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Book ; Online: Amyloid-β

Tanaka, Masashi / Ono, Kenjiro / Saito, Satoshi

Structure, Function, and Pathophysiological Significance in Neurodegenerative Diseases

2023

Keywords	Public health & preventive medicine ; activation phenotypes ; microglia ; neuroinflammation ; immunohistochemistry ; temporal cortex ; Alzheimer's disease ; amyloid ; amyloid β-protein (Aβ) ; mAb158 ; oligomers ; protofibrils ; amyloid aggregation ; supported lipid bilayers ; time-lapse AFM ; molecular dynamics simulation ; alzheimer's disease ; amyloid β ; bryostatin-1 ; ECE1 ; iPS ; nELAV ; neurotoxicity ; oligomer ; protein kinase C ; α-secretase ; APP mutation ; recessive inheritance ; familial Alzheimer's disease ; Aβ oligomers ; amyloid imaging ; microbiota ; bacterial amyloid ; FUBA ; curli ; CsgA ; amyloid beta ; oxidative stress ; supplement ; phosphodiesterase III inhibitor ; cerebral micro-hemorrhage(s) ; cerebral amyloid angiopathy ; amyloid-β protein ; transgenic mice ; NMR ; CD ; Aβ ; β-amyloid peptide ; α/β-discordant ; Dutch-type mutation ; E22Q ; FAD ; Amyloid β ; Polyphenol ; Pro-oxidant ; Alzheimer's Disease ; molecular imaging ; amyloid β-peptides ; islet amyloid polypeptide ; high-speed atomic force microscopy ; amyloid PET ; tau PET ; amyloid precursor protein ; mutation ; cerebellum ; PBB3 ; PiB ; axon ; traditional medicines ; Polygalae Radix ; diosgenin ; naringenin ; kihito ; amyloid-β ; antimicrobial ; antiviral ; antimicrobial peptide ; neurodegenerative disease ; misfolding ; fluorescence microscopy ; FRET ; n/a
Language	English
Size	1 electronic resource (276 pages)
Publisher	MDPI - Multidisciplinary Digital Publishing Institute
Publishing place	Basel
Document type	Book ; Online
Note	English
HBZ-ID	HT030377034
ISBN	9783036567136 ; 3036567135
Database	ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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Book ; Online: Amyloid-β

Tanaka, Masashi / Ono, Kenjiro / Saito, Satoshi

2023

Keywords	Research & information: general ; Biology, life sciences ; activation phenotypes ; microglia ; neuroinflammation ; immunohistochemistry ; temporal cortex ; Alzheimer's disease ; amyloid ; amyloid β-protein (Aβ) ; mAb158 ; oligomers ; protofibrils ; amyloid aggregation ; supported lipid bilayers ; time-lapse AFM ; molecular dynamics simulation ; alzheimer's disease ; amyloid β ; bryostatin-1 ; ECE1 ; iPS ; nELAV ; neurotoxicity ; oligomer ; protein kinase C ; α-secretase ; APP mutation ; recessive inheritance ; familial Alzheimer's disease ; Aβ oligomers ; amyloid imaging ; microbiota ; bacterial amyloid ; FUBA ; curli ; CsgA ; amyloid beta ; oxidative stress ; supplement ; phosphodiesterase III inhibitor ; cerebral micro-hemorrhage(s) ; cerebral amyloid angiopathy ; amyloid-β protein ; transgenic mice ; NMR ; CD ; Aβ ; β-amyloid peptide ; α/β-discordant ; Dutch-type mutation ; E22Q ; FAD ; Amyloid β ; Polyphenol ; Pro-oxidant ; Alzheimer's Disease ; molecular imaging ; amyloid β-peptides ; islet amyloid polypeptide ; high-speed atomic force microscopy ; amyloid PET ; tau PET ; amyloid precursor protein ; mutation ; cerebellum ; PBB3 ; PiB ; axon ; traditional medicines ; Polygalae Radix ; diosgenin ; naringenin ; kihito ; amyloid-β ; antimicrobial ; antiviral ; antimicrobial peptide ; neurodegenerative disease ; misfolding ; fluorescence microscopy ; FRET ; n/a
Language	English
Size	1 electronic resource (276 pages)
Publisher	MDPI - Multidisciplinary Digital Publishing Institute
Publishing place	Basel
Document type	Book ; Online
Note	English
HBZ-ID	HT030374980
ISBN	9783036567136 ; 3036567135
Database	ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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Article: [α-Synuclein as Diagnostic Biomarker].

