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

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,...
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...
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...

You might also read

Related Articles

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

Sort by
Same author

A three-groups non-local model for combining heterogeneous data sources to identify genes associated with Parkinson's disease.

Biometrics·2026
Same author

Predictive Cellular Signatures from Live Human Motor Neurons Distinguish TDP-43 ALS and Enable ALS Subtype Stratification.

bioRxiv : the preprint server for biology·2026
Same author

Survey of the human proteostasis network: the ubiquitin-proteasome system.

bioRxiv : the preprint server for biology·2026
Same author

Neurogenin-2 Reprograms Human Microglial Lineage Cells into Neurons In Vitro and in Chimeric Brains.

bioRxiv : the preprint server for biology·2026
Same author

A myeloid trisomy 21-associated gene variant is protective from Alzheimer's disease.

Nature neuroscience·2025
Same author

Author Correction: Arc in the nucleus regulates PML-dependent GluA1 transcription and homeostatic plasticity.

Nature neuroscience·2025

Related Experiment Video

Updated: May 26, 2026

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species
07:08

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species

Published on: February 27, 2018

Protein aggregates in Huntington's disease.

Montserrat Arrasate1, Steven Finkbeiner

  • 1Division of Neuroscience, Center for Applied Medical Research (CIMA), University of Navarra, Pamplona, E-31008, Spain. marrasatei@unav.es

Experimental Neurology
|December 28, 2011
PubMed
Summary

Huntington's disease (HD) involves mutant huntingtin protein aggregation. Inclusion bodies may represent a cellular response to misfolded protein, potentially explaining neuronal vulnerability in this neurodegenerative disorder.

More Related Videos

Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy
11:22

Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy

Published on: June 27, 2018

Efficient and Scalable Production of Full-length Human Huntingtin Variants in Mammalian Cells using a Transient Expression System
10:52

Efficient and Scalable Production of Full-length Human Huntingtin Variants in Mammalian Cells using a Transient Expression System

Published on: December 10, 2021

Related Experiment Videos

Last Updated: May 26, 2026

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species
07:08

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species

Published on: February 27, 2018

Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy
11:22

Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy

Published on: June 27, 2018

Efficient and Scalable Production of Full-length Human Huntingtin Variants in Mammalian Cells using a Transient Expression System
10:52

Efficient and Scalable Production of Full-length Human Huntingtin Variants in Mammalian Cells using a Transient Expression System

Published on: December 10, 2021

Area of Science:

  • Neuroscience
  • Genetics
  • Molecular Biology

Background:

  • Huntington's disease (HD) is a fatal neurodegenerative disorder.
  • HD stems from CAG repeat expansions in the IT-15 gene, leading to mutant huntingtin (Htt) protein with polyQ expansions.
  • The precise pathogenic mechanisms of HD remain unclear.

Purpose of the Study:

  • To review current knowledge on HD pathogenesis.
  • To focus on the role of intracellular aggregates, or inclusion bodies (IBs), of mutant Htt.
  • To explore the regulation and cellular context-dependency of IB formation.

Main Methods:

  • Literature review of Huntington's disease research.
  • Analysis of pathological features, specifically mutant huntingtin inclusion bodies.
  • Speculative modeling of cellular responses to misfolded proteins.

Main Results:

  • Mutant huntingtin protein (Htt) with polyQ expansions misfolds and aggregates.
  • Intracellular aggregates, inclusion bodies (IBs), are a hallmark of HD pathology.
  • IB formation may be part of a broader cellular coping mechanism against toxic Htt.

Conclusions:

  • Inclusion body formation might be a cellular defense against mutant Htt.
  • The efficacy of this response may depend on clearing toxic protein species.
  • Differential regulation of IB formation could explain selective neuronal vulnerability in HD.