The Parkinson’s disease risk gene cathepsin B promotes fibrillar alpha-synuclein clearance, lysosomal function and glucocerebrosidase activity in dopaminergic neurons

Abstract Background Variants in the CTSB gene encoding the lysosomal hydrolase cathepsin B (catB) are associated with increased risk of Parkinson’s disease (PD). However, neither the specific CTSB variants driving these associations nor the functional pathways that link catB to PD pathogenesis have...

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Main Authors: Jace Jones-Tabah, Kathy He, Nathan Karpilovsky, Konstantin Senkevich, Ghislaine Deyab, Isabella Pietrantonio, Thomas Goiran, Yuting Cousineau, Daria Nikanorova, Taylor Goldsmith, Esther del Cid Pellitero, Carol X.-Q. Chen, Wen Luo, Zhipeng You, Narges Abdian, Jamil Ahmad, Jennifer A. Ruskey, Farnaz Asayesh, Dan Spiegelman, Stanley Fahn, Cheryl Waters, Oury Monchi, Yves Dauvilliers, Nicolas Dupré, Irina Miliukhina, Alla Timofeeva, Anton Emelyanov, Sofya Pchelina, Lior Greenbaum, Sharon Hassin-Baer, Roy N. Alcalay, Austen Milnerwood, Thomas M. Durcan, Ziv Gan-Or, Edward A. Fon
Format: Article
Language:English
Published: BMC 2024-11-01
Series:Molecular Neurodegeneration
Online Access:https://doi.org/10.1186/s13024-024-00779-9
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author Jace Jones-Tabah
Kathy He
Nathan Karpilovsky
Konstantin Senkevich
Ghislaine Deyab
Isabella Pietrantonio
Thomas Goiran
Yuting Cousineau
Daria Nikanorova
Taylor Goldsmith
Esther del Cid Pellitero
Carol X.-Q. Chen
Wen Luo
Zhipeng You
Narges Abdian
Jamil Ahmad
Jennifer A. Ruskey
Farnaz Asayesh
Dan Spiegelman
Stanley Fahn
Cheryl Waters
Oury Monchi
Yves Dauvilliers
Nicolas Dupré
Irina Miliukhina
Alla Timofeeva
Anton Emelyanov
Sofya Pchelina
Lior Greenbaum
Sharon Hassin-Baer
Roy N. Alcalay
Austen Milnerwood
Thomas M. Durcan
Ziv Gan-Or
Edward A. Fon
author_facet Jace Jones-Tabah
Kathy He
Nathan Karpilovsky
Konstantin Senkevich
Ghislaine Deyab
Isabella Pietrantonio
Thomas Goiran
Yuting Cousineau
Daria Nikanorova
Taylor Goldsmith
Esther del Cid Pellitero
Carol X.-Q. Chen
Wen Luo
Zhipeng You
Narges Abdian
Jamil Ahmad
Jennifer A. Ruskey
Farnaz Asayesh
Dan Spiegelman
Stanley Fahn
Cheryl Waters
Oury Monchi
Yves Dauvilliers
Nicolas Dupré
Irina Miliukhina
Alla Timofeeva
Anton Emelyanov
Sofya Pchelina
Lior Greenbaum
Sharon Hassin-Baer
Roy N. Alcalay
Austen Milnerwood
Thomas M. Durcan
Ziv Gan-Or
Edward A. Fon
author_sort Jace Jones-Tabah
collection DOAJ
description Abstract Background Variants in the CTSB gene encoding the lysosomal hydrolase cathepsin B (catB) are associated with increased risk of Parkinson’s disease (PD). However, neither the specific CTSB variants driving these associations nor the functional pathways that link catB to PD pathogenesis have been characterized. CatB activity contributes to lysosomal protein degradation and regulates signaling processes involved in autophagy and lysosome biogenesis. Previous in vitro studies have found that catB can cleave monomeric and fibrillar alpha-synuclein, a key protein involved in the pathogenesis of PD that accumulates in the brains of PD patients. However, truncated synuclein isoforms generated by catB cleavage have an increased propensity to aggregate. Thus, catB activity could potentially contribute to lysosomal degradation and clearance of pathogenic alpha synuclein from the cell, but also has the potential of enhancing synuclein pathology by generating aggregation-prone truncations. Therefore, the mechanisms linking catB to PD pathophysiology remain to be clarified. Methods Here, we conducted genetic analyses of the association between common and rare CTSB variants and risk of PD. We then used genetic and pharmacological approaches to manipulate catB expression and function in cell lines, induced pluripotent stem cell-derived dopaminergic neurons and midbrain organoids and assessed lysosomal activity and the handling of aggregated synuclein fibrils. Results We find that catB inhibition impairs autophagy, reduces glucocerebrosidase (encoded by GBA1) activity, and leads to an accumulation of lysosomal content. In cell lines, reduction of CTSB gene expression impairs the degradation of pre-formed alpha-synuclein fibrils, whereas CTSB gene activation enhances fibril clearance. In midbrain organoids and dopaminergic neurons treated with alpha-synuclein fibrils, catB inhibition potentiates the formation of inclusions which stain positively for phosphorylated alpha-synuclein. Conclusions These results indicate that the reduction of catB function negatively impacts lysosomal pathways associated with PD pathogenesis, while conversely catB activation could promote the clearance of pathogenic alpha-synuclein.
