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Article ; Online: Network models to enhance the translational impact of cross-species studies.

Brynildsen, Julia K / Rajan, Kanaka / Henderson, Michael X / Bassett, Dani S

2023 Volume 24, Issue 9, Page(s) 575–588

Abstract: Neuroscience studies are often carried out in animal models for the purpose of understanding specific aspects of the human condition. However, the translation of findings across species remains a substantial challenge. Network science approaches can ... ...

Abstract	Neuroscience studies are often carried out in animal models for the purpose of understanding specific aspects of the human condition. However, the translation of findings across species remains a substantial challenge. Network science approaches can enhance the translational impact of cross-species studies by providing a means of mapping small-scale cellular processes identified in animal model studies to larger-scale inter-regional circuits observed in humans. In this Review, we highlight the contributions of network science approaches to the development of cross-species translational research in neuroscience. We lay the foundation for our discussion by exploring the objectives of cross-species translational models. We then discuss how the development of new tools that enable the acquisition of whole-brain data in animal models with cellular resolution provides unprecedented opportunity for cross-species applications of network science approaches for understanding large-scale brain networks. We describe how these tools may support the translation of findings across species and imaging modalities and highlight future opportunities. Our overarching goal is to illustrate how the application of network science tools across human and animal model studies could deepen insight into the neurobiology that underlies phenomena observed with non-invasive neuroimaging methods and could simultaneously further our ability to translate findings across species.
MeSH term(s)	Animals ; Humans ; Brain ; Neuroimaging ; Translational Research, Biomedical/methods ; Neurosciences ; Neurobiology
Language	English
Publishing date	2023-07-31
Publishing country	England
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural
ZDB-ID	2034150-7
ISSN	1471-0048 ; 1471-0048 ; 1471-003X
ISSN (online)	1471-0048
ISSN	1471-0048 ; 1471-003X
DOI	10.1038/s41583-023-00720-x
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Zs.A 5473: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article: A topographical atlas of α-synuclein dosage and cell type-specific expression in adult mouse brain and peripheral organs.

Geertsma, Haley M / Fisk, Zoe A / Sauline, Lillian / Prigent, Alice / Kurgat, Kevin / Callaghan, Steve M / Henderson, Michael X / Rousseaux, Maxime W C

NPJ Parkinson's disease

2024 Volume 10, Issue 1, Page(s) 65

Abstract: Parkinson's disease (PD) is the second most common neurodegenerative disease worldwide and presents pathologically with Lewy pathology and dopaminergic neurodegeneration. Lewy pathology contains aggregated α-synuclein (αSyn), a protein encoded by the ... ...

Abstract	Parkinson's disease (PD) is the second most common neurodegenerative disease worldwide and presents pathologically with Lewy pathology and dopaminergic neurodegeneration. Lewy pathology contains aggregated α-synuclein (αSyn), a protein encoded by the SNCA gene which is also mutated or duplicated in a subset of familial PD cases. Due to its predominant presynaptic localization, immunostaining for the protein results in a diffuse reactivity pattern, providing little insight into the types of cells expressing αSyn. As a result, insight into αSyn expression-driven cellular vulnerability has been difficult to ascertain. Using a combination of knock-in mice that target αSyn to the nucleus (Snca
Language	English
Publishing date	2024-03-19
Publishing country	United States
Document type	Journal Article
ZDB-ID	2819218-7
ISSN	2373-8057
ISSN	2373-8057
DOI	10.1038/s41531-024-00672-8
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Article ; Online: LRRK2 Kinase Activity Does Not Alter Cell-Autonomous Tau Pathology Development in Primary Neurons.

Henderson, Michael X / Changolkar, Lakshmi / Trojanowski, John Q / Lee, Virginia M Y

Journal of Parkinson's disease

2021 Volume 11, Issue 3, Page(s) 1187–1196

Abstract: Background: Mutations in leucine-rich repeat kinase 2 (LRRK2) are the most common cause of familial Parkinson's disease (PD) and are also associated with genetic risk in idiopathic PD. Mutations in LRRK2, including the most common p.G2019S lead to ... ...