Ono, Kenjiro

Brain and nerve = Shinkei kenkyu no shinpo

2020 Volume 72, Issue 2, Page(s) 137–141

Abstract: Although α-synuclein protein (αS) undergoes aggregation from a monomer to assemblies, such as oligomers, protofibrils, and mature fibrils, the early intermediate aggregates, that is, oligomers, are considered to be the most toxic species in the ... ...

Abstract	Although α-synuclein protein (αS) undergoes aggregation from a monomer to assemblies, such as oligomers, protofibrils, and mature fibrils, the early intermediate aggregates, that is, oligomers, are considered to be the most toxic species in the pathogenesis of α-synucleinopathies, including Parkinson's disease (PD) and dementia with Lewy bodies (DLB). While it has been reported that the αS concentration in cerebrospinal fluid (CSF) is decreased significantly in patients with PD and DLB, there have been reports of the αS oligomer concentration being elevated in the CSF of patients with PD. Moreover, it is supposed that the αS oligomer concentration is also elevated in the blood of patients with PD. Recently, it has been reported that lower cerebrospinal β-amyloid (Aβ)1-40, Aβ1-42, and αS levels are associated with cognitive decline in PD. Further combination studies of the CSF and blood may lead to the establishment of the candidate αS as a biomarker for α-synucleinopathies, including PD and DLB.
MeSH term(s)	Biomarkers/analysis ; Humans ; Lewy Body Disease/diagnosis ; Parkinson Disease/diagnosis ; alpha-Synuclein/analysis
Chemical Substances	Biomarkers ; alpha-Synuclein
Language	Japanese
Publishing date	2020-01-31
Publishing country	Japan
Document type	Journal Article
ZDB-ID	390389-8
ISSN	1344-8129 ; 1881-6096 ; 0006-8969
ISSN (online)	1344-8129
ISSN	1881-6096 ; 0006-8969
DOI	10.11477/mf.1416201493
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Article ; Online: The Mechanisms of the Roles of α-Synuclein, Amyloid-β, and Tau Protein in the Lewy Body Diseases: Pathogenesis, Early Detection, and Therapeutics.

Noguchi-Shinohara, Moeko / Ono, Kenjiro

International journal of molecular sciences

2023 Volume 24, Issue 12

Abstract: Lewy body diseases (LBD) are pathologically defined as the accumulation of Lewy bodies composed of an aggregation of α-synuclein (αSyn). In LBD, not only the sole aggregation of αSyn but also the co-aggregation of amyloidogenic proteins, such as amyloid- ... ...

Abstract	Lewy body diseases (LBD) are pathologically defined as the accumulation of Lewy bodies composed of an aggregation of α-synuclein (αSyn). In LBD, not only the sole aggregation of αSyn but also the co-aggregation of amyloidogenic proteins, such as amyloid-β (Aβ) and tau, has been reported. In this review, the pathophysiology of co-aggregation of αSyn, Aβ, and tau protein and the advancement in imaging and fluid biomarkers that can detect αSyn and co-occurring Aβ and/or tau pathologies are discussed. Additionally, the αSyn-targeted disease-modifying therapies in clinical trials are summarized.
MeSH term(s)	Humans ; alpha-Synuclein/metabolism ; tau Proteins/metabolism ; Lewy Bodies/metabolism ; Lewy Body Disease/diagnosis ; Lewy Body Disease/therapy ; Lewy Body Disease/metabolism ; Amyloid beta-Peptides/metabolism ; Alzheimer Disease/metabolism
Chemical Substances	alpha-Synuclein ; tau Proteins ; Amyloid beta-Peptides
Language	English
Publishing date	2023-06-17
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms241210215
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Article ; Online: Usefulness of a Scalp Biopsy for Diagnosing Spinal Sarcoidosis.

