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...
Parkinson Disease ll: Pathophysiology01:24

Parkinson Disease ll: Pathophysiology

Parkinson disease (PD) is a progressive neurodegenerative disorder primarily affecting movement, with additional non-motor features. Its pathophysiology involves complex interactions among genetic susceptibility, environmental exposures, and cellular dysfunction, including dopaminergic neuron loss, protein aggregation, and mitochondrial impairment.Selective NeurodegenerationA key feature is the degeneration of dopaminergic neurons in the substantia nigra pars compacta, leading to reduced...
Huntington Disease l: Introduction01:21

Huntington Disease l: Introduction

Huntington disease or HD is a progressive, fatal neurodegenerative disorder inherited in an autosomal dominant pattern.PathophysiologyIt is caused by expansion of the CAG trinucleotide repeat in the HTT gene on chromosome 4 (4p16.3), producing an abnormal huntingtin protein with an expanded polyglutamine tract. This misfolded protein disrupts cellular function, leading to neuronal death. Normal alleles have ≤26 repeats, 27–35 are intermediate (risk of expansion), 36–39 show reduced penetrance,...
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...

You might also read

Related Articles

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

Sort by
Same author

The growing pipeline of natural aminoacyl-tRNA synthetase inhibitors for malaria treatment.

Bioengineered·2016
Same author

Rescue from tau-induced neuronal dysfunction produces insoluble tau oligomers.

Scientific reports·2015
Same author

Neuronal glycogen synthesis contributes to physiological aging.

Aging cell·2014
Same author

Neurons have an active glycogen metabolism that contributes to tolerance to hypoxia.

Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism·2014
Same author

DJ-1 modulates aggregation and pathogenesis in models of Huntington's disease.

Human molecular genetics·2013
Same author

Low endogenous and chemical induced heat shock protein induction in a 0N3Rtau-expressing Drosophila larval model of Alzheimer's disease.

Journal of Alzheimer's disease : JAD·2012
Same journal

Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Molecular Basis of Disease Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

General Subjects Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Erratum to 'on the role of exchangeable hydrogen bonds for the kinetics of P680<sup>+·</sup> Q<sub>A</sub> <sup>-·</sup> formation and P680<sup>+·</sup> Pheo<sup>-·</sup> recombination in photosystem II' [Biochim. Biophys. Acta 1276 (1996) 35-44].

Biochimica et biophysica acta·2019
Same journal

Oligomeric state of the light-harvesting complexes B800-850 and B875 from purple bacterium Rubrivivax gelatinosus in detergent solution.

Biochimica et biophysica acta·2019
Same journal

Regulation of pigment content and enzyme activity in the cyanobacterium Nostoc sp. Mac grown in continuous light, a light-dark photoperiod, or darkness.

Biochimica et biophysica acta·2019
See all related articles

Related Experiment Video

Updated: Jul 4, 2026

Caenorhabditis elegans as a Model System for Discovering Bioactive Compounds Against Polyglutamine-Mediated Neurotoxicity
08:16

Caenorhabditis elegans as a Model System for Discovering Bioactive Compounds Against Polyglutamine-Mediated Neurotoxicity

Published on: September 21, 2021

Polyglutamine gene function and dysfunction in the ageing brain.

Sarah Hands1, Christopher Sinadinos, Andreas Wyttenbach

  • 1Southampton Neuroscience Group, School of Biological Sciences, University of Southampton, Southampton SO16 7PX, UK.

Biochimica Et Biophysica Acta
|June 28, 2008
PubMed
Summary
This summary is machine-generated.

CAG expansion mutations in polyglutamine (polyQ) disorders disrupt nervous system function and aging pathways. These genetic changes lead to neurodegeneration, mirroring age-related conditions like Alzheimer's and Parkinson's diseases.

More Related Videos

Growth Assays to Assess Polyglutamine Toxicity in Yeast
09:06

Growth Assays to Assess Polyglutamine Toxicity in Yeast

Published on: March 5, 2012

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans
06:49

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

Published on: December 17, 2021

Related Experiment Videos

Last Updated: Jul 4, 2026

Caenorhabditis elegans as a Model System for Discovering Bioactive Compounds Against Polyglutamine-Mediated Neurotoxicity
08:16

Caenorhabditis elegans as a Model System for Discovering Bioactive Compounds Against Polyglutamine-Mediated Neurotoxicity

Published on: September 21, 2021

Growth Assays to Assess Polyglutamine Toxicity in Yeast
09:06

Growth Assays to Assess Polyglutamine Toxicity in Yeast

Published on: March 5, 2012

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans
06:49

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

Published on: December 17, 2021

Area of Science:

  • Neuroscience
  • Genetics
  • Molecular Biology

Background:

  • Gene expression and protein interactions are crucial for nervous system development, function, and plasticity.
  • Polyglutamine (polyQ) disorders are linked to mutations in genes with CAG/glutamine repeats, affecting transcriptional regulation and protein interactions.
  • The precise roles of CAG and other low-complexity sequences in eukaryotic genomes remain incompletely understood.

Purpose of the Study:

  • To review the function of genes implicated in polyglutamine disorders within the nervous system.
  • To elucidate how expanded CAG/glutamine repeats cause neuronal dysfunction, with a focus on Huntington's disease (HD).
  • To explore the connection between CAG expansion-induced molecular/cellular pathway dysfunction and central nervous system aging.

Main Methods:

  • Review of scientific literature on polyglutamine disorders and neurodegeneration.
  • Analysis of the role of CAG/glutamine repeat expansions in gene function and protein interactions.
  • Examination of molecular and cellular pathways affected by CAG expansion mutations.

Main Results:

  • CAG/glutamine stretches are vital for transcriptional regulation and protein interactions.
  • Expanded CAG repeats in polyQ disorders lead to neuronal dysfunction and pathology.
  • Dysfunctional pathways include protein degradation, axonal transport, redox homeostasis, and bioenergetics.

Conclusions:

  • CAG expansion mutations alter protein properties, causing slow neurodegeneration similar to aging-related diseases.
  • The molecular and cellular pathways disrupted in polyQ disorders are also implicated in the aging of the central nervous system.
  • Understanding these pathways offers insights into both genetic neurodegenerative disorders and the aging process.