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Article ; Online: Amyloidosis by Bacterial Infection in Critically Ill Patients?

Eisele, Yvonne S

American journal of respiratory and critical care medicine

2018 Volume 198, Issue 12, Page(s) 1475–1476

MeSH term(s)	Amyloidosis ; Anti-Bacterial Agents ; Bacterial Infections ; Critical Illness ; Cross Infection ; Humans ; Pneumonia
Chemical Substances	Anti-Bacterial Agents
Language	English
Publishing date	2018-10-15
Publishing country	United States
Document type	Editorial ; Comment
ZDB-ID	1180953-x
ISSN	1535-4970 ; 0003-0805 ; 1073-449X
ISSN (online)	1535-4970
ISSN	0003-0805 ; 1073-449X
DOI	10.1164/rccm.201809-1777ED
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Article ; Online: From soluble aβ to progressive aβ aggregation: could prion-like templated misfolding play a role?

Eisele, Yvonne S

Brain pathology (Zurich, Switzerland)

2013 Volume 23, Issue 3, Page(s) 333–341

Abstract: ... of individuals affected by Alzheimer's disease (AD) or by cerebral β-amyloid angiopathy (Aβ-CAA). While Aβ is ...

Abstract	Accumulation, aggregation and deposition of Aβ peptides are pathological hallmarks in the brains of individuals affected by Alzheimer's disease (AD) or by cerebral β-amyloid angiopathy (Aβ-CAA). While Aβ is a peptide of yet largely unknown function, it is constantly produced in the human brain where it normally remains in a soluble state. However, Aβ peptides are aggregation prone by their intrinsic ability to adopt alternative conformations rich in β-sheet structure that aggregate into oligomeric as well as fibrillar formations. This transition from soluble to aggregated state has been hypothesized to initiate the pathological cascade and is therefore subject to intensive research. Mounting evidence suggests prion-like templated misfolding as the biochemical phenomenon responsible for promoting progressive Aβ aggregation. Here, we review studies in vitro and in vivo that suggest that cerebral Aβ aggregation may indeed progress via prion-like templated misfolding. The implications of these findings are discussed with respect to understanding initiation and progression of the disease and to developing therapeutics.
MeSH term(s)	Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/chemistry ; Humans ; Prion Diseases/metabolism ; Prion Diseases/pathology ; Protein Structure, Secondary ; Proteostasis Deficiencies/metabolism ; Proteostasis Deficiencies/pathology
Chemical Substances	Amyloid beta-Peptides
Language	English
Publishing date	2013-04-15
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1051484-3
ISSN	1750-3639 ; 1015-6305
ISSN (online)	1750-3639
ISSN	1015-6305
DOI	10.1111/bpa.12049
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Article ; Online: Molecular Imaging of Cardiac Amyloidosis.

Masri, Ahmad / Bukhari, Syed / Eisele, Yvonne S / Soman, Prem

Journal of nuclear medicine : official publication, Society of Nuclear Medicine

2020 Volume 61, Issue 7, Page(s) 965–970

Abstract: Transthyretin and light-chain amyloidosis are the 2 main causes of cardiac amyloidosis. Recent developments in molecular imaging have transformed our ability to diagnose transthyretin cardiac amyloidosis noninvasively and unmasked a hitherto unrecognized ...

Abstract	Transthyretin and light-chain amyloidosis are the 2 main causes of cardiac amyloidosis. Recent developments in molecular imaging have transformed our ability to diagnose transthyretin cardiac amyloidosis noninvasively and unmasked a hitherto unrecognized prevalence of the disease. This review summarizes the current and evolving imaging approaches, their molecular structural basis, and the gaps in imaging capabilities that have arisen as a result of parallel developments in pharmacotherapy delivering the first effective treatment options for this condition.
MeSH term(s)	Amyloidosis/diagnostic imaging ; Cardiomyopathies/diagnostic imaging ; Humans ; Molecular Imaging/methods
Language	English
Publishing date	2020-06-01
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	80272-4
ISSN	1535-5667 ; 0097-9058 ; 0161-5505 ; 0022-3123
ISSN (online)	1535-5667
ISSN	0097-9058 ; 0161-5505 ; 0022-3123
DOI	10.2967/jnumed.120.245381
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Article ; Online: Prevalence of Atrial Fibrillation and Thromboembolic Risk in Wild-Type Transthyretin Amyloid Cardiomyopathy.

