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Article ; Online: A potential protective role of the nuclear receptor-related factor 1 (Nurr1) in multiple sclerosis motor cortex: a neuropathological study.

Pansieri, Jonathan / Pisa, Marco / Yates, Richard L / Esiri, Margaret M / DeLuca, Gabriele C

Brain communications

2023 Volume 5, Issue 2, Page(s) fcad072

Abstract: Cerebral cortical inflammation and neurodegeneration are hallmark pathological features of multiple sclerosis that contribute to irreversible neurological disability. While the reason for nerve cell death is unknown, the pathogenic inflammatory role of ... ...

Abstract	Cerebral cortical inflammation and neurodegeneration are hallmark pathological features of multiple sclerosis that contribute to irreversible neurological disability. While the reason for nerve cell death is unknown, the pathogenic inflammatory role of infiltrating lymphocytes is likely an important contributor. The nuclear receptor-related factor 1 counteracts inflammation in animal models of multiple sclerosis, and protects against neuronal loss in other neurodegenerative disorders, but its expression in post-mortem multiple sclerosis tissue is not known. This study aims to investigate the nuclear receptor-related factor 1 expression in multiple sclerosis motor cortex and evaluate its relationship with motor cortical pathology. To accomplish this, an autopsy cohort of pathologically confirmed multiple sclerosis (
Language	English
Publishing date	2023-03-17
Publishing country	England
Document type	Journal Article
ISSN	2632-1297
ISSN (online)	2632-1297
DOI	10.1093/braincomms/fcad072
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Article: Regional contribution of vascular dysfunction in white matter dementia: clinical and neuropathological insights.

Pansieri, Jonathan / Hadley, Gina / Lockhart, Andrew / Pisa, Marco / DeLuca, Gabriele C

Frontiers in neurology

2023 Volume 14, Page(s) 1199491

Abstract: The maintenance of adequate blood supply and vascular integrity is fundamental to ensure cerebral function. A wide range of studies report vascular dysfunction in white matter dementias, a group of cerebral disorders characterized by substantial white ... ...

Abstract	The maintenance of adequate blood supply and vascular integrity is fundamental to ensure cerebral function. A wide range of studies report vascular dysfunction in white matter dementias, a group of cerebral disorders characterized by substantial white matter damage in the brain leading to cognitive impairment. Despite recent advances in imaging, the contribution of vascular-specific regional alterations in white matter dementia has been not extensively reviewed. First, we present an overview of the main components of the vascular system involved in the maintenance of brain function, modulation of cerebral blood flow and integrity of the blood-brain barrier in the healthy brain and during aging. Second, we review the regional contribution of cerebral blood flow and blood-brain barrier disturbances in the pathogenesis of three distinct conditions: the archetypal white matter predominant neurocognitive dementia that is vascular dementia, a neuroinflammatory predominant disease (multiple sclerosis) and a neurodegenerative predominant disease (Alzheimer's). Finally, we then examine the shared landscape of vascular dysfunction in white matter dementia. By emphasizing the involvement of vascular dysfunction in the white matter, we put forward a hypothetical map of vascular dysfunction during disease-specific progression to guide future research aimed to improve diagnostics and facilitate the development of tailored therapies.
Language	English
Publishing date	2023-06-16
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2564214-5
ISSN	1664-2295
ISSN	1664-2295
DOI	10.3389/fneur.2023.1199491
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Article ; Online: Tuberous sclerosis complex-1 (TSC1) contributes to selective neuronal vulnerability in Alzheimer's disease.

Adriaanse, Bryan A / Brady, Sinead / Wang, Minghui / Beard, Daniel J / Spencer, Jonathan I / Pansieri, Jonathan / Sutherland, Brad A / Esiri, Margaret M / Buchan, Alastair M / Cader, Zameel / Zhang, Bin / DeLuca, Gabriele C

Neuropathology and applied neurobiology

2023 Volume 49, Issue 3, Page(s) e12904

Abstract: Aims: Selective neuronal vulnerability of hippocampal Cornu Ammonis (CA)-1 neurons is a pathological hallmark of Alzheimer's disease (AD) with an unknown underlying mechanism. We interrogated the expression of tuberous sclerosis complex-1 (TSC1; ... ...