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spelling doaj-art-e2786b44f0ab42b995b54fb1787459cd2025-08-20T02:31:44ZengBMCMolecular Neurodegeneration1750-13262024-11-0119112110.1186/s13024-024-00779-9The Parkinson’s disease risk gene cathepsin B promotes fibrillar alpha-synuclein clearance, lysosomal function and glucocerebrosidase activity in dopaminergic neuronsJace Jones-Tabah0Kathy He1Nathan Karpilovsky2Konstantin Senkevich3Ghislaine Deyab4Isabella Pietrantonio5Thomas Goiran6Yuting Cousineau7Daria Nikanorova8Taylor Goldsmith9Esther del Cid Pellitero10Carol X.-Q. Chen11Wen Luo12Zhipeng You13Narges Abdian14Jamil Ahmad15Jennifer A. Ruskey16Farnaz Asayesh17Dan Spiegelman18Stanley Fahn19Cheryl Waters20Oury Monchi21Yves Dauvilliers22Nicolas Dupré23Irina Miliukhina24Alla Timofeeva25Anton Emelyanov26Sofya Pchelina27Lior Greenbaum28Sharon Hassin-Baer29Roy N. Alcalay30Austen Milnerwood31Thomas M. Durcan32Ziv Gan-Or33Edward A. Fon34Neurodegenerative Diseases Group, Department of Neurology and Neurosurgery, McGill Parkinson Program, Montreal Neurological Institute-Hospital, McGill UniversityNeurodegenerative Diseases Group, Department of Neurology and Neurosurgery, McGill Parkinson Program, Montreal Neurological Institute-Hospital, McGill UniversityNeurodegenerative Diseases Group, Department of Neurology and Neurosurgery, McGill Parkinson Program, Montreal Neurological Institute-Hospital, McGill UniversityNeurodegenerative Diseases Group, Department of Neurology and Neurosurgery, McGill Parkinson Program, Montreal Neurological Institute-Hospital, McGill UniversityNeurodegenerative Diseases Group, Department of Neurology and Neurosurgery, McGill Parkinson Program, Montreal Neurological Institute-Hospital, McGill UniversityNeurodegenerative Diseases Group, Department of Neurology and Neurosurgery, McGill Parkinson Program, Montreal Neurological Institute-Hospital, McGill UniversityNeurodegenerative Diseases Group, Department of Neurology and Neurosurgery, McGill Parkinson Program, Montreal Neurological Institute-Hospital, McGill UniversityDepartment of Neurology and Neurosurgery, McGill UniversityResearch Department, Bioinformatics InstituteEarly Drug Discovery Unit (EDDU), Montreal Neurological Institute-Hospital, McGill UniversityNeurodegenerative Diseases Group, Department of Neurology and Neurosurgery, McGill Parkinson Program, Montreal Neurological Institute-Hospital, McGill UniversityEarly Drug Discovery Unit (EDDU), Montreal Neurological Institute-Hospital, McGill UniversityEarly Drug Discovery Unit (EDDU), Montreal Neurological Institute-Hospital, McGill UniversityEarly Drug Discovery Unit (EDDU), Montreal Neurological Institute-Hospital, McGill UniversityEarly Drug Discovery Unit (EDDU), Montreal Neurological Institute-Hospital, McGill UniversityNeurodegenerative Diseases Group, Department of Neurology and Neurosurgery, McGill Parkinson Program, Montreal Neurological Institute-Hospital, McGill UniversityNeurodegenerative Diseases Group, Department of Neurology and Neurosurgery, McGill Parkinson Program, Montreal Neurological Institute-Hospital, McGill UniversityNeurodegenerative Diseases Group, Department of Neurology and Neurosurgery, McGill Parkinson Program, Montreal Neurological Institute-Hospital, McGill UniversityNeurodegenerative Diseases Group, Department of Neurology and Neurosurgery, McGill Parkinson Program, Montreal Neurological Institute-Hospital, McGill UniversityDepartment of Neurology, College of Physicians and Surgeons, Columbia University Medical CenterDepartment of Neurology, College of Physicians and Surgeons, Columbia University Medical CenterDepartment of Neurology and Neurosurgery, McGill UniversitySleep Unit, Department of Neurology, National Reference Center for Narcolepsy, Gui-de-Chauliac Hospital, CHU Montpellier, University of MontpellierNeuroscience Axis, CHU de Québec – Université Laval, Institute of the Human Brain of RASFirst Pavlov State Medical, University of St. PetersburgFirst Pavlov State Medical, University of St. PetersburgFirst Pavlov State Medical, University of St. PetersburgInstitute of the Human Brain of RASSackler Faculty of Medicine, Tel Aviv UniversityDepartment of Neurology, College of Physicians and Surgeons, Columbia University Medical CenterDepartment of Neurology and Neurosurgery, McGill UniversityEarly Drug Discovery Unit (EDDU), Montreal Neurological Institute-Hospital, McGill UniversityNeurodegenerative Diseases Group, Department of Neurology