Bukhari, Syed / Barakat, Amr F / Eisele, Yvonne S / Nieves, Ricardo / Jain, Sandeep / Saba, Samir / Follansbee, William P / Brownell, Amy / Soman, Prem

Circulation

2021 Volume 143, Issue 13, Page(s) 1335–1337

MeSH term(s)	Aged ; Amyloid Neuropathies, Familial/complications ; Amyloid Neuropathies, Familial/physiopathology ; Atrial Fibrillation/diagnosis ; Atrial Fibrillation/pathology ; Cardiomyopathies/classification ; Cardiomyopathies/physiopathology ; Female ; Humans ; Male ; Prevalence ; Retrospective Studies ; Risk Factors ; Thromboembolism
Language	English
Publishing date	2021-03-29
Publishing country	United States
Document type	Letter ; Research Support, Non-U.S. Gov't
ZDB-ID	80099-5
ISSN	1524-4539 ; 0009-7322 ; 0069-4193 ; 0065-8499
ISSN (online)	1524-4539
ISSN	0009-7322 ; 0069-4193 ; 0065-8499
DOI	10.1161/CIRCULATIONAHA.120.052136
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Article ; Online: Propagation of Aß pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies.

Eisele, Yvonne S / Duyckaerts, Charles

Acta neuropathologica

2016 Volume 131, Issue 1, Page(s) 5–25

Abstract: In brains of patients with Alzheimer's disease (AD), Aβ peptides accumulate in parenchyma and ...

Abstract	In brains of patients with Alzheimer's disease (AD), Aβ peptides accumulate in parenchyma and, almost invariably, also in the vascular walls. Although Aβ aggregation is, by definition, present in AD, its impact is only incompletely understood. It occurs in a stereotypical spatiotemporal distribution within neuronal networks in the course of the disease. This suggests a role for synaptic connections in propagating Aβ pathology, and possibly of axonal transport in an antero- or retrograde way-although, there is also evidence for passive, extracellular diffusion. Striking, in AD, is the conjunction of tau and Aβ pathology. Tau pathology in the cell body of neurons precedes Aβ deposition in their synaptic endings in several circuits such as the entorhino-dentate, cortico-striatal or subiculo-mammillary connections. However, genetic evidence suggests that Aβ accumulation is the first step in AD pathogenesis. To model the complexity and consequences of Aβ aggregation in vivo, various transgenic (tg) rodents have been generated. In rodents tg for the human Aβ precursor protein, focal injections of preformed Aβ aggregates can induce Aβ deposits in the vicinity of the injection site, and over time in more distant regions of the brain. This suggests that Aβ shares with α-synuclein, tau and other proteins the property to misfold and aggregate homotypic molecules. We propose to group those proteins under the term "propagons". Propagons may lack the infectivity of prions. We review findings from neuropathological examinations of human brains in different stages of AD and from studies in rodent models of Aβ aggregation and discuss putative mechanisms underlying the initiation and spread of Aβ pathology.
MeSH term(s)	Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Brain/metabolism ; Brain/pathology ; Disease Models, Animal ; Humans ; tau Proteins/metabolism
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; tau Proteins
Language	English
Publishing date	2016-01
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1079-0
ISSN	1432-0533 ; 0001-6322
ISSN (online)	1432-0533
ISSN	0001-6322
DOI	10.1007/s00401-015-1516-y
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Article ; Online: α-Synuclein Oligomers Induce Glutamate Release from Astrocytes and Excessive Extrasynaptic NMDAR Activity in Neurons, Thus Contributing to Synapse Loss.

Trudler, Dorit / Sanz-Blasco, Sara / Eisele, Yvonne S / Ghatak, Swagata / Bodhinathan, Karthik / Akhtar, Mohd Waseem / Lynch, William P / Piña-Crespo, Juan C / Talantova, Maria / Kelly, Jeffery W / Lipton, Stuart A

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

2021 Volume 41, Issue 10, Page(s) 2264–2273

Abstract: Synaptic and neuronal loss are major neuropathological characteristics of Parkinson's ... Lewy body dementia, Alzheimer's disease, and frontotemporal dementia. However, the effects of αSyn and its mechanism ...