Abstract	Background: Mutations in leucine-rich repeat kinase 2 (LRRK2) are the most common cause of familial Parkinson's disease (PD) and are also associated with genetic risk in idiopathic PD. Mutations in LRRK2, including the most common p.G2019S lead to elevated kinase activity, making LRRK2 kinase inhibitors prime targets for therapeutic development. However, the role of LRRK2 kinase activity in PD pathogenesis has remained unclear. While essentially all LRRK2-PD patients exhibit dopaminergic neuron loss, many of these patients do not have α-synuclein Lewy bodies in their brains. So, what is the neuropathological substrate of LRRK2-PD? Tau has emerged as a possible candidate due to the presence of tau pathology in the majority of LRRK2 mutation carriers and reports of hyperphosphorylated tau in LRRK2 animal models. Objective: In the current study, we aim to address whether a mutation in LRRK2 changes the cell-autonomous seeding of tau pathology in primary neurons. We also aim to assess whether LRRK2 kinase inhibitors are able to modulate tau pathology. Methods/results: Treatment of primary neurons with LRRK2 kinase inhibitors leads to prolonged kinase inhibition but does not alter tau pathology induction. The lack of an effect of LRRK2 kinase activity was further confirmed in primary neurons expressing LRRK2G2019S and with two different forms of pathogenic tau. In no case was there more than a minor change in tau pathology induction. Conclusion: Together, our results indicate that LRRK2 kinase activity is not playing a major role in the induction of tau pathology in individual neurons. Understanding the impact of LRRK2 kinase inhibitors on pathology generation is important as kinase inhibitors move forward in clinical trials.
MeSH term(s)	Animals ; Brain/metabolism ; Humans ; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2/genetics ; Lewy Bodies/metabolism ; Mutation/genetics ; Neurons/metabolism ; Parkinson Disease/genetics
Chemical Substances	LRRK2 protein, human (EC 2.7.11.1) ; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 (EC 2.7.11.1)
Language	English
Publishing date	2021-03-15
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2620609-2
ISSN	1877-718X ; 1877-7171
ISSN (online)	1877-718X
ISSN	1877-7171
DOI	10.3233/JPD-212562
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Zs.A 6964: Show issues

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Article ; Online: Spatial transcriptomics reveals molecular dysfunction associated with cortical Lewy pathology.

Goralski, Thomas M / Meyerdirk, Lindsay / Breton, Libby / Brasseur, Laura / Kurgat, Kevin / DeWeerd, Daniella / Turner, Lisa / Becker, Katelyn / Adams, Marie / Newhouse, Daniel J / Henderson, Michael X

Nature communications

2024 Volume 15, Issue 1, Page(s) 2642

Abstract: A key hallmark of Parkinson's disease (PD) is Lewy pathology. Composed of α-synuclein, Lewy pathology is found both in dopaminergic neurons that modulate motor function, and cortical regions that control cognitive function. Recent work has established ... ...

Abstract	A key hallmark of Parkinson's disease (PD) is Lewy pathology. Composed of α-synuclein, Lewy pathology is found both in dopaminergic neurons that modulate motor function, and cortical regions that control cognitive function. Recent work has established the molecular identity of dopaminergic neurons susceptible to death, but little is known about cortical neurons susceptible to Lewy pathology or molecular changes induced by aggregates. In the current study, we use spatial transcriptomics to capture whole transcriptome signatures from cortical neurons with α-synuclein pathology compared to neurons without pathology. We find, both in PD and related PD dementia, dementia with Lewy bodies and in the pre-formed fibril α-synucleinopathy mouse model, that specific classes of excitatory neurons are vulnerable to developing Lewy pathology. Further, we identify conserved gene expression changes in aggregate-bearing neurons that we designate the Lewy-associated molecular dysfunction from aggregates (LAMDA) signature. Neurons with aggregates downregulate synaptic, mitochondrial, ubiquitin-proteasome, endo-lysosomal, and cytoskeletal genes and upregulate DNA repair and complement/cytokine genes. Our results identify neurons vulnerable to Lewy pathology in the PD cortex and describe a conserved signature of molecular dysfunction in both mice and humans.
MeSH term(s)	Humans ; Mice ; Animals ; alpha-Synuclein/metabolism ; Lewy Body Disease/pathology ; Parkinson Disease/metabolism ; Synucleinopathies ; Dopaminergic Neurons/metabolism ; Gene Expression Profiling
Chemical Substances	alpha-Synuclein
Language	English
Publishing date	2024-03-26
Publishing country	England
Document type	Journal Article
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-024-47027-8
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Article ; Online: α-Synuclein pathology in Parkinson's disease and related α-synucleinopathies.

Henderson, Michael X / Trojanowski, John Q / Lee, Virginia M-Y

Neuroscience letters

2019 Volume 709, Page(s) 134316

Abstract: Over 20 years ago, the synaptic protein α-synuclein was identified as the primary component of the Lewy bodies (LBs) that are a sine qua non of Parkinson's disease (PD). Since that time, extensive research has demonstrated that α-synuclein pathology is ... ...

