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

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...
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...
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
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...
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

Visceral adipose tissue differentially affects tau and Aβ pathology in 3xTg-AD mice.

Cell communication and signaling : CCS·2026
Same author

The TREM2 R47H variant is associated with liver-plasma-brain axis dyshomeostasis in the 5xFAD mouse model of Alzheimer's disease.

Neurobiology of aging·2026
Same author

Abi3<sup>S212F</sup> Alzheimer's disease variant alters plaque structure and disrupts microglia.

Alzheimer's & dementia : the journal of the Alzheimer's Association·2026
Same author

Basic Science and Pathogenesis.

Alzheimer's & dementia : the journal of the Alzheimer's Association·2025
Same author

Basic Science and Pathogenesis.

Alzheimer's & dementia : the journal of the Alzheimer's Association·2025
Same author

Basic Science and Pathogenesis.

Alzheimer's & dementia : the journal of the Alzheimer's Association·2025

Related Experiment Video

Updated: Jun 10, 2026

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
09:22

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

Pathways linking Abeta and tau pathologies.

Frank M LaFerla1

  • 1Department of Neurobiology and Behavior and Institute for Memory Impairments and Neurological Disorders, University of California Irvine, Irvine, CA 92697, USA. laferla@uci.edu

Biochemical Society Transactions
|July 28, 2010
PubMed
Summary

Amyloid beta-peptide (Abeta) and tau proteins contribute to Alzheimer's disease. New research shows Abeta pathology can directly influence tau pathology, offering new therapeutic targets for Alzheimer's treatment.

More Related Videos

Assessment of Spontaneous Alternation, Novel Object Recognition and Limb Clasping in Transgenic Mouse Models of Amyloid-&#946; and Tau Neuropathology
10:02

Assessment of Spontaneous Alternation, Novel Object Recognition and Limb Clasping in Transgenic Mouse Models of Amyloid-β and Tau Neuropathology

Published on: May 28, 2017

Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry
12:31

Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry

Published on: December 8, 2015

Related Experiment Videos

Last Updated: Jun 10, 2026

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
09:22

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

Assessment of Spontaneous Alternation, Novel Object Recognition and Limb Clasping in Transgenic Mouse Models of Amyloid-&#946; and Tau Neuropathology
10:02

Assessment of Spontaneous Alternation, Novel Object Recognition and Limb Clasping in Transgenic Mouse Models of Amyloid-β and Tau Neuropathology

Published on: May 28, 2017

Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry
12:31

Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry

Published on: December 8, 2015

Area of Science:

  • Neuroscience
  • Biochemistry
  • Pathology

Background:

  • Alzheimer's disease (AD) is characterized by amyloid plaques and neurofibrillary tangles (NFTs).
  • Abeta and tau proteins misfold and accumulate in AD, forming plaques (extracellular) and NFTs (intracellular).
  • Previously, distinct pathways were assumed for plaque and NFT formation due to their cellular locations.

Purpose of the Study:

  • To review evidence linking Abeta pathology to tau pathology development.
  • To explore the implications of Abeta-tau interactions for Alzheimer's disease treatment.

Main Methods:

  • Review of animal and cell studies.
  • Analysis of data from multiple research laboratories.

Main Results:

  • Evidence suggests Abeta facilitates tau pathology development through various mechanisms.
  • Modulating Abeta pathology directly impacts tau pathology progression.

Conclusions:

  • Abeta and tau pathologies are interconnected in Alzheimer's disease.
  • Targeting Abeta pathology may be a viable therapeutic strategy for AD.
  • Understanding Abeta-tau interactions is crucial for developing effective AD treatments.