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Article ; Online: Neuroinflammation in Gaucher disease, neuronal ceroid lipofuscinosis, and commonalities with Parkinson's disease.

Francelle, Laetitia / Mazzulli, Joseph R

2022 Volume 1780, Page(s) 147798

Abstract: Lysosomal storage diseases (LSDs) are rare genetic disorders caused by a disruption in cellular clearance, resulting in pathological storage of undegraded lysosomal substrates. Recent clinical and genetic studies have uncovered links between multiple ... ...

Abstract	Lysosomal storage diseases (LSDs) are rare genetic disorders caused by a disruption in cellular clearance, resulting in pathological storage of undegraded lysosomal substrates. Recent clinical and genetic studies have uncovered links between multiple LSDs and common neurodegenerative diseases such as Parkinson's disease (PD). Here, we review recent literature describing the role of glia cells and neuroinflammation in PD and LSDs, including Gaucher disease (GD) and neuronal ceroid lipofuscinosis (NCL), and highlight converging inflammation pathways that lead to neuron loss. Recent data indicates that lysosomal dysfunction and accumulation of storage materials can initiate the activation of glial cells, through interaction with cell surface or cytosolic pattern recognition receptors that detect pathogenic aggregates of cellular debris. Activated glia cells could act to protect neurons through the elimination of toxic protein or lipid aggregates early in the disease process. However prolonged glial activation that occurs over several decades in chronic-age related neurodegeneration could induce the inappropriate elimination of synapses, leading to neuron loss. These studies provide mechanistic insight into the relationship between lysosomal dysfunction and glial activation, and offer novel therapeutic pathways for the treatment of PD and LSDs focused on reducing neuroinflammation and mitigating cell loss.
MeSH term(s)	Animals ; Gaucher Disease/metabolism ; Gaucher Disease/pathology ; Humans ; Lysosomes/metabolism ; Lysosomes/pathology ; Neuroinflammatory Diseases/metabolism ; Neuroinflammatory Diseases/pathology ; Neuronal Ceroid-Lipofuscinoses/metabolism ; Neuronal Ceroid-Lipofuscinoses/pathology ; Parkinson Disease/metabolism ; Parkinson Disease/pathology
Language	English
Publishing date	2022-01-19
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1200-2
ISSN	1872-6240 ; 0006-8993
ISSN (online)	1872-6240
ISSN	0006-8993
DOI	10.1016/j.brainres.2022.147798
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Article ; Online: α-Synuclein: Multiple pathogenic roles in trafficking and proteostasis pathways in Parkinson's disease.

Zalon, Annie J / Quiriconi, Drew J / Pitcairn, Caleb / Mazzulli, Joseph R

The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry

2024 , Page(s) 10738584241232963

Abstract: Parkinson's disease (PD) is a common age-related neurodegenerative disorder characterized by the loss of dopaminergic neurons in the midbrain. A hallmark of both familial and sporadic PD is the presence of Lewy body inclusions composed mainly of ... ...

Abstract	Parkinson's disease (PD) is a common age-related neurodegenerative disorder characterized by the loss of dopaminergic neurons in the midbrain. A hallmark of both familial and sporadic PD is the presence of Lewy body inclusions composed mainly of aggregated α-synuclein (α-syn), a presynaptic protein encoded by the
Language	English
Publishing date	2024-02-29
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1233753-5
ISSN	1089-4098 ; 1073-8584
ISSN (online)	1089-4098
ISSN	1073-8584
DOI	10.1177/10738584241232963
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Article ; Online: Detection of pathological alpha-synuclein aggregates in human iPSC-derived neurons and tissue.

Stojkovska, Iva / Mazzulli, Joseph R

STAR protocols

2021 Volume 2, Issue 1, Page(s) 100372

Abstract: The accumulation of proteins into insoluble aggregates is a common feature of several neurodegenerative diseases. Aggregated α-synuclein is a major component of Lewy bodies that pathologically define Parkinson's disease (PD). Here, we present methods for ...