Abstract	Over 20 years ago, the synaptic protein α-synuclein was identified as the primary component of the Lewy bodies (LBs) that are a sine qua non of Parkinson's disease (PD). Since that time, extensive research has demonstrated that α-synuclein pathology is not only a hallmark of PD, but can also cause neuronal dysfunction and death. Detailed staging of α-synuclein pathology in the brains of patients has revealed a progressive pattern of pathology that correlates with the symptoms of disease. Early in the disease course, PD patients exhibit motor dysfunction, and α-synuclein pathology at this stage is primarily found in regions controlling motor function. At later stages of disease as patients' cognitive function deteriorates, α-synuclein pathology can be found in cortical structures responsible for higher cognitive processing. The stereotypical progression of α-synuclein pathology through the brain over time suggests that there may be a physical transmission of pathological α-synuclein from one area of the brain to another. The transmission hypothesis posits that an initial seed of pathological α-synuclein in one neuron may be released and taken up by another vulnerable neuron and thereby initiate pathological misfolding of α-synuclein in the recipient neuron. In recent years, convergent evidence from various studies has indicated that pathological protein transmission can occur in the human brain. Cell and animal models based on the transmission hypothesis have shown not only that pathological α-synuclein can be transmitted from cell-to-cell, but that this pathology can lead to neuronal dysfunction and degeneration. The α-synuclein transmission hypothesis has profound implications for treatment of what is currently an intractable neurodegenerative disease. In this review, we explore the evidence for cell-to-cell transmission of pathological α-synuclein, the current understanding of how pathological α-synuclein can move to a new cell and template misfolding, and the therapeutic implications of α-synuclein transmission.
MeSH term(s)	Animals ; Brain/metabolism ; Brain/pathology ; Glymphatic System/metabolism ; Glymphatic System/pathology ; Humans ; Lewy Bodies/metabolism ; Lewy Bodies/pathology ; Parkinson Disease/genetics ; Parkinson Disease/metabolism ; Parkinson Disease/pathology ; Synucleinopathies/genetics ; Synucleinopathies/metabolism ; Synucleinopathies/pathology ; alpha-Synuclein/genetics ; alpha-Synuclein/metabolism
Chemical Substances	alpha-Synuclein
Language	English
Publishing date	2019-06-03
Publishing country	Ireland
Document type	Journal Article ; Review
ZDB-ID	194929-9
ISSN	1872-7972 ; 0304-3940
ISSN (online)	1872-7972
ISSN	0304-3940
DOI	10.1016/j.neulet.2019.134316
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Zs.A 1166: Show issues

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Article: LRRK2 kinase inhibition reverses G2019S mutation-dependent effects on tau pathology progression.

Lubben, Noah / Brynildsen, Julia K / Webb, Connor M / Li, Howard L / Leyns, Cheryl E G / Changolkar, Lakshmi / Zhang, Bin / Meymand, Emily S / O'Reilly, Mia / Madaj, Zach / DeWeerd, Daniella / Fell, Matthew J / Lee, Virginia M Y / Bassett, Dani S / Henderson, Michael X

Translational neurodegeneration

2024 Volume 13, Issue 1, Page(s) 13

Abstract: Background: Mutations in leucine-rich repeat kinase 2 (LRRK2) are the most common cause of familial Parkinson's disease (PD). These mutations elevate the LRRK2 kinase activity, making LRRK2 kinase inhibitors an attractive therapeutic. LRRK2 kinase ... ...

