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Article ; Online: A mutant methionyl-tRNA synthetase-based toolkit to assess induced-mesenchymal stromal cell secretome in mixed-culture disease models.

Burgess, Jeremy D / Amerna, Danilyn / Norton, Emily S / Parsons, Tammee M / Perkerson, Ralph B / Faroqi, Ayman H / Wszolek, Zbigniew K / Guerrero Cazares, Hugo / Kanekiyo, Takahisa / Delenclos, Marion / McLean, Pamela J

Stem cell research & therapy

2023 Volume 14, Issue 1, Page(s) 289

Abstract: Background: Mesenchymal stromal cells (MSCs) have a dynamic secretome that plays a critical role in tissue repair and regeneration. However, studying the MSC secretome in mixed-culture disease models remains challenging. This study aimed to develop a ... ...

Abstract	Background: Mesenchymal stromal cells (MSCs) have a dynamic secretome that plays a critical role in tissue repair and regeneration. However, studying the MSC secretome in mixed-culture disease models remains challenging. This study aimed to develop a mutant methionyl-tRNA synthetase-based toolkit (MetRS Methods: We used CRISPR/Cas9 homology-directed repair to stably integrate MetRS Results: Our results showed successful integration of MetRS Conclusions: The MetRS
MeSH term(s)	Methionine-tRNA Ligase/genetics ; Methionine-tRNA Ligase/metabolism ; Lipopolysaccharides ; Secretome ; Mesenchymal Stem Cells/metabolism ; Amino Acids
Chemical Substances	Methionine-tRNA Ligase (EC 6.1.1.10) ; Lipopolysaccharides ; Amino Acids
Language	English
Publishing date	2023-10-05
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2548671-8
ISSN	1757-6512 ; 1757-6512
ISSN (online)	1757-6512
ISSN	1757-6512
DOI	10.1186/s13287-023-03515-0
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Article: A Mutant Methionyl-tRNA Synthetase-Based toolkit to assess induced-Mesenchymal Stromal Cell secretome in mixed-culture disease models.

Burgess, Jeremy D / Amerna, Danilyn / Norton, Emily S / Parsons, Tammee M / Perkerson, Ralph B / Faroqi, Ayman H / Wszolek, Zbigniew K / Cazares, Hugo Guerrero / Kanekiyo, Takahisa / Delenclos, Marion / McLean, Pamela J

Research square

2023

Abstract: ... ...

Abstract	Background
Language	English
Publishing date	2023-05-03
Publishing country	United States
Document type	Preprint
DOI	10.21203/rs.3.rs-2838195/v1
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Article: Honokiol decreases alpha-synuclein mRNA levels and reveals novel targets for modulating alpha-synuclein expression.

Fagen, Sara J / Burgess, Jeremy D / Lim, Melina J / Amerna, Danilyn / Kaya, Zeynep B / Faroqi, Ayman H / Perisetla, Priyanka / DeMeo, Natasha N / Stojkovska, Iva / Quiriconi, Drew J / Mazzulli, Joseph R / Delenclos, Marion / Boschen, Suelen L / McLean, Pamela J

Frontiers in aging neuroscience

2023 Volume 15, Page(s) 1179086

Abstract: Background: Intracytoplasmic inclusions comprised of aggregated alpha-synuclein (αsyn) represent a key histopathological feature of neurological disorders collectively termed "synucleinopathies," which includes Parkinson's disease (PD). Mutations and ... ...

Abstract	Background: Intracytoplasmic inclusions comprised of aggregated alpha-synuclein (αsyn) represent a key histopathological feature of neurological disorders collectively termed "synucleinopathies," which includes Parkinson's disease (PD). Mutations and multiplications in the Methods: Human neuroglioma cells stably overexpressing αsyn, mouse primary neurons, and human iPSC-derived neurons were exposed to HKL and αsyn protein and Results: We demonstrate that HKL can successfully reduce αsyn protein levels and Conclusion: This study supports a HKL-mediated downregulation of
Language	English
Publishing date	2023-08-10
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2558898-9
ISSN	1663-4365
ISSN	1663-4365
DOI	10.3389/fnagi.2023.1179086
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Article ; Online: Cellular models of alpha-synuclein toxicity and aggregation.

