The molecular tweezer CLR01 reduces aggregated, pathologic, and seeding-competent α-synuclein in experimental multiple system atrophy.


Journal

Biochimica et biophysica acta. Molecular basis of disease
ISSN: 1879-260X
Titre abrégé: Biochim Biophys Acta Mol Basis Dis
Pays: Netherlands
ID NLM: 101731730

Informations de publication

Date de publication:
01 11 2019
Historique:
received: 22 01 2019
revised: 09 07 2019
accepted: 12 07 2019
pubmed: 19 7 2019
medline: 27 5 2020
entrez: 19 7 2019
Statut: ppublish

Résumé

Multiple system atrophy (MSA) is a fatal, adult-onset neurodegenerative disorder that has no cure and very limited treatment options. MSA is characterized by deposition of fibrillar α-synuclein (α-syn) in glial cytoplasmic inclusions in oligodendrocytes. Similar to other synucleinopathies, α-syn self-assembly is thought to be a key pathologic event and a prominent target for disease modification in MSA. Molecular tweezers are broad-spectrum nanochaperones that prevent formation of toxic protein assemblies and enhance their clearance. The current lead compound, CLR01, has been shown to inhibit α-syn aggregation but has not yet been tested in the context of MSA. To fill this gap, here, we conducted a proof-of-concept study to assess the efficacy of CLR01 in remodeling MSA-like α-syn pathology in the PLP-α-syn mouse model of MSA. Six-month-old mice received intracerebroventricular CLR01 (0.3 or 1 mg/kg per day) or vehicle for 32 days. Open-field test revealed a significant, dose-dependent amelioration of an anxiety-like phenotype. Subsequently, immunohistochemical and biochemical analyses showed dose-dependent reduction of pathological and seeding-competent forms of α-syn, which correlated with the behavioral phenotype. CLR01 treatment also promoted dopaminergic neuron survival in the substantia nigra. To our knowledge, this is the first demonstration of an agent that reduces formation of putative high-molecular-weight oligomers and seeding-competent α-syn in a mouse model of MSA, supporting the view that these species are key to the neurodegenerative process and its cell-to-cell progression in MSA. Our study suggests that CLR01 is an attractive therapeutic candidate for disease modification in MSA and related synucleinopathies, supporting further preclinical development.

Identifiants

pubmed: 31319154
pii: S0925-4439(19)30230-3
doi: 10.1016/j.bbadis.2019.07.007
pmc: PMC8425273
mid: NIHMS1732855
pii:
doi:

Substances chimiques

Bridged-Ring Compounds 0
CLR01 compound 0
Neuroprotective Agents 0
Organophosphates 0
alpha-Synuclein 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

165513

Subventions

Organisme : Austrian Science Fund FWF
ID : I 2102
Pays : Austria
Organisme : NIA NIH HHS
ID : R01 AG050721
Pays : United States
Organisme : NCATS NIH HHS
ID : UL1 TR001881
Pays : United States
Organisme : NCI NIH HHS
ID : P30 CA016042
Pays : United States
Organisme : NIAID NIH HHS
ID : P30 AI028697
Pays : United States

Informations de copyright

Copyright © 2019 Elsevier B.V. All rights reserved.

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Auteurs

Marcos Herrera-Vaquero (M)

Division of Neurobiology, Department of Neurology, Medical University of Innsbruck, Austria.

Danielle Bouquio (D)

Department of Neurology, David Geffen School of Medicine, University of California, Los Angeles, CA, USA; Department of Molecular and Medical Pharmacology, David Geffen School of Medicine, University of California, Los Angeles, CA, USA.

Martin Kallab (M)

Division of Neurobiology, Department of Neurology, Medical University of Innsbruck, Austria.

Karl Biggs (K)

Department of Neurology, David Geffen School of Medicine, University of California, Los Angeles, CA, USA.

Gayatri Nair (G)

Department of Neurology, David Geffen School of Medicine, University of California, Los Angeles, CA, USA.

Jessica Ochoa (J)

Department of Neurology, David Geffen School of Medicine, University of California, Los Angeles, CA, USA; Brain Research Institute and Molecular Biology Institute, University of California, Los Angeles, CA, USA.

Antonio Heras-Garvin (A)

Division of Neurobiology, Department of Neurology, Medical University of Innsbruck, Austria.

Christian Heid (C)

Institute of Chemistry, University of Duisburg-Essen, Essen, Germany.

Inesa Hadrovic (I)

Institute of Chemistry, University of Duisburg-Essen, Essen, Germany.

Werner Poewe (W)

Division of Neurobiology, Department of Neurology, Medical University of Innsbruck, Austria.

Gregor K Wenning (GK)

Division of Neurobiology, Department of Neurology, Medical University of Innsbruck, Austria.

Frank-Gerrit Klärner (FG)

Institute of Chemistry, University of Duisburg-Essen, Essen, Germany.

Thomas Schrader (T)

Institute of Chemistry, University of Duisburg-Essen, Essen, Germany.

Gal Bitan (G)

Department of Neurology, David Geffen School of Medicine, University of California, Los Angeles, CA, USA; Brain Research Institute and Molecular Biology Institute, University of California, Los Angeles, CA, USA. Electronic address: gbitan@mednet.ucla.edu.

Nadia Stefanova (N)

Division of Neurobiology, Department of Neurology, Medical University of Innsbruck, Austria. Electronic address: nadia.stefanova@i-med.ac.at.

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Classifications MeSH