Abstract	Background: Mutations in leucine-rich repeat kinase 2 (LRRK2) are the most common cause of familial Parkinson's disease (PD). These mutations elevate the LRRK2 kinase activity, making LRRK2 kinase inhibitors an attractive therapeutic. LRRK2 kinase activity has been consistently linked to specific cell signaling pathways, mostly related to organelle trafficking and homeostasis, but its relationship to PD pathogenesis has been more difficult to define. LRRK2-PD patients consistently present with loss of dopaminergic neurons in the substantia nigra but show variable development of Lewy body or tau tangle pathology. Animal models carrying LRRK2 mutations do not develop robust PD-related phenotypes spontaneously, hampering the assessment of the efficacy of LRRK2 inhibitors against disease processes. We hypothesized that mutations in LRRK2 may not be directly related to a single disease pathway, but instead may elevate the susceptibility to multiple disease processes, depending on the disease trigger. To test this hypothesis, we have previously evaluated progression of α-synuclein and tau pathologies following injection of proteopathic seeds. We demonstrated that transgenic mice overexpressing mutant LRRK2 show alterations in the brain-wide progression of pathology, especially at older ages. Methods: Here, we assess tau pathology progression in relation to long-term LRRK2 kinase inhibition. Wild-type or LRRK2 Results: Consistent with our previous work, we found systemic alterations in the progression of tau pathology in LRRK2 Conclusions: This work supports a protective role of LRRK2 kinase inhibition in G2019S carriers and provides a rational workflow for systematic evaluation of brain-wide phenotypes in therapeutic development.
MeSH term(s)	Animals ; Humans ; Mice ; Brain ; Dopaminergic Neurons ; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2/genetics ; Lewy Bodies ; Mice, Transgenic ; Mutation/genetics
Chemical Substances	Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 (EC 2.7.11.1) ; LRRK2 protein, human (EC 2.7.11.1) ; Lrrk2 protein, mouse (EC 2.7.11.1)
Language	English
Publishing date	2024-03-04
Publishing country	England
Document type	Journal Article
ZDB-ID	2653701-1
ISSN	2047-9158
ISSN	2047-9158
DOI	10.1186/s40035-024-00403-2
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Article ; Online: The roles of connectivity and neuronal phenotype in determining the pattern of α-synuclein pathology in Parkinson's disease.

Henderson, Michael X / Henrich, Martin T / Geibl, Fanni F / Oertel, Wolfgang H / Brundin, Patrik / Surmeier, D James

Neurobiology of disease

2022 Volume 168, Page(s) 105687

Abstract: Parkinson's disease (PD) is the most common neurodegenerative movement disorder, and motor dysfunction has been attributed to loss of dopaminergic neurons. However, motor dysfunction is only one of many symptoms experienced by patients. A ... ...

Abstract	Parkinson's disease (PD) is the most common neurodegenerative movement disorder, and motor dysfunction has been attributed to loss of dopaminergic neurons. However, motor dysfunction is only one of many symptoms experienced by patients. A neuropathological hallmark of PD is intraneuronal protein aggregates called Lewy pathology (LP). Neuropathological staging studies have shown that dopaminergic neurons are only one of the many cell types prone to manifest LP. Progressive appearance of LP in multiple brain regions, as well as peripheral nerves, has led to the popular hypothesis that LP and misfolded forms of one of its major components - α-synuclein (aSYN) - can spread through synaptically connected circuits. However, not all brain regions or neurons within connected circuits develop LP, suggesting that cell autonomous factors modulate the development of pathology. Here, we review studies about how LP develops and progressively engages additional brain regions. We focus on how connectivity constrains progression and discuss cell autonomous factors that drive pathology development. We propose a mixed model of cell autonomous factors and trans-synaptic spread as mediators of pathology progression and put forward this model as a framework for future experiments exploring PD pathophysiology.
MeSH term(s)	Dopaminergic Neurons/metabolism ; Humans ; Parkinson Disease/metabolism ; Phenotype ; Synucleinopathies ; alpha-Synuclein/metabolism
Chemical Substances	alpha-Synuclein
Language	English
Publishing date	2022-03-10
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1211786-9
ISSN	1095-953X ; 0969-9961
ISSN (online)	1095-953X
ISSN	0969-9961
DOI	10.1016/j.nbd.2022.105687
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Article ; Online: MOG-IgG Among Participants in the Pediatric Optic Neuritis Prospective Outcomes Study.

Chen, John J / Pineles, Stacy L / Repka, Michael X / Pittock, Sean J / Henderson, Robert J / Liu, Grant T

JAMA ophthalmology

2021 Volume 139, Issue 5, Page(s) 583–585

MeSH term(s)	Autoantibodies ; Child ; Humans ; Immunoglobulin G ; Myelin-Oligodendrocyte Glycoprotein ; Optic Neuritis/diagnosis ; Optic Neuritis/drug therapy ; Prospective Studies
Chemical Substances	Autoantibodies ; Immunoglobulin G ; Myelin-Oligodendrocyte Glycoprotein
Language	English
Publishing date	2021-03-04
Publishing country	United States
Document type	Letter ; Research Support, N.I.H., Extramural
ZDB-ID	2701705-9
ISSN	2168-6173 ; 2168-6165
ISSN (online)	2168-6173
ISSN	2168-6165
DOI	10.1001/jamaophthalmol.2021.0349
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Article: Spatial transcriptomics reveals molecular dysfunction associated with Lewy pathology.