Delenclos, Marion / Burgess, Jeremy D / Lamprokostopoulou, Agaristi / Outeiro, Tiago F / Vekrellis, Kostas / McLean, Pamela J

Journal of neurochemistry

2019 Volume 150, Issue 5, Page(s) 566–576

Abstract: Misfolding and aggregation of alpha-synuclein (α-synuclein) with concomitant cytotoxicity is a hallmark of Lewy body related disorders such as Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. Although it plays a pivotal role ... ...

Abstract	Misfolding and aggregation of alpha-synuclein (α-synuclein) with concomitant cytotoxicity is a hallmark of Lewy body related disorders such as Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. Although it plays a pivotal role in pathogenesis and disease progression, the function of α-synuclein and the molecular mechanisms underlying α-synuclein-induced neurotoxicity in these diseases are still elusive. Many in vitro and in vivo experimental models mimicking α-synuclein pathology such as oligomerization, toxicity and more recently neuronal propagation have been generated over the years. In particular, cellular models have been crucial for our comprehension of the pathogenic process of the disease and are beneficial for screening of molecules capable of modulating α-synuclein toxicity. Here, we review α-synuclein based cell culture models that reproduce some features of the neuronal populations affected in patients, from basic unicellular organisms to mammalian cell lines and primary neurons, to the cutting edge models of patient-specific cell lines. These reprogrammed cells known as induced pluripotent stem cells (iPSCs) have garnered attention because they closely reproduce the characteristics of neurons found in patients and provide a valuable tool for mechanistic studies. We also discuss how different cell models may constitute powerful tools for high-throughput screening of molecules capable of modulating α-synuclein toxicity and prevention of its propagation. This article is part of the Special Issue "Synuclein".
MeSH term(s)	Cell Culture Techniques ; Cells, Cultured ; Cellular Reprogramming ; Dopamine/metabolism ; Drug Evaluation, Preclinical ; HEK293 Cells ; Humans ; In Vitro Techniques ; Induced Pluripotent Stem Cells/metabolism ; Lewy Bodies/metabolism ; Models, Neurological ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology ; Neurons/metabolism ; Protein Aggregation, Pathological/metabolism ; Protein Folding ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Synucleinopathies/metabolism ; alpha-Synuclein/metabolism
Chemical Substances	Recombinant Proteins ; Saccharomyces cerevisiae Proteins ; alpha-Synuclein ; Dopamine (VTD58H1Z2X)
Language	English
Publishing date	2019-07-30
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	80158-6
ISSN	1471-4159 ; 0022-3042 ; 1474-1644
ISSN (online)	1471-4159
ISSN	0022-3042 ; 1474-1644
DOI	10.1111/jnc.14806
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Article ; Online: In Vivo

Faroqi, Ayman H / Lim, Melina J / Kee, Emma C / Lee, Jannifer H / Burgess, Jeremy D / Chen, Ridong / Di Virgilio, Francesco / Delenclos, Marion / McLean, Pamela J

Journal of neurotrauma

2020 Volume 38, Issue 5, Page(s) 655–664

Abstract: Traumatic brain injury (TBI) is traditionally characterized by primary and secondary injury phases, both contributing to pathological and morphological changes. The mechanisms of damage and chronic consequences of TBI remain to be fully elucidated, but ... ...