Abstract	The accumulation of proteins into insoluble aggregates is a common feature of several neurodegenerative diseases. Aggregated α-synuclein is a major component of Lewy bodies that pathologically define Parkinson's disease (PD). Here, we present methods for the detection of pathogenic conformations of α-synuclein in induced pluripotent stem cell (iPSC) patient-derived neuron models and brain tissue. These methods can be applied to studies of PD pathogenesis and the discovery of novel therapeutics that restore physiological α-synuclein. For complete details on the use and execution of this protocol, please refer to Cuddy et al. (2019) and Zunke et al. (2018).
MeSH term(s)	Chromatography, Gel/methods ; Fluorescent Antibody Technique/methods ; Humans ; Induced Pluripotent Stem Cells/metabolism ; Neurons/cytology ; Protein Aggregation, Pathological/diagnostic imaging ; alpha-Synuclein/analysis ; alpha-Synuclein/isolation & purification ; alpha-Synuclein/metabolism
Chemical Substances	alpha-Synuclein
Language	English
Publishing date	2021-03-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	2666-1667
ISSN (online)	2666-1667
DOI	10.1016/j.xpro.2021.100372
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Article ; Online: Analysis of lysosomal hydrolase trafficking and activity in human iPSC-derived neuronal models.

Cuddy, Leah K / Mazzulli, Joseph R

STAR protocols

2021 Volume 2, Issue 1, Page(s) 100340

Abstract: Lysosomes are critical for maintaining protein homeostasis and cellular metabolism. Lysosomal dysfunction and disrupted protein trafficking contribute to cell death in neurodegenerative disorders, including Parkinson's disease and dementia. We describe ... ...

Abstract	Lysosomes are critical for maintaining protein homeostasis and cellular metabolism. Lysosomal dysfunction and disrupted protein trafficking contribute to cell death in neurodegenerative disorders, including Parkinson's disease and dementia. We describe three complementary protocols-the use of protein glycosylation, western blotting, immunofluorescence, and hydrolase activity measurement-to analyze the trafficking and activity of lysosomal proteins in patient-derived neurons differentiated from iPSCs. These methods should help to identify lysosomal phenotypes in patient-derived cultures and aid the discovery of therapeutics that augment lysosomal function. For complete details on the use and execution of this protocol, please refer to Cuddy et al. (2019).
MeSH term(s)	Cell Differentiation ; Humans ; Hydrolases/metabolism ; Induced Pluripotent Stem Cells/enzymology ; Induced Pluripotent Stem Cells/pathology ; Lysosomes/enzymology ; Lysosomes/pathology ; Models, Neurological ; Parkinson Disease/enzymology ; Parkinson Disease/pathology ; Protein Transport
Chemical Substances	Hydrolases (EC 3.-)
Language	English
Publishing date	2021-02-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	2666-1667
ISSN (online)	2666-1667
DOI	10.1016/j.xpro.2021.100340
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Article ; Online: Modeling neuronopathic storage diseases with patient-derived culture systems.

Zunke, Friederike / Mazzulli, Joseph R

Neurobiology of disease

2019 Volume 127, Page(s) 147–162

Abstract: Lysosomes are organelles involved in the degradation and recycling of macromolecules, and play a critical role in sensing metabolic information in the cell. A class of rare metabolic diseases called lysosomal storage disorders (LSD) are characterized by ... ...

