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

10.2K
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,...
10.2K
Amyloid Fibrils03:03

Amyloid Fibrils

5.2K
5.2K
Subviral Agents01:29

Subviral Agents

933
Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...
933
Parkinson Disease ll: Pathophysiology01:24

Parkinson Disease ll: Pathophysiology

28
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...
28
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

14.7K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
14.7K
Alzheimer Disease ll: Pathophysiology01:23

Alzheimer Disease ll: Pathophysiology

35
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...
35

You might also read

Related Articles

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

Sort by
Same author

An approach to characterize mechanisms of action of anti-amyloidogenic compounds in vitro and in situ.

NPJ Parkinson's disease·2025
Same author

Alpha-synuclein aggregates are phosphatase resistant.

Acta neuropathologica communications·2024
Same author

Alpha-synuclein aggregates are phosphatase resistant.

bioRxiv : the preprint server for biology·2024
Same author

Rationale and design of the CRAFT (Continuous ReAssessment with Flexible ExTension in Rare Malignancies) multicenter phase II trial.

ESMO open·2021
Same author

Alpha-synuclein and the prion hypothesis in Parkinson's disease.

Revue neurologique·2018
Same author

ɑ-Synuclein strains and seeding in Parkinson's disease, incidental Lewy body disease, dementia with Lewy bodies and multiple system atrophy: similarities and differences.

Cell and tissue research·2018

Related Experiment Video

Updated: May 1, 2026

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster
10:26

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster

Published on: March 12, 2018

7.6K

Protein aggregation and prionopathies.

M Renner1, R Melki2

  • 1Biologie cellulaire de la synapse, institut de biologie de l'École normale supérieure (IBENS), Inserm U1024 - CNRS 8197, 46, rue d'Ulm, 75005 Paris, France.

Pathologie-Biologie
|April 5, 2014
PubMed
Summary

Prion and prion-like proteins misfold and aggregate, causing neurodegenerative diseases like Alzheimer's. These toxic protein aggregates can spread between cells, contributing to disease progression and impacting human health.

Keywords:
Agrégation des protéinesAlpha-synucleinopathiesAlpha-synucléinopathiesAlzheimerAmyotrophic lateral sclerosisHuntingtonParkinsonPrionProtein aggregationSclérose latérale amyotrophiqueTauopathies

More Related Videos

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
12:57

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

15.7K
Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis
10:03

Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis

Published on: July 16, 2008

31.2K

Related Experiment Videos

Last Updated: May 1, 2026

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster
10:26

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster

Published on: March 12, 2018

7.6K
Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
12:57

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

15.7K
Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis
10:03

Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis

Published on: July 16, 2008

31.2K

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Prion and prion-like proteins share characteristics, including conformational changes leading to insoluble aggregates.
  • These aggregates evade cellular clearance and amplify, contributing to neurodegenerative diseases such as Creutzfeldt-Jacob, Alzheimer, Parkinson, and Huntington diseases.

Purpose of the Study:

  • To explore the molecular mechanisms and implications of prion-like protein aggregate propagation in neurodegenerative diseases.
  • To highlight the potential for inter-cellular trafficking and transmissibility of these pathological protein assemblies.

Main Methods:

  • Review of molecular characteristics of prion and prion-like proteins.
  • Analysis of evidence for inter-cellular trafficking and propagation of protein aggregates.
  • Examination of experimental data supporting cell-to-cell spread in animal models.

Main Results:

  • Prion-like proteins aggregate and resist clearance, driving neurodegeneration.
  • Evidence supports the cell-to-cell transmission of protein aggregates, similar to prion diseases.
  • Potential overlaps and crosstalk between different neurodegenerative disorders are emerging.

Conclusions:

  • Cell-to-cell propagation of protein aggregates is a common mechanism in neurodegenerative diseases.
  • Understanding these prion-like mechanisms is crucial for addressing human health impacts.
  • Further research is needed to elucidate toxicity mechanisms and therapeutic targets.