Abstract	Traumatic brain injury (TBI) is traditionally characterized by primary and secondary injury phases, both contributing to pathological and morphological changes. The mechanisms of damage and chronic consequences of TBI remain to be fully elucidated, but synaptic homeostasis disturbances and impaired energy metabolism are proposed to be a major contributor. It has been proposed that an increase of extracellular (eATP) adenosine triphosphate (ATP) in the area immediately surrounding impact may play a pivotal role in this sequence of events. After tissue injury, rupture of cell membranes allows release of intracellular ATP into the extracellular space, triggering a cascade of toxic events and inflammation. ATP is a ubiquitous messenger; however, simple and reliable techniques to measure its concentration have proven elusive. Here, we integrate a sensitive bioluminescent eATP sensor known as pmeLUC, with a controlled cortical impact mouse model to monitor eATP changes in a living animal after injury. Using the pmeLUC probe, a rapid increase of eATP is observed proximal to the point of impact within minutes of the injury. This event is significantly attenuated when animals are pretreated with an ATP hydrolyzing agent (apyrase) before surgery, confirming the contribution of eATP. This new eATP reporter could be useful for understanding the role of eATP in the pathogenesis in TBI and may identify a window of opportunity for therapeutic intervention.
MeSH term(s)	Adenosine Triphosphate/metabolism ; Animals ; Apyrase ; Brain Injuries, Traumatic/etiology ; Brain Injuries, Traumatic/metabolism ; Brain Injuries, Traumatic/pathology ; Disease Models, Animal ; Extracellular Space/metabolism ; Luminescent Measurements ; Mice ; Predictive Value of Tests ; Time Factors
Chemical Substances	Adenosine Triphosphate (8L70Q75FXE) ; Apyrase (EC 3.6.1.5)
Language	English
Publishing date	2020-10-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	645092-1
ISSN	1557-9042 ; 0897-7151
ISSN (online)	1557-9042
ISSN	0897-7151
DOI	10.1089/neu.2020.7226
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Article ; Online: Alpha-synuclein-induced mitochondrial dysfunction is mediated via a sirtuin 3-dependent pathway.

Park, Jae-Hyeon / Burgess, Jeremy D / Faroqi, Ayman H / DeMeo, Natasha N / Fiesel, Fabienne C / Springer, Wolfdieter / Delenclos, Marion / McLean, Pamela J

Molecular neurodegeneration

2020 Volume 15, Issue 1, Page(s) 5

Abstract: Background: Misfolding and aggregation of the presynaptic protein alpha-synuclein (αsyn) is a hallmark of Parkinson's disease (PD) and related synucleinopathies. Although predominantly localized in the cytosol, a body of evidence has shown that αsyn ... ...

Abstract	Background: Misfolding and aggregation of the presynaptic protein alpha-synuclein (αsyn) is a hallmark of Parkinson's disease (PD) and related synucleinopathies. Although predominantly localized in the cytosol, a body of evidence has shown that αsyn localizes to mitochondria and contributes to the disruption of key mitochondrial processes. Mitochondrial dysfunction is central to the progression of PD and mutations in mitochondrial-associated proteins are found in familial cases of PD. The sirtuins are highly conserved nicotinamide adenine dinucleotide (NAD Methods: The level of mitochondrial SIRT3 was assessed in cells expressing oligomeric αsyn within the cytosolic and mitochondrial-enriched fractions. Mitochondrial integrity, respiration, and health were examined using several markers of mitochondrial dynamics and stress response and by measuring the rate of oxygen consumption (OCR). Our findings were validated in a rodent model of PD as well as in human post-mortem Lewy body disease (LBD) brain tissue. Results: Here, we demonstrate that αsyn associates with mitochondria and induces a decrease in mitochondrial SIRT3 levels and mitochondrial biogenesis. We show that SIRT3 downregulation is accompanied by decreased phosphorylation of AMPK and cAMP-response element binding protein (CREB), as well as increased phosphorylation of dynamin-related protein 1 (DRP1), indicative of impaired mitochondrial dynamics. OCR was significantly decreased suggesting a mitochondria respiratory deficit. Interestingly treatment with AMPK agonist 5-aminoimidazole-4-carboxamide-1-β-d-ribofuranoside (AICAR) restores SIRT3 expression, improves mitochondrial function, and decreases αsyn oligomer formation in a SIRT3-dependent manner. Conclusions: Together, our findings suggest that pharmacologically increasing SIRT3 levels can counteract αsyn-induced mitochondrial dysfunction by reducing αsyn oligomers and normalizing mitochondrial bioenergetics. These data support a protective role for SIRT3 in PD-associated pathways and contribute significant mechanistic insight into the interplay of SIRT3 and αsyn.
MeSH term(s)	Aged ; Animals ; Female ; Humans ; Male ; Mice ; Middle Aged ; Mitochondria/metabolism ; Mitochondria/pathology ; Parkinson Disease/metabolism ; Parkinson Disease/pathology ; Rats ; Rats, Sprague-Dawley ; Sirtuin 3/metabolism ; alpha-Synuclein/metabolism
Chemical Substances	alpha-Synuclein ; Sirtuin 3 (EC 3.5.1.-)
Language	English
Publishing date	2020-01-13
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2244557-2
ISSN	1750-1326 ; 1750-1326
ISSN (online)	1750-1326
ISSN	1750-1326
DOI	10.1186/s13024-019-0349-x
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Article ; Online: APOE4 exacerbates α-synuclein seeding activity and contributes to neurotoxicity in Alzheimer's disease with Lewy body pathology.

