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

9.2K
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,...
9.2K
Long-term Depression01:03

Long-term Depression

2.5K
Long-term depression, or LTD, is one of the ways by which synaptic plasticity—changes in the strength of chemical synapses—can occur in the brain. LTD is the process of synaptic weakening that occurs over time between pre and postsynaptic neuronal connections. The synaptic weakening of LTD works in opposition to synaptic strengthening by long-term potentiation (LTP) and together are the main mechanisms that underlie learning and memory.
Calcium Ion Concentration Mechanism
If over...
2.5K
Long-term Potentiation01:25

Long-term Potentiation

2.7K
Long-term potentiation, or LTP, is one of the ways by which synaptic plasticity—changes in the strength of chemical synapses—can occur in the brain. LTP is the process of synaptic strengthening that occurs over time between pre and postsynaptic neuronal connections. The synaptic strengthening of LTP works in opposition to the synaptic weakening of long-term depression (LTD) and together are the main mechanisms that underlie learning and memory.
Hebbian LTP
LTP can occur when...
2.7K
Neural Regulation01:37

Neural Regulation

39.1K
Digestion begins with a cephalic phase that prepares the digestive system to receive food. When our brain processes visual or olfactory information about food, it triggers impulses in the cranial nerves innervating the salivary glands and stomach to prepare for food.
39.1K
Psychosis: Pathophysiology of Schizophrenia and Other Psychotic Disorders01:27

Psychosis: Pathophysiology of Schizophrenia and Other Psychotic Disorders

442
Schizophrenia is a neurodevelopmental disorder whose origins are rooted in complex genetic components. Despite our burgeoning understanding, the pathophysiology of this disorder remains incompletely deciphered.
Researchers have identified genetic factors that increase susceptibility to schizophrenia, underscoring the intricate interplay between genetics and environment in disease development. At the core of schizophrenia's pathophysiology is excessive dopaminergic neurotransmission within...
442
Parkinson's Disease: Overview01:15

Parkinson's Disease: Overview

476
Neurodegenerative disorders are progressive diseases that cause irreversible damage and loss to neurons in specific brain areas. Examples of these disorders include Parkinson's disease, Alzheimer's disease, Multiple Sclerosis (MS), and Amyotrophic Lateral Sclerosis (ALS). These disorders share characteristics such as proteinopathies, selective neuronal vulnerability, and a complex interplay between genetic and environmental factors. The primary therapeutic goal for these conditions is...
476

You might also read

Related Articles

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

Sort by
Same author

SIRT5-dependent regulation of ASL controls arginine metabolism and T cell function.

bioRxiv : the preprint server for biology·2026
Same author

IgE-Sensitized Mast Cells Release Extracellular Vesicles that Transfer IgE and Spread Allergic Sensitization.

The Journal of allergy and clinical immunology·2026
Same author

Bactofilins are essential spatial organizers of peptidoglycan insertion in the Lyme disease spirochete <i>Borrelia burgdorferi</i>.

Journal of bacteriology·2026
Same author

Historical and contemporary chronic wasting disease prions from the western United States demonstrate similar strain properties.

The Journal of general virology·2026
Same author

Single-dose mRNA vaccines against Andes hantavirus.

Lancet (London, England)·2026
Same author

Ketogenic diet synergistic reprogramming of both host and microbiome promotes tissue regeneration.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Jun 4, 2025

Technique for Intranasal Administration of &#945;-Synuclein Aggregates
04:49

Technique for Intranasal Administration of α-Synuclein Aggregates

Published on: November 8, 2024

387

Limbic system synaptic dysfunctions associated with prion disease onset.

Simote T Foliaki1, Bradley R Groveman2, Emmett A Dews2

  • 1Laboratory of Neurological Infections and Immunity, National Institute of Allergy and Infectious Diseases, Division of Intramural Research, Rocky Mountain Laboratories, National Institutes of Health, Hamilton, MT, USA. simote.foliaki@nih.gov.

Acta Neuropathologica Communications
|December 20, 2024
PubMed
Summary

Prion diseases disrupt synaptic function in the limbic system, affecting cognition and mood. Early synaptic damage in the hippocampus, hypothalamus, and amygdala correlates with disease onset.

Keywords:
CognitionEmotionLimbic systemNeurodegenerationPrion diseaseSynaptic transmission

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

15.8K
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

8.0K

Related Experiment Videos

Last Updated: Jun 4, 2025

Technique for Intranasal Administration of &#945;-Synuclein Aggregates
04:49

Technique for Intranasal Administration of α-Synuclein Aggregates

Published on: November 8, 2024

387
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

15.8K
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

8.0K

Area of Science:

  • Neuroscience
  • Prion Biology
  • Synaptic Physiology

Background:

  • Prion diseases (PrDs) involve misfolded prion protein (PrPC) forming pathological prions.
  • Clinical signs of PrDs include cognitive decline and mood changes, linked to the limbic system.
  • Synaptic dysfunction in limbic regions during PrDs is poorly understood.

Purpose of the Study:

  • To investigate how prion infection disrupts synaptic function in the hippocampus, hypothalamus, and amygdala.
  • To correlate synaptic dysfunction with cognitive and behavioral deficits at pre-clinical and clinical stages.
  • To identify potential therapeutic targets for delaying PrD onset.

Main Methods:

  • Studied prion-infected mice at pre-clinical and early clinical stages.
  • Assessed synaptic function, calcium flux, neuronal firing, and neural oscillations in specific limbic regions.
  • Analyzed neurotransmitter levels, synaptic vesicle recycling, and cytoskeletal integrity.

Main Results:

  • Pre-clinically, PrD caused calcium dysregulation, reduced neuronal firing, and slowed oscillations in the hippocampus, hypothalamus, and amygdala.
  • Clinically, synaptic transmission and plasticity were significantly disrupted.
  • Observed depletion of soluble prion protein, synapse loss, abnormal neurotransmitter release, and cytoskeletal damage.

Conclusions:

  • Prion disease causes synaptic damage in key limbic regions starting pre-clinically.
  • Synaptic plasticity dysfunction correlates with early disease signs, impacting cognition and mood.
  • Targeting early neuronal dysfunction may offer therapeutic strategies to delay clinical onset of prion diseases.