Abstract	Aims: Selective neuronal vulnerability of hippocampal Cornu Ammonis (CA)-1 neurons is a pathological hallmark of Alzheimer's disease (AD) with an unknown underlying mechanism. We interrogated the expression of tuberous sclerosis complex-1 (TSC1; hamartin) and mTOR-related proteins in hippocampal CA1 and CA3 subfields. Methods: A human post-mortem cohort of mild (n = 7) and severe (n = 10) AD and non-neurological controls (n = 9) was used for quantitative and semi-quantitative analyses. We also developed an in vitro TSC1 knockdown model in rat hippocampal neurons, and transcriptomic analyses of TSC1 knockdown neuronal cultures were performed. Results: We found a selective increase of TSC1 cytoplasmic inclusions in human AD CA1 neurons with hyperactivation of one of TSC1's downstream targets, the mammalian target of rapamycin complex-1 (mTORC1), suggesting that TSC1 is no longer active in AD. TSC1 knockdown experiments showed accelerated cell death independent of amyloid-beta toxicity. Transcriptomic analyses of TSC1 knockdown neuronal cultures revealed signatures that were significantly enriched for AD-related pathways. Conclusions: Our combined data point to TSC1 dysregulation as a key driver of selective neuronal vulnerability in the AD hippocampus. Future work aimed at identifying targets amenable to therapeutic manipulation is urgently needed to halt selective neurodegeneration, and by extension, debilitating cognitive impairment characteristic of AD.
MeSH term(s)	Humans ; Rats ; Animals ; Alzheimer Disease/pathology ; Tuberous Sclerosis/metabolism ; Hippocampus/pathology ; TOR Serine-Threonine Kinases/metabolism ; Neurons/pathology ; Mammals/metabolism
Chemical Substances	TOR Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2023-04-05
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	80371-6
ISSN	1365-2990 ; 0305-1846
ISSN (online)	1365-2990
ISSN	0305-1846
DOI	10.1111/nan.12904
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Article ; Online: Charge detection mass spectrometry on human-amplified fibrils from different synucleinopathies.

Tsirkou, Aikaterini / Kaczorowski, Flora / Verdurand, Mathieu / Raffoul, Rana / Pansieri, Jonathan / Quadrio, Isabelle / Chauveau, Fabien / Antoine, Rodolphe

Chemical communications (Cambridge, England)

2022 Volume 58, Issue 51, Page(s) 7192–7195

Abstract: Amyloid fibrils are self-assembled mesoscopic protein aggregates, which can accumulate to form deposits or plaques in the brain. ...

Abstract	Amyloid fibrils are self-assembled mesoscopic protein aggregates, which can accumulate to form deposits or plaques in the brain.
MeSH term(s)	Amyloid/chemistry ; Brain/metabolism ; Humans ; Mass Spectrometry ; Parkinson Disease/metabolism ; Protein Aggregates ; Synucleinopathies ; alpha-Synuclein/chemistry
Chemical Substances	Amyloid ; Protein Aggregates ; alpha-Synuclein
Language	English
Publishing date	2022-06-23
Publishing country	England
Document type	Journal Article
ZDB-ID	1472881-3
ISSN	1364-548X ; 1359-7345 ; 0009-241X
ISSN (online)	1364-548X
ISSN	1359-7345 ; 0009-241X
DOI	10.1039/d2cc00200k
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Article ; Online: Residue-specific binding of Ni(II) ions influences the structure and aggregation of amyloid beta (Aβ) peptides.

Berntsson, Elina / Vosough, Faraz / Svantesson, Teodor / Pansieri, Jonathan / Iashchishyn, Igor A / Ostojić, Lucija / Dong, Xiaolin / Paul, Suman / Jarvet, Jüri / Roos, Per M / Barth, Andreas / Morozova-Roche, Ludmilla A / Gräslund, Astrid / Wärmländer, Sebastian K T S

Scientific reports

2023 Volume 13, Issue 1, Page(s) 3341

Abstract: Alzheimer's disease (AD) is the most common cause of dementia worldwide. AD brains display deposits of insoluble amyloid plaques consisting mainly of aggregated amyloid-β (Aβ) peptides, and Aβ oligomers are likely a toxic species in AD pathology. AD ... ...

