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

12.4K
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,...
12.4K

You might also read

Related Articles

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

Sort by
Same author

A Subset of Caveolin-1 Interacts with a Fraction of Acyl-CoA:Cholesterol Acyltransferase 1 (ACAT1/SOAT1) at an Endoplasmic Reticulum Subdomain to Attenuate Cholesteryl Ester Biosynthesis.

Biomolecules·2026
Same author

Electrophilic monocarbonyl curcumin derivatives reveal differential vulnerabilities in the selenium metabolic network.

Free radical biology & medicine·2026
Same author

Association of Trust in COVID-19 Information Providers and Media With 3Cs Avoidance and Infection Anxiety Among Residents in Tokyo and Osaka.

Japanese journal of infectious diseases·2026
Same author

Lipid peroxidation, ferroptosis, and antioxidants.

Free radical biology & medicine·2025
Same author

Unconventional secretion of PARK7 requires lysosomal delivery via chaperone-mediated autophagy and specialized SNARE complex.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

Therapeutic effect of curcumin derivative GT863 on prion-infected mice.

Scientific reports·2025

Related Experiment Video

Updated: Mar 10, 2026

Labeling and Imaging of Amyloid Plaques in Brain Tissue Using the Natural Polyphenol Curcumin
10:15

Labeling and Imaging of Amyloid Plaques in Brain Tissue Using the Natural Polyphenol Curcumin

Published on: November 1, 2019

13.5K

Decrease of Amyloid-β Levels by Curcumin Derivative via Modulation of Amyloid-β Protein Precursor Trafficking.

Rina Kotani1, Yasuomi Urano1, Hachiro Sugimoto2

  • 1Department of Medical Life Systems, Faculty of Life and Medical Sciences, Doshisha University, Kyoto, Japan.

Journal of Alzheimer'S Disease : JAD
|December 17, 2016
PubMed
Summary

A novel curcumin derivative, CU6, effectively reduces amyloid-β (Aβ) production in Alzheimer

Keywords:
Alzheimer’s diseaseamyloid-β peptidescurcumin derivativesendoplasmic reticulum

More Related Videos

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
06:17

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

Published on: May 22, 2018

12.7K
Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices
04:41

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices

Published on: July 14, 2010

24.1K

Related Experiment Videos

Last Updated: Mar 10, 2026

Labeling and Imaging of Amyloid Plaques in Brain Tissue Using the Natural Polyphenol Curcumin
10:15

Labeling and Imaging of Amyloid Plaques in Brain Tissue Using the Natural Polyphenol Curcumin

Published on: November 1, 2019

13.5K
A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
06:17

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

Published on: May 22, 2018

12.7K
Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices
04:41

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices

Published on: July 14, 2010

24.1K

Area of Science:

  • Neuroscience
  • Biochemistry
  • Pharmacology

Background:

  • Alzheimer's disease (AD) is characterized by abnormal amyloid-β (Aβ) peptide production and deposition.
  • Aβ is generated from amyloid-β protein precursor (AβPP) via sequential cleavage by β- and γ-secretases.
  • Targeting secretase activity directly may cause adverse effects; thus, alternative strategies to inhibit Aβ production are needed.

Purpose of the Study:

  • To evaluate the efficacy of curcumin derivatives in reducing Aβ production.
  • To investigate the mechanism by which CU6 suppresses Aβ generation.

Main Methods:

  • Utilized human neuroblastoma SH-SY5Y cells and CHO cells stably expressing human AβPP (CHO-AβPP).
  • Assessed Aβ secretion levels.
  • Measured β- and γ-secretase activities.
  • Analyzed AβPP processing and localization within cellular compartments (ER, Golgi).
  • Investigated the role of ER chaperones, specifically glucose-regulated protein 78 (GRP78).

Main Results:

  • The curcumin derivative CU6 demonstrated superior efficacy in reducing Aβ secretion compared to curcumin.
  • CU6 did not inhibit β- or γ-secretase activity.
  • Accumulation of immature AβPP forms was observed in the endoplasmic reticulum (ER).
  • CU6 induced GRP78 expression and enhanced the formation of the AβPP/GRP78 complex.
  • These findings indicate that CU6 downregulates intracellular AβPP trafficking.

Conclusions:

  • CU6 effectively suppresses Aβ production through a mechanism independent of direct secretase inhibition.
  • CU6 modulates AβPP intracellular trafficking and processing.
  • This suggests CU6 as a potential therapeutic agent for Alzheimer's disease by targeting AβPP metabolism.