Jin, Yunjung / Li, Fuyao / Sonoustoun, Berkiye / Kondru, Naveen Chandra / Martens, Yuka A / Qiao, Wenhui / Heckman, Michael G / Ikezu, Tadafumi C / Li, Zonghua / Burgess, Jeremy D / Amerna, Danilyn / O'Leary, Justin / DeTure, Michael A / Zhao, Jing / McLean, Pamela J / Dickson, Dennis W / Ross, Owen A / Bu, Guojun / Zhao, Na

Acta neuropathologica

2022 Volume 143, Issue 6, Page(s) 641–662

Abstract: Approximately half of Alzheimer's disease (AD) brains have concomitant Lewy pathology at autopsy, suggesting that α-synuclein (α-SYN) aggregation is a regulated event in the pathogenesis of AD. Genome-wide association studies revealed that the ε4 allele ... ...

Abstract	Approximately half of Alzheimer's disease (AD) brains have concomitant Lewy pathology at autopsy, suggesting that α-synuclein (α-SYN) aggregation is a regulated event in the pathogenesis of AD. Genome-wide association studies revealed that the ε4 allele of the apolipoprotein E (APOE4) gene, the strongest genetic risk factor for AD, is also the most replicated genetic risk factor for Lewy body dementia (LBD), signifying an important role of APOE4 in both amyloid-β (Aβ) and α-SYN pathogenesis. How APOE4 modulates α-SYN aggregation in AD is unclear. In this study, we aimed to determine how α-SYN is associated with AD-related pathology and how APOE4 impacts α-SYN seeding and toxicity. We measured α-SYN levels and their association with other established AD-related markers in brain samples from autopsy-confirmed AD patients (N = 469), where 54% had concomitant LB pathology (AD + LB). We found significant correlations between the levels of α-SYN and those of Aβ40, Aβ42, tau and APOE, particularly in insoluble fractions of AD + LB. Using a real-time quaking-induced conversion (RT-QuIC) assay, we measured the seeding activity of soluble α-SYN and found that α-SYN seeding was exacerbated by APOE4 in the AD cohort, as well as a small cohort of autopsy-confirmed LBD brains with minimal Alzheimer type pathology. We further fractionated the soluble AD brain lysates by size exclusion chromatography (SEC) ran on fast protein liquid chromatography (FPLC) and identified the α-SYN species (~ 96 kDa) that showed the strongest seeding activity. Finally, using human induced pluripotent stem cell (iPSC)-derived neurons, we showed that amplified α-SYN aggregates from AD + LB brain of patients with APOE4 were highly toxic to neurons, whereas the same amount of α-SYN monomer was not toxic. Our findings suggest that the presence of LB pathology correlates with AD-related pathologies and that APOE4 exacerbates α-SYN seeding activity and neurotoxicity, providing mechanistic insight into how APOE4 affects α-SYN pathogenesis in AD.
MeSH term(s)	Alzheimer Disease/pathology ; Apolipoprotein E4/genetics ; Apolipoproteins E ; Genome-Wide Association Study ; Humans ; Induced Pluripotent Stem Cells/metabolism ; Lewy Bodies/pathology ; Lewy Body Disease/pathology ; Neurotoxicity Syndromes ; alpha-Synuclein/metabolism ; tau Proteins/metabolism
Chemical Substances	ApoE protein, human ; Apolipoprotein E4 ; Apolipoproteins E ; alpha-Synuclein ; tau Proteins
Language	English
Publishing date	2022-04-26
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1079-0
ISSN	1432-0533 ; 0001-6322
ISSN (online)	1432-0533
ISSN	0001-6322
DOI	10.1007/s00401-022-02421-8
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Article ; Online: MAPT haplotype-stratified GWAS reveals differential association for AD risk variants.