Abstract	Lysosomes are organelles involved in the degradation and recycling of macromolecules, and play a critical role in sensing metabolic information in the cell. A class of rare metabolic diseases called lysosomal storage disorders (LSD) are characterized by lysosomal dysfunction and the accumulation of macromolecular substrates. The central nervous system appears to be particularly vulnerable to lysosomal dysfunction, since many LSDs are characterized by severe, widespread neurodegeneration with pediatric onset. Furthermore, variants in lysosomal genes are strongly associated with some common neurodegenerative disorders such as Parkinson's disease (PD). To better understand disease pathology and develop novel treatment strategies, it is critical to study the fundamental molecular disease mechanisms in the affected cell types that harbor endogenously expressed mutations. The discovery of methods for reprogramming of patient-derived somatic cells into induced pluripotent stem cells (iPSCs), and their differentiation into distinct neuronal and glial cell types, have provided novel opportunities to study mechanisms of lysosomal dysfunction within the relevant, vulnerable cell types. These models also expand our ability to develop and test novel therapeutic targets. We discuss recently developed methods for iPSC differentiation into distinct neuronal and glial cell types, while addressing the need for meticulous experimental techniques and parameters that are essential to accurately identify inherent cellular pathologies. iPSC models for neuronopathic LSDs and their relationship to sporadic age-related neurodegeneration are also discussed. These models should facilitate the discovery and development of personalized therapies in the future.
MeSH term(s)	Cells, Cultured ; Humans ; Lysosomal Storage Diseases/pathology ; Lysosomes/pathology ; Neurodegenerative Diseases/pathology ; Neurons/pathology
Language	English
Publishing date	2019-02-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1211786-9
ISSN	1095-953X ; 0969-9961
ISSN (online)	1095-953X
ISSN	0969-9961
DOI	10.1016/j.nbd.2019.01.018
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Article ; Online: Impaired Autophagic-Lysosomal Fusion in Parkinson's Patient Midbrain Neurons Occurs through Loss of ykt6 and Is Rescued by Farnesyltransferase Inhibition.

Pitcairn, Caleb / Murata, Naomi / Zalon, Annie J / Stojkovska, Iva / Mazzulli, Joseph R

The Journal of neuroscience : the official journal of the Society for Neuroscience

2023 Volume 43, Issue 14, Page(s) 2615–2629

Abstract: Macroautophagy is a catabolic process that coordinates with lysosomes to degrade aggregation-prone proteins and damaged organelles. Loss of macroautophagy preferentially affects neuron viability and is associated with age-related neurodegeneration. We ... ...

Abstract	Macroautophagy is a catabolic process that coordinates with lysosomes to degrade aggregation-prone proteins and damaged organelles. Loss of macroautophagy preferentially affects neuron viability and is associated with age-related neurodegeneration. We previously found that α-synuclein (α-syn) inhibits lysosomal function by blocking ykt6, a farnesyl-regulated soluble NSF attachment protein receptor (SNARE) protein that is essential for hydrolase trafficking in midbrain neurons. Using Parkinson's disease (PD) patient iPSC-derived midbrain cultures, we find that chronic, endogenous accumulation of α-syn directly inhibits autophagosome-lysosome fusion by impairing ykt6-SNAP-29 complexes. In wild-type (WT) cultures, ykt6 depletion caused a near-complete block of autophagic flux, highlighting its critical role for autophagy in human iPSC-derived neurons. In PD, macroautophagy impairment was associated with increased farnesyltransferase (FTase) activity, and FTase inhibitors restored macroautophagic flux through promoting active forms of ykt6 in human cultures, and male and female mice. Our findings indicate that ykt6 mediates cellular clearance by coordinating autophagic-lysosomal fusion and hydrolase trafficking, and that macroautophagy impairment in PD can be rescued by FTase inhibitors.
MeSH term(s)	Humans ; Male ; Mice ; Animals ; Female ; Parkinson Disease/metabolism ; Farnesyltranstransferase/metabolism ; alpha-Synuclein/metabolism ; Autophagy/physiology ; Mesencephalon/metabolism ; Neurons/metabolism ; Lysosomes/metabolism ; SNARE Proteins/metabolism ; Hydrolases/metabolism ; R-SNARE Proteins/metabolism
Chemical Substances	Farnesyltranstransferase (EC 2.5.1.29) ; alpha-Synuclein ; SNARE Proteins ; Hydrolases (EC 3.-) ; YKT6 protein, human ; R-SNARE Proteins
Language	English
Publishing date	2023-02-14
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	604637-x
ISSN	1529-2401 ; 0270-6474
ISSN (online)	1529-2401
ISSN	0270-6474
DOI	10.1523/JNEUROSCI.0610-22.2023
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Article ; Online: Is Parkinson's disease a lysosomal disorder?

