Cholesterol Accelerates Aggregation of α-Synuclein Simultaneously Increasing the Toxicity of Amyloid Fibrils.

Caenorhabditis elegans ROS cholesterol fibrils α-synuclein

Journal

ACS chemical neuroscience
ISSN: 1948-7193
Titre abrégé: ACS Chem Neurosci
Pays: United States
ID NLM: 101525337

Informations de publication

Date de publication:
29 Oct 2024
Historique:
medline: 29 10 2024
pubmed: 29 10 2024
entrez: 29 10 2024
Statut: aheadofprint

Résumé

A hallmark of Parkinson disease (PD) is a progressive degeneration of neurons in the substantia nigra pars compacta, hypothalamus, and thalamus. Although the exact etiology of irreversible neuronal degeneration is unclear, a growing body of experimental evidence indicates that PD could be triggered by the abrupt aggregation of α-synuclein (α-Syn), a small membrane protein that is responsible for cell vesicle trafficking. Phospholipids uniquely alter the rate of α-Syn aggregation and, consequently, change the cytotoxicity of α-Syn oligomers and fibrils. However, the role of cholesterol in the aggregation of α-Syn remains unclear. In this study, we used

Identifiants

pubmed: 39469734
doi: 10.1021/acschemneuro.4c00501
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Auteurs

Mikhail Matveyenka (M)

Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, United States.

Abid Ali (A)

Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, United States.

Charles L Mitchell (CL)

Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, United States.

Harris C Brown (HC)

Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, United States.

Dmitry Kurouski (D)

Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, United States.

Classifications MeSH