Mori, Makoto / Komatsu, Junji / Muramatsu, Daiki / Ono, Kenjiro

Internal medicine (Tokyo, Japan)

2024

Language	English
Publishing date	2024-02-26
Publishing country	Japan
Document type	Journal Article
ZDB-ID	32371-8
ISSN	1349-7235 ; 0021-5120 ; 0918-2918
ISSN (online)	1349-7235
ISSN	0021-5120 ; 0918-2918
DOI	10.2169/internalmedicine.3143-23
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Article: [The Roles of Aβ in Alzheimer's Disease: In Light of the Latest Findings].

Ono, Kenjiro / Shiina, Hiroko / Matsumoto, Mariko / Nakamura, Yosuke

Brain and nerve = Shinkei kenkyu no shinpo

2024 Volume 76, Issue 4, Page(s) 399–408

Abstract: The 'amyloid hypothesis', initially put forward in 1992, posits that amyloid β protein (Aβ) contributes to neurodegeneration through aberrant aggregation. In the process of this aberrant aggregation, Aβ forms oligomers, protofibrils, and mature fibrils, ... ...

Abstract	The 'amyloid hypothesis', initially put forward in 1992, posits that amyloid β protein (Aβ) contributes to neurodegeneration through aberrant aggregation. In the process of this aberrant aggregation, Aβ forms oligomers, protofibrils, and mature fibrils, ultimately developing plaques. These mature fibrils and plaques were believed to be the culprits behind the neurotoxicity and neurodegeneration seen in Alzheimer's disease (AD). However, growing evidence in recent years has led to the 'Aβ oligomer hypothesis', which suggests that the intermediate forms of aggregates, such as oligomers and protofibrils, exhibit stronger neurotoxicity than the mature forms. Consequently, efforts have been made to develop anti-Aβ antibody drugs that specifically target these intermediate aggregates. Such interventions hold promise as disease-modifying treatments for AD.
MeSH term(s)	Humans ; Alzheimer Disease ; Amyloid beta-Peptides ; Amyloid/metabolism ; Plaque, Amyloid
Chemical Substances	Amyloid beta-Peptides ; Amyloid
Language	Japanese
Publishing date	2024-04-08
Publishing country	Japan
Document type	English Abstract ; Journal Article
ZDB-ID	390389-8
ISSN	1344-8129 ; 1881-6096 ; 0006-8969
ISSN (online)	1344-8129
ISSN	1881-6096 ; 0006-8969
DOI	10.11477/mf.1416202619
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Zs.A 398: Show issues

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Article ; Online: Corrigendum to 'Acquisition and processing of high-speed atomic force microscopy videos for single amyloid aggregate observation' [Methods (2022), 197, 4-12].

Watanabe-Nakayama, Takahiro / Ono, Kenjiro

Methods (San Diego, Calif.)

2022 Volume 199, Page(s) 80

Language	English
Publishing date	2022-02-04
Publishing country	United States
Document type	Published Erratum
ZDB-ID	1066584-5
ISSN	1095-9130 ; 1046-2023
ISSN (online)	1095-9130
ISSN	1046-2023
DOI	10.1016/j.ymeth.2022.01.010
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Article ; Online: Single-molecule observation of self-propagating amyloid fibrils.

Watanabe-Nakayama, Takahiro / Ono, Kenjiro

Microscopy (Oxford, England)

2022 Volume 71, Issue 3, Page(s) 133–141

Abstract: The assembly of misfolded proteins into amyloid fibrils is associated with amyloidosis, including neurodegenerative diseases such as Alzheimer's, Parkinson's and prion diseases. The self-propagation of amyloid fibrils is widely observed in the ... ...

