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 Experiment Videos

Alzheimer beta-amyloid peptides: normal and abnormal localization.

R H Takahashi1, E E Nam, M Edgar

  • 1Department of Neurology and Neuroscience, Weill Medical College of Cornell University, New York, NY 10021, USA.

Histology and Histopathology
|January 30, 2002
PubMed
Summary

Alzheimer's disease involves amyloid plaques (SPs) and neurofibrillary tangles (NFTs). This review examines the localization of beta-amyloid (A beta) peptides, both intracellular and extracellular, to understand their role in AD pathogenesis.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Maternal separation differentially modulates early pathology by sex in 5xFAD Alzheimer's disease-transgenic mice.

Brain, behavior, & immunity - health·2023
Same author

Early-life stress elicits peripheral and brain immune activation differently in wild type and 5xFAD mice in a sex-specific manner.

Journal of neuroinflammation·2022
Same author

Determinations of the peroxidative susceptibilities of cod liver oils by a newly-developed <sup>1</sup>H NMR-based method: resistance of an antioxidant-fortified product isolated from pre-fermented sources.

BMC research notes·2020
Same author

Pre-plaque conformational changes in Alzheimer's disease-linked Aβ and APP.

Nature communications·2017
Same author

Effect of anthropogenic organic complexants on the solubility of Ni, Th, U(IV) and U(VI).

Journal of hazardous materials·2015
Same author

Thy28 protects against anti-CD3-mediated thymic cell death in vivo.

Apoptosis : an international journal on programmed cell death·2014

Area of Science:

  • Neuroscience
  • Cell Biology
  • Pathology

Background:

  • Alzheimer's disease (AD) is characterized by senile plaques (SPs) and neurofibrillary tangles (NFTs).
  • SPs are mainly composed of beta-amyloid (A beta) peptides, with familial AD mutations increasing A beta42 production, implicating A beta in AD pathogenesis.
  • A beta is generated by sequential cleavage of amyloid precursor protein (APP) by beta- and gamma-secretases within cellular compartments like the ER, Golgi, and endosomal/lysosomal system.

Purpose of the Study:

  • To review current knowledge on the localization of both intracellular and extracellular A beta.
  • To explore the central question of whether extracellular A beta deposition or intracellular A beta accumulation initiates the disease process in Alzheimer's disease.

Main Methods:

  • Review of existing cell biological studies and scientific literature.

Related Experiment Videos

  • Analysis of the proposed mechanisms of A beta generation and aggregation.
  • Examination of the evidence for A beta toxicity in both extracellular and intracellular compartments.

    • Main Results:

    • A beta peptides are generated within the endoplasmic reticulum, Golgi, and endosomal/lysosomal system.
    • A beta42 readily aggregates, potentially seeding fibril formation and plaque deposition.
    • Both extracellular SPs and intracellular A beta accumulation are considered in the context of neuronal toxicity in AD.

    Conclusions:

    • The precise role of extracellular versus intracellular A beta in initiating Alzheimer's disease pathogenesis remains a key area of investigation.
    • Understanding the localization of A beta is crucial for elucidating its toxic mechanisms in AD.
    • Further research into the intracellular biology of APP and A beta may reveal novel therapeutic targets for Alzheimer's disease.