Strickland, Samantha L / Reddy, Joseph S / Allen, Mariet / N'songo, Aurelie / Burgess, Jeremy D / Corda, Morgane M / Ballard, Travis / Wang, Xue / Carrasquillo, Minerva M / Biernacka, Joanna M / Jenkins, Gregory D / Mukherjee, Shubhabrata / Boehme, Kevin / Crane, Paul / Kauwe, John S / Ertekin-Taner, Nilüfer

Alzheimer's & dementia : the journal of the Alzheimer's Association

2020 Volume 16, Issue 7, Page(s) 983–1002

Abstract: Introduction: MAPT H1 haplotype is implicated as a risk factor for neurodegenerative diseases including Alzheimer's disease (AD).: Methods: Using Alzheimer's Disease Genetics Consortium (ADGC) genome-wide association study (GWAS) data (n = 18,841), ... ...

Abstract	Introduction: MAPT H1 haplotype is implicated as a risk factor for neurodegenerative diseases including Alzheimer's disease (AD). Methods: Using Alzheimer's Disease Genetics Consortium (ADGC) genome-wide association study (GWAS) data (n = 18,841), we conducted a MAPT H1/H2 haplotype-stratified association to discover MAPT haplotype-specific AD risk loci. Results: We identified 11 loci-5 in H2-non-carriers and 6 in H2-carriers-although none of the MAPT haplotype-specific associations achieved genome-wide significance. The most significant H2 non-carrier-specific association was with a NECTIN2 intronic (P = 1.33E-07) variant, and that for H2 carriers was near NKX6-1 (P = 1.99E-06). The GABRG2 locus had the strongest epistasis with MAPT H1/H2 variant rs8070723 (P = 3.91E-06). Eight of the 12 genes at these loci had transcriptome-wide significant differential expression in AD versus control temporal cortex (q < 0.05). Six genes were members of the brain transcriptional co-expression network implicated in "synaptic transmission" (P = 9.85E-59), which is also enriched for neuronal genes (P = 1.0E-164), including MAPT. Discussion: This stratified GWAS identified loci that may confer AD risk in a MAPT haplotype-specific manner. This approach may preferentially enrich for neuronal genes implicated in synaptic transmission.
MeSH term(s)	Alzheimer Disease/genetics ; Genetic Loci ; Genetic Predisposition to Disease ; Genome-Wide Association Study ; Genotype ; Haplotypes ; Humans ; Polymorphism, Single Nucleotide ; tau Proteins/genetics
Chemical Substances	MAPT protein, human ; tau Proteins
Language	English
Publishing date	2020-05-13
Publishing country	United States
Document type	Journal Article
ZDB-ID	2211627-8
ISSN	1552-5279 ; 1552-5260
ISSN (online)	1552-5279
ISSN	1552-5260
DOI	10.1002/alz.12099
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Article ; Online: Integrative functional genomic analysis of intron retention in human and mouse brain with Alzheimer's disease.

Alzheimer's & dementia : the journal of the Alzheimer's Association

2021 Volume 17, Issue 6, Page(s) 984–1004

Abstract: Intron retention (IR) has been implicated in the pathogenesis of complex diseases such as cancers; its association with Alzheimer's disease (AD) remains unexplored. We performed genome-wide analysis of IR through integrating genetic, transcriptomic, and ... ...