and Neurosurgery, McGill Parkinson Program, Montreal Neurological Institute-Hospital, McGill UniversityNeurodegenerative Diseases Group, Department of Neurology and Neurosurgery, McGill Parkinson Program, Montreal Neurological Institute-Hospital, McGill UniversityAbstract Background Variants in the CTSB gene encoding the lysosomal hydrolase cathepsin B (catB) are associated with increased risk of Parkinson’s disease (PD). However, neither the specific CTSB variants driving these associations nor the functional pathways that link catB to PD pathogenesis have been characterized. CatB activity contributes to lysosomal protein degradation and regulates signaling processes involved in autophagy and lysosome biogenesis. Previous in vitro studies have found that catB can cleave monomeric and fibrillar alpha-synuclein, a key protein involved in the pathogenesis of PD that accumulates in the brains of PD patients. However, truncated synuclein isoforms generated by catB cleavage have an increased propensity to aggregate. Thus, catB activity could potentially contribute to lysosomal degradation and clearance of pathogenic alpha synuclein from the cell, but also has the potential of enhancing synuclein pathology by generating aggregation-prone truncations. Therefore, the mechanisms linking catB to PD pathophysiology remain to be clarified. Methods Here, we conducted genetic analyses of the association between common and rare CTSB variants and risk of PD. We then used genetic and pharmacological approaches to manipulate catB expression and function in cell lines, induced pluripotent stem cell-derived dopaminergic neurons and midbrain organoids and assessed lysosomal activity and the handling of aggregated synuclein fibrils. Results We find that catB inhibition impairs autophagy, reduces glucocerebrosidase (encoded by GBA1) activity, and leads to an accumulation of lysosomal content. In cell lines, reduction of CTSB gene expression impairs the degradation of pre-formed alpha-synuclein fibrils, whereas CTSB gene activation enhances fibril clearance. In midbrain organoids and dopaminergic neurons treated with alpha-synuclein fibrils, catB inhibition potentiates the formation of inclusions which stain positively for phosphorylated alpha-synuclein. Conclusions These results indicate that the reduction of catB function negatively impacts lysosomal pathways associated with PD pathogenesis, while conversely catB activation could promote the clearance of pathogenic alpha-synuclein.https://doi.org/10.1186/s13024-024-00779-9
spellingShingle Jace Jones-Tabah
Kathy He
Nathan Karpilovsky
Konstantin Senkevich
Ghislaine Deyab
Isabella Pietrantonio
Thomas Goiran
Yuting Cousineau
Daria Nikanorova
Taylor Goldsmith
Esther del Cid Pellitero
Carol X.-Q. Chen
Wen Luo
Zhipeng You
Narges Abdian
Jamil Ahmad
Jennifer A. Ruskey
Farnaz Asayesh
Dan Spiegelman
Stanley Fahn
Cheryl Waters
Oury Monchi
Yves Dauvilliers
Nicolas Dupré
Irina Miliukhina
Alla Timofeeva
Anton Emelyanov
Sofya Pchelina
Lior Greenbaum
Sharon Hassin-Baer
Roy N. Alcalay
Austen Milnerwood
Thomas M. Durcan
Ziv Gan-Or
Edward A. Fon
The Parkinson’s disease risk gene cathepsin B promotes fibrillar alpha-synuclein clearance, lysosomal function and glucocerebrosidase activity in dopaminergic neurons
Molecular Neurodegeneration
title The Parkinson’s disease risk gene cathepsin B promotes fibrillar alpha-synuclein clearance, lysosomal function and glucocerebrosidase activity in dopaminergic neurons
title_full The Parkinson’s disease risk gene cathepsin B promotes fibrillar alpha-synuclein clearance, lysosomal function and glucocerebrosidase activity in dopaminergic neurons
title_fullStr The Parkinson’s disease risk gene cathepsin B promotes fibrillar alpha-synuclein clearance, lysosomal function and glucocerebrosidase activity in dopaminergic neurons
title_full_unstemmed The Parkinson’s disease risk gene cathepsin B promotes fibrillar alpha-synuclein clearance, lysosomal function and glucocerebrosidase activity in dopaminergic neurons
title_short The Parkinson’s disease risk gene cathepsin B promotes fibrillar alpha-synuclein clearance, lysosomal function and glucocerebrosidase activity in dopaminergic neurons
title_sort parkinson s disease risk gene cathepsin b promotes fibrillar alpha synuclein clearance lysosomal function and glucocerebrosidase activity in dopaminergic neurons
url https://doi.org/10.1186/s13024-024-00779-9
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