Abstract	Alzheimer's disease (AD) is the most common cause of dementia worldwide. AD brains display deposits of insoluble amyloid plaques consisting mainly of aggregated amyloid-β (Aβ) peptides, and Aβ oligomers are likely a toxic species in AD pathology. AD patients display altered metal homeostasis, and AD plaques show elevated concentrations of metals such as Cu, Fe, and Zn. Yet, the metal chemistry in AD pathology remains unclear. Ni(II) ions are known to interact with Aβ peptides, but the nature and effects of such interactions are unknown. Here, we use numerous biophysical methods-mainly spectroscopy and imaging techniques-to characterize Aβ/Ni(II) interactions in vitro, for different Aβ variants: Aβ(1-40), Aβ(1-40)(H6A, H13A, H14A), Aβ(4-40), and Aβ(1-42). We show for the first time that Ni(II) ions display specific binding to the N-terminal segment of full-length Aβ monomers. Equimolar amounts of Ni(II) ions retard Aβ aggregation and direct it towards non-structured aggregates. The His6, His13, and His14 residues are implicated as binding ligands, and the Ni(II)·Aβ binding affinity is in the low µM range. The redox-active Ni(II) ions induce formation of dityrosine cross-links via redox chemistry, thereby creating covalent Aβ dimers. In aqueous buffer Ni(II) ions promote formation of beta sheet structure in Aβ monomers, while in a membrane-mimicking environment (SDS micelles) coil-coil helix interactions appear to be induced. For SDS-stabilized Aβ oligomers, Ni(II) ions direct the oligomers towards larger sizes and more diverse (heterogeneous) populations. All of these structural rearrangements may be relevant for the Aβ aggregation processes that are involved in AD brain pathology.
MeSH term(s)	Humans ; Alzheimer Disease ; Amyloid beta-Peptides ; Biophysics ; Brain ; Ions ; Plaque, Amyloid ; Nickel/chemistry
Chemical Substances	Amyloid beta-Peptides ; Ions ; Nickel (7OV03QG267)
Language	English
Publishing date	2023-02-27
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-023-29901-5
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Article ; Online: The influence of HLA-DRB1*15 on the relationship between microglia and neurons in multiple sclerosis normal appearing cortical grey matter.

Yates, Richard L / Pansieri, Jonathan / Li, Qizhu / Bell, Jack S / Yee, Sydney A / Palace, Jacqueline / Esiri, Margaret M / DeLuca, Gabriele C

Brain pathology (Zurich, Switzerland)

2021 Volume 32, Issue 4, Page(s) e13041

Abstract: Cortical tissue injury is common in multiple sclerosis (MS) and associates with disability progression. We have previously shown that HLA-DRB1*15 genotype status associates with the extent of cortical inflammatory pathology. In the current study, we ... ...

Abstract	Cortical tissue injury is common in multiple sclerosis (MS) and associates with disability progression. We have previously shown that HLA-DRB115 genotype status associates with the extent of cortical inflammatory pathology. In the current study, we sought to examine the influence of HLA-DRB115 on relationships between inflammation and neurodegeneration in MS. Human post-mortem MS cases (n = 47) and controls (n = 10) were used. Adjacent sections of motor cortex were stained for microglia (Iba1+, CD68+, TMEM119+), lymphocytes (CD3+, CD8+), GFAP+ astrocytes, and neurons (NeuN+). A subset of MS cases (n = 20) and controls (n = 7) were double-labeled for neurofilament and glutamic acid decarboxylase 65/67 (GAD+) to assess the extent of the inhibitory synaptic loss. In MS cases, microglial protein expression positively correlated with neuron density (Iba1+: r = 0.548, p < 0.001, CD68+: r = 0.498, p = 0.001, TMEM119+ r = 0.437, p = 0.003). This finding was restricted to MS cases not carrying HLA-DRB1*15. Evidence of a 14% reduction in inhibitory synapses in MS was detected (MS: 0.299 ± 0.006 synapses/μm
MeSH term(s)	Gray Matter/pathology ; HLA-DRB1 Chains/genetics ; HLA-DRB1 Chains/metabolism ; Humans ; Inflammation/pathology ; Microglia/pathology ; Multiple Sclerosis/pathology ; Neurons/pathology
Chemical Substances	HLA-DRB1 Chains
Language	English
Publishing date	2021-12-13
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1051484-3
ISSN	1750-3639 ; 1015-6305
ISSN (online)	1750-3639
ISSN	1015-6305
DOI	10.1111/bpa.13041
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Article: Charge detection mass spectrometry on human-amplified fibrils from different synucleinopathies

Tsirkou, Aikaterini / Kaczorowski, Flora / Verdurand, Mathieu / Raffoul, Rana / Pansieri, Jonathan / Quadrio, Isabelle / Chauveau, Fabien / Antoine, Rodolphe

Chemical communications. 2022 June 23, v. 58, no. 51

2022

Abstract: Amyloid fibrils are self-assembled mesoscopic protein aggregates, which can accumulate to form deposits or plaques in the brain. In vitro amplification of fibrils can be achieved with real-time quaking-induced conversion (RT-QuIC). However, this emerging ...

