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

Hsp70 Reduces alpha-Synuclein Aggregation and Toxicity.

Jochen Klucken1, Youngah Shin, Eliezer Masliah

  • 1Alzheimer's Disease Research Laboratory, Harvard Medical School, Massachusetts General Hospital, Charlestown, Massachusetts 02129, USA.

The Journal of Biological Chemistry
|March 27, 2004
PubMed
Summary
This summary is machine-generated.

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

Reconstitution of the Alzheimer's Disease Tau Core Structure from Recombinant Tau<sup>297-391</sup> Yields Variable Quaternary Structures as Seen by Negative Stain and Cryo-EM.

Biochemistry·2023
Same author

Aberrant vascular architecture in the hippocampus correlates with tau burden in mild cognitive impairment and Alzheimer's disease.

Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism·2023
Same author

Cases of familial idiopathic normal pressure hydrocephalus implicate genetic factors in disease pathogenesis.

Cerebral cortex (New York, N.Y. : 1991)·2023
Same author

Reply: Soluble oligomers or insoluble fibrils?

Acta neuropathologica·2023
Same author

Age-Dependent Increase in Tau Phosphorylation at Serine 396 in Huntington's Disease Prefrontal Cortex.

Journal of Huntington's disease·2023
Same author

APOE2 gene therapy reduces amyloid deposition, and improves markers of neuroinflammation and neurodegeneration in a mouse model of Alzheimer disease.

bioRxiv : the preprint server for biology·2023
Same journal

Isotope-Edited ESEEM: A New Method for Probing Copper Binding Sites in Neurodegenerative Proteins.

The Journal of biological chemistry·2026
Same journal

Introduction to the Thematic Review Series on Intracellular Protein Degradation. The ubiquitous biology of intracellular protein degradation: a tribute to Alfred L. ("Fred") Goldberg.

The Journal of biological chemistry·2026
Same journal

Correction: Aromatic residue-rich amino-terminal segments of temporin L self-assemble into collagen-mimetic peptides with cell-adhesion properties.

The Journal of biological chemistry·2026
Same journal

YhbO is a DJ-1 family glyoxalase and α-oxoaldehyde hydratase that confers resistance to reactive carbonyl stress (112).

The Journal of biological chemistry·2026
Same journal

ARMH3 acts as a central scaffold at the Golgi/TGN through interactions with Arl5, GBF1, and PI4KB.

The Journal of biological chemistry·2026
Same journal

PAX8 controls proximal tubule epithelial identity and stress response through epigenetic modification of distal regulatory elements.

The Journal of biological chemistry·2026
See all related articles

The molecular chaperone Hsp70 reduces toxic alpha-synuclein aggregates in dementia with Lewy bodies (DLB) models. Hsp70 protects against alpha-synuclein-induced cellular toxicity in vitro and in vivo.

Area of Science:

  • Neurobiology
  • Molecular Chaperones
  • Neurodegenerative Diseases

Background:

  • Misfolded alpha-synuclein aggregation is central to Parkinson's disease and dementia with Lewy bodies (DLB).
  • Identifying therapeutic targets to mitigate alpha-synuclein toxicity is crucial for neurodegenerative disease treatment.

Purpose of the Study:

  • To investigate the role of the molecular chaperone Hsp70 in reducing misfolded alpha-synuclein species.
  • To assess Hsp70's protective effects against alpha-synuclein-induced cellular toxicity.

Main Methods:

  • Detection of misfolded, aggregated alpha-synuclein in DLB patient brain tissue and in vitro/in vivo models.
  • Utilizing alpha-synuclein transgenic mice crossed with Hsp70-overexpressing mice for in vivo studies.
  • Assessing alpha-synuclein species and cellular toxicity following Hsp70 intervention.

Related Experiment Videos

Main Results:

  • Misfolded, aggregated alpha-synuclein was detected in DLB patient brains and aggregation models.
  • Hsp70 overexpression significantly reduced high molecular weight and detergent-insoluble alpha-synuclein species in vivo.
  • In vitro Hsp70 overexpression decreased detergent-insoluble alpha-synuclein and protected cells from toxicity.

Conclusions:

  • The molecular chaperone Hsp70 effectively reduces pathological alpha-synuclein species in both in vivo and in vitro models.
  • Hsp70 demonstrates potential as a therapeutic agent against alpha-synuclein-dependent neurotoxicity in diseases like DLB.