Abstract	Synaptic and neuronal loss are major neuropathological characteristics of Parkinson's disease. Misfolded protein aggregates in the form of Lewy bodies, comprised mainly of α-synuclein (αSyn), are associated with disease progression, and have also been linked to other neurodegenerative diseases, including Lewy body dementia, Alzheimer's disease, and frontotemporal dementia. However, the effects of αSyn and its mechanism of synaptic damage remain incompletely understood. Here, we show that αSyn oligomers induce Ca
MeSH term(s)	Animals ; Astrocytes/drug effects ; Astrocytes/metabolism ; Astrocytes/pathology ; Cells, Cultured ; Female ; Glutamic Acid/metabolism ; Hippocampus/metabolism ; Hippocampus/pathology ; Humans ; Induced Pluripotent Stem Cells/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology ; Neurons/drug effects ; Neurons/metabolism ; Neurons/pathology ; Rats ; Rats, Sprague-Dawley ; Receptors, N-Methyl-D-Aspartate/antagonists & inhibitors ; Receptors, N-Methyl-D-Aspartate/metabolism ; Synapses/metabolism ; Synapses/pathology ; alpha-Synuclein/metabolism ; alpha-Synuclein/pharmacology
Chemical Substances	Receptors, N-Methyl-D-Aspartate ; alpha-Synuclein ; Glutamic Acid (3KX376GY7L)
Language	English
Publishing date	2021-01-22
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.1871-20.2020
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Article ; Online: Efficient 1-Hour Technetium-99 m Pyrophosphate Imaging Protocol for the Diagnosis of Transthyretin Cardiac Amyloidosis.

Masri, Ahmad / Bukhari, Syed / Ahmad, Shahzad / Nieves, Ricardo / Eisele, Yvonne S / Follansbee, William / Brownell, Amy / Wong, Timothy C / Schelbert, Erik / Soman, Prem

Circulation. Cardiovascular imaging

2020 Volume 13, Issue 2, Page(s) e010249

Abstract: Background: Technetium-99 m pyrophosphate protocols for transthyretin cardiac amyloidosis diagnosis have variably used 1- and 3-hour imaging time points. We investigated whether imaging at 1 hour with superior efficiency had comparable diagnostic ... ...

Abstract	Background: Technetium-99 m pyrophosphate protocols for transthyretin cardiac amyloidosis diagnosis have variably used 1- and 3-hour imaging time points. We investigated whether imaging at 1 hour with superior efficiency had comparable diagnostic accuracy as 3-hour imaging. Methods: This is a registry analysis of patients with suspected transthyretin cardiac amyloidosis referred for technetium-99 m pyrophosphate at a single tertiary center from June 2015 through January 2019. Patients underwent planar and single-photon emission computed tomography (SPECT) imaging at 1 and 3 hours. A positive Tc-99m pyrophosphate study was defined by the presence of diffuse myocardial tracer uptake on SPECT. For planar imaging, visual semiquantitative (grades 0-3, ≥2 considered positive) and quantitative heart to contralateral ratios (≥1.5 considered positive) were used. Results: Two hundred thirty-three patients (69% men; median age, 77 [69-83] years) underwent the study protocol. There were 60 (25.8%) patients with diffuse myocardial uptake, 1 (0.4%) with regional uptake, and 172 (73.8%) with no myocardial uptake. Results of SPECT were identical at 1 and 3 hours. Planar imaging at 1 hour had 98% sensitivity and 96% specificity. Planar grade 0 uptake or heart to contralateral ratio ≤1.2 and planar grade 3 uptake or heart to contralateral ratio ≥2.0 were always associated with negative and positive SPECT, respectively. For planar grades 1 and 2 uptake and heart to contralateral ratio 1.3 to 1.9, SPECT was needed to make a diagnosis. No patient with light-chain cardiac amyloidosis had positive SPECT. Conclusions: An efficient 1-hour technetium-99 m pyrophosphate protocol had comparable diagnostic performance to a 3-hour protocol.
MeSH term(s)	Aged ; Aged, 80 and over ; Amyloid Neuropathies, Familial/diagnosis ; Cardiomyopathies/diagnosis ; Diagnosis, Differential ; Female ; Follow-Up Studies ; Humans ; Male ; Radiopharmaceuticals/pharmacology ; Reproducibility of Results ; Retrospective Studies ; Technetium Tc 99m Pyrophosphate/pharmacology ; Time Factors ; Tomography, Emission-Computed, Single-Photon/methods
Chemical Substances	Radiopharmaceuticals ; Technetium Tc 99m Pyrophosphate (5L76I61H2B)
Language	English
Publishing date	2020-02-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2435045-X
ISSN	1942-0080 ; 1941-9651
ISSN (online)	1942-0080
ISSN	1941-9651
DOI	10.1161/CIRCIMAGING.119.010249
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Article ; Online: Soluble α-synuclein-antibody complexes activate the NLRP3 inflammasome in hiPSC-derived microglia.

