessed neuronal survival under trophic deprivation and excitotoxicity.
  • Investigated the involvement of the PI-3-K/IGF-1 signaling pathway.

Main Results:

  • Synthetic Abeta(1-42) monomers demonstrated neuroprotective effects, supporting developing neuron survival and protecting mature neurons from excitotoxicity.
  • The neuroprotection was mediated by the phosphatidylinositol-3-kinase (PI-3-K) pathway, involving insulin-like growth factor-1 (IGF-1) receptors.
  • Abeta(1-42) monomers with the Arctic mutation (E22G) failed to provide neuroprotection.

Conclusions:

  • Monomeric Abeta(1-42) possesses neuroprotective properties, counteracting neurodegeneration.
  • Pathological aggregation of Abeta(1-42) may lead to neurodegeneration through a loss-of-function mechanism, depriving neurons of protective monomers.
  • Therapeutic strategies targeting Abeta burden in AD should consider the potential loss of beneficial monomeric functions.