Abstract	Amyloid fibrils are self-assembled mesoscopic protein aggregates, which can accumulate to form deposits or plaques in the brain. In vitro amplification of fibrils can be achieved with real-time quaking-induced conversion (RT-QuIC). However, this emerging technique would benefit from a complementary method to assess structural properties of the amplification products. This work demonstrates the feasibility of nanospray-charge-detection-mass-spectrometry (CDMS) performed on α-synuclein (αSyn) fibrils amplified from human brains with Parkinson's disease (PD) or Dementia with Lewy bodies (DLB) and its synergistic combination with RT-QuIC.
Keywords	Parkinson disease ; amyloid ; brain ; dementia ; genetic techniques and protocols ; humans ; mass spectrometry
Language	English
Dates of publication	2022-0623
Size	p. 7192-7195.
Publishing place	The Royal Society of Chemistry
Document type	Article
ZDB-ID	1472881-3
ISSN	1364-548X ; 1359-7345 ; 0009-241X
ISSN (online)	1364-548X
ISSN	1359-7345 ; 0009-241X
DOI	10.1039/d2cc00200k
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Article ; Online: S100A9 amyloid growth and S100A9 fibril-induced impairment of gamma oscillations in area CA3 of mouse hippocampus ex vivo is prevented by Bri2 BRICHOS.

Andrade-Talavera, Yuniesky / Chen, Gefei / Pansieri, Jonathan / Arroyo-García, Luis Enrique / Toleikis, Zigmantas / Smirnovas, Vytautas / Johansson, Jan / Morozova-Roche, Ludmilla / Fisahn, André

Progress in neurobiology

2022 Volume 219, Page(s) 102366

Abstract: The pro-inflammatory and highly amyloidogenic protein S100A9 is central to the amyloid-neuroinflammatory cascade in neurodegenerative diseases leading to cognitive impairment. Molecular chaperone activity of Bri2 BRICHOS has been demonstrated against a ... ...

Abstract	The pro-inflammatory and highly amyloidogenic protein S100A9 is central to the amyloid-neuroinflammatory cascade in neurodegenerative diseases leading to cognitive impairment. Molecular chaperone activity of Bri2 BRICHOS has been demonstrated against a range of amyloidogenic polypeptides. Using a combination of thioflavin T fluorescence kinetic assay, atomic force microscopy and immuno electron microscopy we show here that recombinant Bri2 BRICHOS effectively inhibits S100A9 amyloid growth by capping amyloid fibrils. Using ex-vivo neuronal network electrophysiology in mouse brain slices we also show that both native S100A9 and amyloids of S100A9 disrupt cognition-relevant gamma oscillation power and rhythmicity in hippocampal area CA3 in a time- and protein conformation-dependent manner. Both effects were associated with Toll-like receptor 4 (TLR4) activation and were not observed upon TLR4 blockade. Importantly, S100A9 that had co-aggregated with Bri2 BRICHOS did not elicit degradation of gamma oscillations. Taken together, this work provides insights on the potential influence of S100A9 on cognitive dysfunction in Alzheimer's disease (AD) via gamma oscillation impairment from experimentally-induced gamma oscillations, and further highlights Bri2 BRICHOS as a chaperone against detrimental effects of amyloid self-assembly.
MeSH term(s)	Animals ; Mice ; Toll-Like Receptor 4/metabolism ; Amyloid/metabolism ; Amyloidogenic Proteins/metabolism ; Alzheimer Disease/metabolism ; Hippocampus/metabolism ; Amyloid beta-Peptides/metabolism ; Calgranulin B/metabolism
Chemical Substances	Toll-Like Receptor 4 ; Amyloid ; Amyloidogenic Proteins ; Amyloid beta-Peptides ; S100A9 protein, mouse ; Calgranulin B
Language	English
Publishing date	2022-10-20
Publishing country	England
Document type	Journal Article
ZDB-ID	185535-9
ISSN	1873-5118 ; 0301-0082
ISSN (online)	1873-5118
ISSN	0301-0082
DOI	10.1016/j.pneurobio.2022.102366
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Article ; Online: Anterior optic pathway pathology in CNS demyelinating diseases.