Klein, Andrés D / Mazzulli, Joseph R

Brain : a journal of neurology

2018 Volume 141, Issue 8, Page(s) 2255–2262

Abstract: Common forms of Parkinson's disease have long been described as idiopathic, with no single penetrant genetic factor capable of influencing disease aetiology. Recent genetic studies indicate a clear association of variants within several lysosomal genes ... ...

Abstract	Common forms of Parkinson's disease have long been described as idiopathic, with no single penetrant genetic factor capable of influencing disease aetiology. Recent genetic studies indicate a clear association of variants within several lysosomal genes as risk factors for idiopathic Parkinson's disease. The emergence of novel variants suggest that the aetiology of idiopathic Parkinson's disease may be explained by the interaction of several partially penetrant mutations that, while seemingly complex, all appear to converge on cellular clearance pathways. These newly evolving data are consistent with mechanistic studies linking α-synuclein toxicity to lysosomal abnormalities, and indicate that idiopathic Parkinson's disease resembles features of Mendelian lysosomal storage disorders at a genetic and biochemical level. These findings offer novel pathways to exploit for the development of disease-altering therapies for idiopathic Parkinson's disease that target specific components of the lysosomal system.
MeSH term(s)	Gaucher Disease/genetics ; Gaucher Disease/physiopathology ; Humans ; Lysosomal Storage Diseases/genetics ; Lysosomal Storage Diseases/physiopathology ; Lysosomes/genetics ; Lysosomes/physiology ; Mitochondria/pathology ; Parkinson Disease/etiology ; Parkinson Disease/genetics ; Parkinson Disease/physiopathology ; Risk Factors ; alpha-Synuclein/metabolism
Chemical Substances	alpha-Synuclein
Language	English
Publishing date	2018-06-01
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80072-7
ISSN	1460-2156 ; 0006-8950
ISSN (online)	1460-2156
ISSN	0006-8950
DOI	10.1093/brain/awy147
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Article ; Online: Dysregulation of the autophagic-lysosomal pathway in Gaucher and Parkinson's disease.

Pitcairn, Caleb / Wani, Willayat Yousuf / Mazzulli, Joseph R

Neurobiology of disease

2018 Volume 122, Page(s) 72–82

Abstract: The finding that mutations in the Gaucher's Disease (GD) gene GBA1 are a strong risk factor for Parkinson's Disease (PD) has allowed for unique insights into pathophysiology centered on disruption of the autophagic-lysosomal pathway. Protein aggregations ...

Abstract	The finding that mutations in the Gaucher's Disease (GD) gene GBA1 are a strong risk factor for Parkinson's Disease (PD) has allowed for unique insights into pathophysiology centered on disruption of the autophagic-lysosomal pathway. Protein aggregations in the form of Lewy bodies and the effects of canonical PD mutations that converge on the lysosomal degradation system suggest that neurodegeneration in PD is mediated by dysregulation of protein homeostasis. The well-characterized clinical and pathological relationship between PD and the lysosomal storage disorder GD emphasizes the importance of dysregulated protein metabolism in neurodegeneration, and one intriguing piece of this relationship is a shared phenotype of autophagic-lysosomal dysfunction in both diseases. Translational application of these findings may be accelerated by the use of midbrain dopamine neuronal models derived from induced pluripotent stem cells (iPSCs) that recapitulate several pathological features of GD and PD. In this review, we discuss evidence linking autophagic dysfunction to the pathophysiology of GD and GBA1-linked parkinsonism and focus more specifically on studies performed recently in iPSC-derived neurons.
MeSH term(s)	Animals ; Autophagy/physiology ; Gaucher Disease/physiopathology ; Humans ; Lysosomes/physiology ; Parkinson Disease/physiopathology
Language	English
Publishing date	2018-03-14
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1211786-9
ISSN	1095-953X ; 0969-9961
ISSN (online)	1095-953X
ISSN	0969-9961
DOI	10.1016/j.nbd.2018.03.008
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Article: Molecular mechanisms of α-synuclein and GBA1 in Parkinson’s disease