Goralski, Thomas / Meyerdirk, Lindsay / Breton, Libby / Brasseur, Laura / Kurgat, Kevin / DeWeerd, Daniella / Turner, Lisa / Becker, Katelyn / Adams, Marie / Newhouse, Daniel / Henderson, Michael X

bioRxiv : the preprint server for biology

2023

Abstract: Lewy pathology composed of α-synuclein is the key pathological hallmark of Parkinson's disease (PD), found both in dopaminergic neurons that control motor function, and throughout cortical regions that control cognitive function. Recent work has ... ...

Abstract	Lewy pathology composed of α-synuclein is the key pathological hallmark of Parkinson's disease (PD), found both in dopaminergic neurons that control motor function, and throughout cortical regions that control cognitive function. Recent work has investigated which dopaminergic neurons are most susceptible to death, but little is known about which neurons are vulnerable to developing Lewy pathology and what molecular changes an aggregate induces. In the current study, we use spatial transcriptomics to selectively capture whole transcriptome signatures from cortical neurons with Lewy pathology compared to those without pathology in the same brains. We find, both in PD and in a mouse model of PD, that there are specific classes of excitatory neurons that are vulnerable to developing Lewy pathology in the cortex. Further, we identify conserved gene expression changes in aggregate-bearing neurons that we designate the Lewy-associated molecular dysfunction from aggregates (LAMDA) signature. This gene signature indicates that neurons with aggregates downregulate synaptic, mitochondrial, ubiquitin-proteasome, endo-lysosomal, and cytoskeletal genes and upregulate DNA repair and complement/cytokine genes. However, beyond DNA repair gene upregulation, we find that neurons also activate apoptotic pathways, suggesting that if DNA repair fails, neurons undergo programmed cell death. Our results identify neurons vulnerable to Lewy pathology in the PD cortex and identify a conserved signature of molecular dysfunction in both mice and humans.
Language	English
Publishing date	2023-05-17
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.05.17.541144
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Article ; Online: Alzheimer's disease tau is a prominent pathology in LRRK2 Parkinson's disease.

Henderson, Michael X / Sengupta, Medha / Trojanowski, John Q / Lee, Virginia M Y

Acta neuropathologica communications

2019 Volume 7, Issue 1, Page(s) 183

Abstract: Mutations in leucine-rich repeat kinase 2 (LRRK2) are the most common cause of familial Parkinson's disease (PD). While the clinical presentation of LRRK2 mutation carriers is similar to that of idiopathic PD (iPD) patients, the neuropathology of LRRK2 ... ...

Abstract	Mutations in leucine-rich repeat kinase 2 (LRRK2) are the most common cause of familial Parkinson's disease (PD). While the clinical presentation of LRRK2 mutation carriers is similar to that of idiopathic PD (iPD) patients, the neuropathology of LRRK2 PD is less clearly defined. Lewy bodies (LBs) composed of α-synuclein are a major feature of iPD, but are not present in all LRRK2 PD cases. There is some evidence that tau may act as a neuropathological substrate in LB-negative LRRK2 PD, but this has not been examined systematically. In the current study, we examined α-synuclein, tau, and amyloid β (Aβ) pathologies in 12 LRRK2 mutation carriers. We find that α-synuclein pathology is present in 63.6% of LRRK2 mutation carriers, but tau pathology can be found in 100% of carriers and is abundant in 91% of carriers. We further use an antibody which selectively binds Alzheimer's disease (AD)-type tau and use quantitative analysis of tau pathology to demonstrate that AD tau is the prominent type of tau present in LRRK2 mutation carriers. Abundant Aβ pathology can also be found in LRRK2 mutation carriers and is consistent with comorbid AD pathology. Finally, we assessed the association of neuropathology with clinical features in LRRK2 mutation carriers and idiopathic individuals and find that LRRK2 PD shares clinical and pathological features of idiopathic PD. The prevalence of AD-type tau pathology in LRRK2 PD is an important consideration for understanding PD pathogenesis and refining clinical trial inclusion and progression criterion.
MeSH term(s)	Alzheimer Disease/genetics ; Alzheimer Disease/pathology ; Brain/pathology ; Heterozygote ; Humans ; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2/genetics ; Mutation/genetics ; Parkinson Disease/genetics ; Parkinson Disease/pathology ; tau Proteins/genetics
Chemical Substances	MAPT protein, human ; tau Proteins ; LRRK2 protein, human (EC 2.7.11.1) ; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 (EC 2.7.11.1)
Language	English
Publishing date	2019-11-16
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2715589-4
ISSN	2051-5960 ; 2051-5960
ISSN (online)	2051-5960
ISSN	2051-5960
DOI	10.1186/s40478-019-0836-x
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