Pisa, Marco / Pansieri, Jonathan / Yee, Sydney / Ruiz, Jennifer / Leite, Isabel M / Palace, Jacqueline / Comi, Giancarlo / Esiri, Margaret M / Leocani, Letizia / DeLuca, Gabriele C

Brain : a journal of neurology

2022

Abstract: The anterior optic pathway is one of the preferential sites of involvement in CNS inflammatory demyelinating diseases, such as multiple sclerosis and neuromyelitis optica, with optic neuritis being a common presenting symptom. What is more, optic nerve ... ...

Abstract	The anterior optic pathway is one of the preferential sites of involvement in CNS inflammatory demyelinating diseases, such as multiple sclerosis and neuromyelitis optica, with optic neuritis being a common presenting symptom. What is more, optic nerve involvement in these diseases is often subclinical, with optical coherence tomography demonstrating progressive neuroretinal thinning in absence of optic neuritis. The pathological substrate for these findings is poorly understood and requires investigation. We had access to post-mortem tissue samples of optic nerves, chiasms, and tracts from 29 multiple sclerosis (mean age 59.5, range 25-84 years; 73 samples), 6 neuromyelitis optica spectrum disorders (56, 18-84 years; 22 samples), 6 acute disseminated encephalomyelitis (25, 10-39 years; 12 samples) cases and 5 non-neurological controls (55.2, 44-64 years; 16 samples). Formalin-fixed paraffin-embedded samples were immunolabelled for myelin, inflammation (microglial/macrophage, T- and B-cells, complement), acute axonal injury and astrocytes. We assessed the extent and distribution of these markers along the anterior optic pathway for each case in all compartments (i.e. parenchymal, perivascular, and meningeal), where relevant. Demyelinated plaques were classified as active based on established criteria. In multiple sclerosis, demyelination was present in 82.8% of cases of which 75% showed activity. Microglia/macrophage and lymphocyte inflammation were frequently found both in the parenchymal and meningeal compartments in non-demyelinated regions. Acute axonal injury affected 41.4% of cases and correlated with extent of inflammatory activity in each compartment even in cases that died at advanced age with over 20 years of disease duration. An antero-posterior gradient of anterior optic pathway involvement was observed with optic nerves being most severely affected by inflammation and acute axonal injury compared to the optic tract, where a higher proportion of remyelinated plaques were seen. In neuromyelitis optica spectrum disorder, cases with a history of optic neuritis had extensive demyelination and lost aquaporin-4 reactivity. In contrast, those without prior optic neuritis did not have demyelination but rather diffuse microglial/macrophage, T and B-lymphocyte inflammation in both parenchymal and meningeal compartments, and acute axonal injury was present in 75% of cases. Acute demyelinating encephalomyelitis featured intense inflammation, and perivenular demyelination in 33% of cases. Our findings suggest that chronic inflammation is frequent and leads to neurodegeneration in multiple sclerosis and neuromyelitis optica, regardless of disease stage. The chronic inflammation and subsequent neurodegeneration occurring along the optic pathway broadens the plaque-centred view of these diseases and partly explains the progressive neuroretinal changes observed in optic coherence tomography studies.
Language	English
Publishing date	2022-02-03
Publishing country	England
Document type	Journal Article
ZDB-ID	80072-7
ISSN	1460-2156 ; 0006-8950
ISSN (online)	1460-2156
ISSN	0006-8950
DOI	10.1093/brain/awac030
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Article: Chaperones mainly suppress primary nucleation during formation of functional amyloid required for bacterial biofilm formation.

Nagaraj, Madhu / Najarzadeh, Zahra / Pansieri, Jonathan / Biverstål, Henrik / Musteikyte, Greta / Smirnovas, Vytautas / Matthews, Steve / Emanuelsson, Cecilia / Johansson, Janne / Buxbaum, Joel N / Morozova-Roche, Ludmilla / Otzen, Daniel E

Chemical science

2021 Volume 13, Issue 2, Page(s) 536–553

Abstract: Unlike misfolding in neurodegenerative diseases, aggregation of functional amyloids involved in bacterial biofilm, ...

Abstract	Unlike misfolding in neurodegenerative diseases, aggregation of functional amyloids involved in bacterial biofilm,
Language	English
Publishing date	2021-12-13
Publishing country	England
Document type	Journal Article
ZDB-ID	2559110-1
ISSN	2041-6539 ; 2041-6520
ISSN (online)	2041-6539
ISSN	2041-6520
DOI	10.1039/d1sc05790a
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