Trudler, Dorit / Nazor, Kristopher L / Eisele, Yvonne S / Grabauskas, Titas / Dolatabadi, Nima / Parker, James / Sultan, Abdullah / Zhong, Zhenyu / Goodwin, Marshall S / Levites, Yona / Golde, Todd E / Kelly, Jeffery W / Sierks, Michael R / Schork, Nicholas J / Karin, Michael / Ambasudhan, Rajesh / Lipton, Stuart A

Proceedings of the National Academy of Sciences of the United States of America

2021 Volume 118, Issue 15

Abstract: Parkinson's disease is characterized by accumulation of α-synuclein (αSyn). Release of oligomeric ...

Abstract	Parkinson's disease is characterized by accumulation of α-synuclein (αSyn). Release of oligomeric/fibrillar αSyn from damaged neurons may potentiate neuronal death in part via microglial activation. Heretofore, it remained unknown if oligomeric/fibrillar αSyn could activate the nucleotide-binding oligomerization domain (NOD)-like receptor (NLR) family pyrin domain-containing 3 (NLRP3) inflammasome in human microglia and whether anti-αSyn antibodies could prevent this effect. Here, we show that αSyn activates the NLRP3 inflammasome in human induced pluripotent stem cell (hiPSC)-derived microglia (hiMG) via dual stimulation involving Toll-like receptor 2 (TLR2) engagement and mitochondrial damage. In vitro, hiMG can be activated by mutant (A53T) αSyn secreted from hiPSC-derived A9-dopaminergic neurons. Surprisingly, αSyn-antibody complexes enhanced rather than suppressed inflammasome-mediated interleukin-1β (IL-1β) secretion, indicating these complexes are neuroinflammatory in a human context. A further increase in inflammation was observed with addition of oligomerized amyloid-β peptide (Aβ) and its cognate antibody. In vivo, engraftment of hiMG with αSyn in humanized mouse brain resulted in caspase-1 activation and neurotoxicity, which was exacerbated by αSyn antibody. These findings may have important implications for antibody therapies aimed at depleting misfolded/aggregated proteins from the human brain, as they may paradoxically trigger inflammation in human microglia.
MeSH term(s)	Amyloid beta-Peptides/immunology ; Antibodies/immunology ; Cell Differentiation ; Cells, Cultured ; Humans ; Induced Pluripotent Stem Cells/cytology ; Inflammasomes/metabolism ; Microglia/cytology ; Microglia/immunology ; NLR Family, Pyrin Domain-Containing 3 Protein/metabolism ; Parkinson Disease/immunology ; Toll-Like Receptor 2/metabolism ; alpha-Synuclein/genetics ; alpha-Synuclein/immunology
Chemical Substances	Amyloid beta-Peptides ; Antibodies ; Inflammasomes ; NLR Family, Pyrin Domain-Containing 3 Protein ; NLRP3 protein, human ; TLR2 protein, human ; Toll-Like Receptor 2 ; alpha-Synuclein
Language	English
Publishing date	2021-04-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2025847118
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Article ; Online: Prominent microglial inclusions in transgenic mouse models of α-synucleinopathy that are distinct from neuronal lesions.

Tanriöver, Gaye / Bacioglu, Mehtap / Schweighauser, Manuel / Mahler, Jasmin / Wegenast-Braun, Bettina M / Skodras, Angelos / Obermüller, Ulrike / Barth, Melanie / Kronenberg-Versteeg, Deborah / Nilsson, K Peter R / Shimshek, Derya R / Kahle, Philipp J / Eisele, Yvonne S / Jucker, Mathias

Acta neuropathologica communications

2020 Volume 8, Issue 1, Page(s) 133

Abstract: ... for Thioflavin S and showed immunoreactivity with antibodies recognizing the N-terminus of αS, but were largely p ...

