Juvenile CLN3 disease is a lysosomal cholesterol storage disorder: similarities with Niemann-Pick type C disease.


Journal

EBioMedicine
ISSN: 2352-3964
Titre abrégé: EBioMedicine
Pays: Netherlands
ID NLM: 101647039

Informations de publication

Date de publication:
Jun 2023
Historique:
received: 29 11 2022
revised: 30 04 2023
accepted: 10 05 2023
medline: 19 6 2023
pubmed: 29 5 2023
entrez: 28 5 2023
Statut: ppublish

Résumé

The most common form of neuronal ceroid lipofuscinosis (NCL) is juvenile CLN3 disease (JNCL), a currently incurable neurodegenerative disorder caused by mutations in the CLN3 gene. Based on our previous work and on the premise that CLN3 affects the trafficking of the cation-independent mannose-6 phosphate receptor and its ligand NPC2, we hypothesised that dysfunction of CLN3 leads to the aberrant accumulation of cholesterol in the late endosomes/lysosomes (LE/Lys) of JNCL patients' brains. An immunopurification strategy was used to isolate intact LE/Lys from frozen autopsy brain samples. LE/Lys isolated from samples of JNCL patients were compared with age-matched unaffected controls and Niemann-Pick Type C (NPC) disease patients. Indeed, mutations in NPC1 or NPC2 result in the accumulation of cholesterol in LE/Lys of NPC disease samples, thus providing a positive control. The lipid and protein content of LE/Lys was then analysed using lipidomics and proteomics, respectively. Lipid and protein profiles of LE/Lys isolated from JNCL patients were profoundly altered compared to controls. Importantly, cholesterol accumulated in LE/Lys of JNCL samples to a comparable extent than in NPC samples. Lipid profiles of LE/Lys were similar in JNCL and NPC patients, except for levels of bis(monoacylglycero)phosphate (BMP). Protein profiles detected in LE/Lys of JNCL and NPC patients appeared identical, except for levels of NPC1. Our results support that JNCL is a lysosomal cholesterol storage disorder. Our findings also support that JNCL and NPC disease share pathogenic pathways leading to aberrant lysosomal accumulation of lipids and proteins, and thus suggest that the treatments available for NPC disease may be beneficial to JNCL patients. This work opens new avenues for further mechanistic studies in model systems of JNCL and possible therapeutic interventions for this disorder. San Francisco Foundation.

Sections du résumé

BACKGROUND BACKGROUND
The most common form of neuronal ceroid lipofuscinosis (NCL) is juvenile CLN3 disease (JNCL), a currently incurable neurodegenerative disorder caused by mutations in the CLN3 gene. Based on our previous work and on the premise that CLN3 affects the trafficking of the cation-independent mannose-6 phosphate receptor and its ligand NPC2, we hypothesised that dysfunction of CLN3 leads to the aberrant accumulation of cholesterol in the late endosomes/lysosomes (LE/Lys) of JNCL patients' brains.
METHODS METHODS
An immunopurification strategy was used to isolate intact LE/Lys from frozen autopsy brain samples. LE/Lys isolated from samples of JNCL patients were compared with age-matched unaffected controls and Niemann-Pick Type C (NPC) disease patients. Indeed, mutations in NPC1 or NPC2 result in the accumulation of cholesterol in LE/Lys of NPC disease samples, thus providing a positive control. The lipid and protein content of LE/Lys was then analysed using lipidomics and proteomics, respectively.
FINDINGS RESULTS
Lipid and protein profiles of LE/Lys isolated from JNCL patients were profoundly altered compared to controls. Importantly, cholesterol accumulated in LE/Lys of JNCL samples to a comparable extent than in NPC samples. Lipid profiles of LE/Lys were similar in JNCL and NPC patients, except for levels of bis(monoacylglycero)phosphate (BMP). Protein profiles detected in LE/Lys of JNCL and NPC patients appeared identical, except for levels of NPC1.
INTERPRETATION CONCLUSIONS
Our results support that JNCL is a lysosomal cholesterol storage disorder. Our findings also support that JNCL and NPC disease share pathogenic pathways leading to aberrant lysosomal accumulation of lipids and proteins, and thus suggest that the treatments available for NPC disease may be beneficial to JNCL patients. This work opens new avenues for further mechanistic studies in model systems of JNCL and possible therapeutic interventions for this disorder.
FUNDING BACKGROUND
San Francisco Foundation.

Identifiants

pubmed: 37245481
pii: S2352-3964(23)00193-7
doi: 10.1016/j.ebiom.2023.104628
pmc: PMC10227369
pii:
doi:

Substances chimiques

Cholesterol 97C5T2UQ7J
Proteins 0
CLN3 protein, human 0
Membrane Glycoproteins 0
Molecular Chaperones 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

104628

Subventions

Organisme : NIA NIH HHS
ID : R01 AG071868
Pays : United States
Organisme : NIA NIH HHS
ID : R21 AG070768
Pays : United States

Informations de copyright

Copyright © 2023 The Author(s). Published by Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests The authors declare no competing financial interests.

Auteurs

Jacinda Chen (J)

Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University Irving Medical Center, New York City, NY 10032, USA.

Rajesh Kumar Soni (RK)

Proteomics and Macromolecular Crystallography Shared Resource, Herbert Irving Comprehensive Cancer Center, New York City, NY 10032, USA.

Yimeng Xu (Y)

Biomarkers Core Laboratory, Irving Institute for Clinical and Translational Research, Columbia University Irving Medical Center, New York City, NY 10032, USA.

Sabrina Simoes (S)

Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University Irving Medical Center, New York City, NY 10032, USA; Department of Neurology, Columbia University Irving Medical Center, New York City, NY 10032, USA.

Feng-Xia Liang (FX)

Microscopy Core Laboratory of Division of Advanced Research Technologies, New York University Grossman School of Medicine, New York City, NY 10016, USA.

Laura DeFreitas (L)

Biomarkers Core Laboratory, Irving Institute for Clinical and Translational Research, Columbia University Irving Medical Center, New York City, NY 10032, USA.

Robert Hwang (R)

Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University Irving Medical Center, New York City, NY 10032, USA.

Jorge Montesinos (J)

Department of Neurology, Columbia University Irving Medical Center, New York City, NY 10032, USA.

Joseph H Lee (JH)

Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University Irving Medical Center, New York City, NY 10032, USA; Department of Neurology, Columbia University Irving Medical Center, New York City, NY 10032, USA; G. H. Sergievsky Center, Columbia University Irving Medical Center, New York City, NY 10032, USA; Department of Epidemiology, Columbia University Irving Medical Center, New York City, NY 10032, USA.

Estela Area-Gomez (E)

Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University Irving Medical Center, New York City, NY 10032, USA; Department of Neurology, Columbia University Irving Medical Center, New York City, NY 10032, USA; Institute of Human Nutrition, Columbia University Irving Medical Center, New York City, NY 10032, USA.

Renu Nandakumar (R)

Biomarkers Core Laboratory, Irving Institute for Clinical and Translational Research, Columbia University Irving Medical Center, New York City, NY 10032, USA.

Badri Vardarajan (B)

Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University Irving Medical Center, New York City, NY 10032, USA; Department of Neurology, Columbia University Irving Medical Center, New York City, NY 10032, USA; G. H. Sergievsky Center, Columbia University Irving Medical Center, New York City, NY 10032, USA.

Catherine Marquer (C)

Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University Irving Medical Center, New York City, NY 10032, USA; Department of Pathology and Cell Biology, Columbia University Irving Medical Center, New York City, NY 10032, USA. Electronic address: cm3244@cumc.columbia.edu.

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Classifications MeSH