Stojkovska, Iva / Krainc, Dimitri / Mazzulli, Joseph R

Cell and tissue research. 2018 July, v. 373, no. 1

2018

Abstract: Parkinson’s disease (PD) is a neurodegenerative movement disorder characterized pathologically by the presence of Lewy bodies comprised of insoluble alpha (α)-synuclein. Pathological, clinical and genetic studies demonstrate that mutations in the GBA1 ... ...

Abstract	Parkinson’s disease (PD) is a neurodegenerative movement disorder characterized pathologically by the presence of Lewy bodies comprised of insoluble alpha (α)-synuclein. Pathological, clinical and genetic studies demonstrate that mutations in the GBA1 gene, which encodes the lysosomal enzyme glucocerebrosidase (GCase) that is deficient in Gaucher’s disease, are important risk factors for the development of PD. The molecular mechanism for the association between these two diseases is not completely understood. We discuss several possible mechanisms that may lead to GBA1-related neuronal death and α-synuclein accumulation including disruptions in lipid metabolism, protein trafficking and impaired protein quality control mechanisms. Elucidating the mechanism between GCase and α-synuclein may provide insight into potential therapeutic pathways for PD and related synucleinopathies.
Keywords	Lewy bodies ; Parkinson disease ; cell death ; genes ; glucosylceramidase ; lipid metabolism ; mutation ; protein transport ; risk factors ; therapeutics
Language	English
Dates of publication	2018-07
Size	p. 51-60.
Publishing place	Springer Berlin Heidelberg
Document type	Article
Note	Review
ZDB-ID	125067-x
ISSN	1432-0878 ; 0302-766X
ISSN (online)	1432-0878
ISSN	0302-766X
DOI	10.1007/s00441-017-2704-y
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Article ; Online: Molecular mechanisms of α-synuclein and GBA1 in Parkinson's disease.

Stojkovska, Iva / Krainc, Dimitri / Mazzulli, Joseph R

Cell and tissue research

2017 Volume 373, Issue 1, Page(s) 51–60

Abstract: Parkinson's disease (PD) is a neurodegenerative movement disorder characterized pathologically by the presence of Lewy bodies comprised of insoluble alpha (α)-synuclein. Pathological, clinical and genetic studies demonstrate that mutations in the GBA1 ... ...

Abstract	Parkinson's disease (PD) is a neurodegenerative movement disorder characterized pathologically by the presence of Lewy bodies comprised of insoluble alpha (α)-synuclein. Pathological, clinical and genetic studies demonstrate that mutations in the GBA1 gene, which encodes the lysosomal enzyme glucocerebrosidase (GCase) that is deficient in Gaucher's disease, are important risk factors for the development of PD. The molecular mechanism for the association between these two diseases is not completely understood. We discuss several possible mechanisms that may lead to GBA1-related neuronal death and α-synuclein accumulation including disruptions in lipid metabolism, protein trafficking and impaired protein quality control mechanisms. Elucidating the mechanism between GCase and α-synuclein may provide insight into potential therapeutic pathways for PD and related synucleinopathies.
MeSH term(s)	Animals ; Glucosylceramidase/metabolism ; Humans ; Lysosomes/metabolism ; Models, Biological ; Mutation/genetics ; Parkinson Disease/genetics ; Parkinson Disease/therapy ; alpha-Synuclein/metabolism
Chemical Substances	alpha-Synuclein ; Glucosylceramidase (EC 3.2.1.45)
Language	English
Publishing date	2017-10-24
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	125067-x
ISSN	1432-0878 ; 0302-766X
ISSN (online)	1432-0878
ISSN	0302-766X
DOI	10.1007/s00441-017-2704-y
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