Abstract	Alpha-synucleinopathies are a group of progressive neurodegenerative disorders, characterized by intracellular deposits of aggregated α-synuclein (αS). The clinical heterogeneity of these diseases is thought to be attributed to conformers (or strains) of αS but the contribution of inclusions in various cell types is unclear. The aim of the present work was to study αS conformers among different transgenic (TG) mouse models of α-synucleinopathies. To this end, four different TG mouse models were studied (Prnp-h[A53T]αS; Thy1-h[A53T]αS; Thy1-h[A30P]αS; Thy1-mαS) that overexpress human or murine αS and differed in their age-of-symptom onset and subsequent disease progression. Postmortem analysis of end-stage brains revealed robust neuronal αS pathology as evidenced by accumulation of αS serine 129 (p-αS) phosphorylation in the brainstem of all four TG mouse lines. Overall appearance of the pathology was similar and only modest differences were observed among additionally affected brain regions. To study αS conformers in these mice, we used pentameric formyl thiophene acetic acid (pFTAA), a fluorescent dye with amyloid conformation-dependent spectral properties. Unexpectedly, besides the neuronal αS pathology, we also found abundant pFTAA-positive inclusions in microglia of all four TG mouse lines. These microglial inclusions were also positive for Thioflavin S and showed immunoreactivity with antibodies recognizing the N-terminus of αS, but were largely p-αS-negative. In all four lines, spectral pFTAA analysis revealed conformational differences between microglia and neuronal inclusions but not among the different mouse models. Concomitant with neuronal lesions, microglial inclusions were already present at presymptomatic stages and could also be induced by seeded αS aggregation. Although nature and significance of microglial inclusions for human α-synucleinopathies remain to be clarified, the previously overlooked abundance of microglial inclusions in TG mouse models of α-synucleinopathy bears importance for mechanistic and preclinical-translational studies.
MeSH term(s)	Animals ; Disease Models, Animal ; Humans ; Inclusion Bodies/pathology ; Mice ; Mice, Transgenic ; Microglia/pathology ; Neurons/pathology ; Protein Aggregation, Pathological/genetics ; Protein Aggregation, Pathological/metabolism ; Protein Aggregation, Pathological/pathology ; Protein Conformation ; Synucleinopathies/genetics ; Synucleinopathies/pathology ; alpha-Synuclein/chemistry ; alpha-Synuclein/genetics ; alpha-Synuclein/metabolism
Chemical Substances	alpha-Synuclein
Language	English
Publishing date	2020-08-12
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2715589-4
ISSN	2051-5960 ; 2051-5960
ISSN (online)	2051-5960
ISSN	2051-5960
DOI	10.1186/s40478-020-00993-8
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Article ; Online: Formaldehyde-fixed brain tissue from spontaneously ill α-synuclein transgenic mice induces fatal α-synucleinopathy in transgenic hosts.

Schweighauser, Manuel / Bacioglu, Mehtap / Fritschi, Sarah K / Shimshek, Derya R / Kahle, Philipp J / Eisele, Yvonne S / Jucker, Mathias

Acta neuropathologica

2015 Volume 129, Issue 1, Page(s) 157–159

MeSH term(s)	Animals ; Brain Stem/pathology ; Brain Stem/physiopathology ; Dentate Gyrus/pathology ; Dentate Gyrus/physiopathology ; Female ; Formaldehyde ; Immunoblotting ; Immunohistochemistry ; Mice, Transgenic ; Neurodegenerative Diseases/pathology ; Neurodegenerative Diseases/physiopathology ; Proteostasis Deficiencies/pathology ; Proteostasis Deficiencies/physiopathology ; Survival Analysis ; Tissue Extracts ; Tissue Fixation ; alpha-Synuclein/genetics ; alpha-Synuclein/metabolism
Chemical Substances	SNCA protein, human ; Snca protein, mouse ; Tissue Extracts ; alpha-Synuclein ; Formaldehyde (1HG84L3525)
Language	English
Publishing date	2015-01
Publishing country	Germany
Document type	Letter
ZDB-ID	1079-0
ISSN	1432-0533 ; 0001-6322
ISSN (online)	1432-0533
ISSN	0001-6322
DOI	10.1007/s00401-014-1360-5
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