Abstract	Intron retention (IR) has been implicated in the pathogenesis of complex diseases such as cancers; its association with Alzheimer's disease (AD) remains unexplored. We performed genome-wide analysis of IR through integrating genetic, transcriptomic, and proteomic data of AD subjects and mouse models from the Accelerating Medicines Partnership-Alzheimer's Disease project. We identified 4535 and 4086 IR events in 2173 human and 1736 mouse genes, respectively. Quantitation of IR enabled the identification of differentially expressed genes that conventional exon-level approaches did not reveal. There were significant correlations of intron expression within innate immune genes, like HMBOX1, with AD in humans. Peptides with a high probability of translation from intron-retained mRNAs were identified using mass spectrometry. Further, we established AD-specific intron expression Quantitative Trait Loci, and identified splicing-related genes that may regulate IR. Our analysis provides a novel resource for the search for new AD biomarkers and pathological mechanisms.
MeSH term(s)	Alzheimer Disease/genetics ; Alzheimer Disease/pathology ; Animals ; Autopsy ; Brain/pathology ; Disease Models, Animal ; Genomics ; Homeodomain Proteins/genetics ; Humans ; Introns/genetics ; Mice ; Proteomics ; Quantitative Trait Loci ; Transcriptome
Chemical Substances	Hmbox1 protein, mouse ; Homeodomain Proteins
Language	English
Publishing date	2021-01-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2211627-8
ISSN	1552-5279 ; 1552-5260
ISSN (online)	1552-5279
ISSN	1552-5260
DOI	10.1002/alz.12254
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Article ; Online: Genome-wide transcriptome analysis identifies novel dysregulated genes implicated in Alzheimer's pathology.

Alzheimer's & dementia : the journal of the Alzheimer's Association

2020 Volume 16, Issue 9, Page(s) 1213–1223

Abstract: Introduction: Abnormal gene expression patterns may contribute to the onset and progression of late-onset Alzheimer's disease (LOAD).: Methods: We performed transcriptome-wide meta-analysis (N = 1440) of blood-based microarray gene expression ... ...

Abstract	Introduction: Abnormal gene expression patterns may contribute to the onset and progression of late-onset Alzheimer's disease (LOAD). Methods: We performed transcriptome-wide meta-analysis (N = 1440) of blood-based microarray gene expression profiles as well as neuroimaging and cerebrospinal fluid (CSF) endophenotype analysis. Results: We identified and replicated five genes (CREB5, CD46, TMBIM6, IRAK3, and RPAIN) as significantly dysregulated in LOAD. The most significantly altered gene, CREB5, was also associated with brain atrophy and increased amyloid beta (Aβ) accumulation, especially in the entorhinal cortex region. cis-expression quantitative trait loci mapping analysis of CREB5 detected five significant associations (P < 5 × 10 Discussion: RNA from peripheral blood indicated a differential gene expression pattern in LOAD. Genes identified have been implicated in biological processes relevant to Alzheimer's disease. CREB, in particular, plays a key role in nervous system development, cell survival, plasticity, and learning and memory.
MeSH term(s)	Aged ; Alzheimer Disease/blood ; Alzheimer Disease/genetics ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/cerebrospinal fluid ; Amyloid beta-Peptides/metabolism ; Aniline Compounds ; Atrophy/pathology ; Brain/pathology ; Cyclic AMP Response Element-Binding Protein A/genetics ; Entorhinal Cortex/pathology ; Ethylene Glycols ; Female ; Gene Expression Profiling ; Genotyping Techniques ; Humans ; Male ; Positron-Emission Tomography
Chemical Substances	Amyloid beta-Peptides ; Aniline Compounds ; CREB5 protein, human ; Cyclic AMP Response Element-Binding Protein A ; Ethylene Glycols ; florbetapir (6867Q6IKOD)
Language	English
Publishing date	2020-08-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2211627-8
ISSN	1552-5279 ; 1552-5260
ISSN (online)	1552-5279
ISSN	1552-5260
DOI	10.1002/alz.12092
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