Abstract	The assembly of misfolded proteins into amyloid fibrils is associated with amyloidosis, including neurodegenerative diseases such as Alzheimer's, Parkinson's and prion diseases. The self-propagation of amyloid fibrils is widely observed in the aggregation pathways of numerous amyloidogenic proteins. This propensity with plasticity in primary nucleation allows amyloid fibril polymorphism, which is correlated with the pathology/phenotypes of patients. Because the interference with the nucleation and replication processes of amyloid fibrils can alter the amyloid structure and the outcome of the disease, these processes can be a target for developing clinical drugs. Single-molecule observations of amyloid fibril replication can be an experimental system to provide the kinetic parameters for simulation studies and confirm the effect of clinical drugs. Here, we review the single-molecule observation of the amyloid fibril replication process using fluorescence microscopy and time-lapse atomic force microscopy, including high-speed atomic force microscopy. We discussed the amyloid fibril replication process and combined single-molecule observation results with molecular dynamics simulations.
MeSH term(s)	Amyloid/chemistry ; Humans ; Kinetics ; Microscopy, Atomic Force ; Microscopy, Fluorescence ; Molecular Dynamics Simulation
Chemical Substances	Amyloid
Language	English
Publishing date	2022-03-07
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2707496-1
ISSN	2050-5701 ; 2050-5698
ISSN (online)	2050-5701
ISSN	2050-5698
DOI	10.1093/jmicro/dfac011
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Article ; Online: Interactions of amyloid coaggregates with biomolecules and its relevance to neurodegeneration.

Murakami, Kazuma / Ono, Kenjiro

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

2022 Volume 36, Issue 9, Page(s) e22493

Abstract: The aggregation of amyloidogenic proteins is a pathological hallmark of various neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis. In these diseases, oligomeric intermediates or toxic ... ...

Abstract	The aggregation of amyloidogenic proteins is a pathological hallmark of various neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis. In these diseases, oligomeric intermediates or toxic aggregates of amyloids cause neuronal damage and degeneration. Despite the substantial effort made over recent decades to implement therapeutic interventions, these neurodegenerative diseases are not yet understood at the molecular level. In many cases, multiple disease-causing amyloids overlap in a sole pathological feature or a sole disease-causing amyloid represents multiple pathological features. Various amyloid pathologies can coexist in the same brain with or without clinical presentation and may even occur in individuals without disease. From sparse data, speculation has arisen regarding the coaggregation of amyloids with disparate amyloid species and other biomolecules, which are the same characteristics that make diagnostics and drug development challenging. However, advances in research related to biomolecular condensates and structural analysis have been used to overcome some of these challenges. Considering the development of these resources and techniques, herein we review the cross-seeding of amyloidosis, for example, involving the amyloids amyloid β, tau, α-synuclein, and human islet amyloid polypeptide, and their cross-inhibition by transthyretin and BRICHOS. The interplay of nucleic acid-binding proteins, such as prions, TAR DNA-binding protein 43, fused in sarcoma/translated in liposarcoma, and fragile X mental retardation polyglycine, with nucleic acids in the pathology of neurodegeneration are also described, and we thereby highlight the potential clinical applications in central nervous system therapy.
MeSH term(s)	Amyloid/metabolism ; Amyloid beta-Peptides ; Amyloidogenic Proteins ; Amyloidosis ; Humans ; Neurodegenerative Diseases/metabolism
Chemical Substances	Amyloid ; Amyloid beta-Peptides ; Amyloidogenic Proteins
Language	English
Publishing date	2022-08-15
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	639186-2
ISSN	1530-6860 ; 0892-6638
ISSN (online)	1530-6860
ISSN	0892-6638
DOI	10.1096/fj.202200235R
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Article ; Online: The Oligomer Hypothesis in α-Synucleinopathy.

Ono, Kenjiro

Neurochemical research

2017 Volume 42, Issue 12, Page(s) 3362–3371

Abstract: Lewy bodies and Lewy neurites in the brain constitute the main histopathological features of Parkinson's disease (PD) and dementia with Lewy bodies. They comprise amyloid-like fibrils composed of α-synuclein (αS), a small protein (~14 kDa). Because the ... ...

Abstract	Lewy bodies and Lewy neurites in the brain constitute the main histopathological features of Parkinson's disease (PD) and dementia with Lewy bodies. They comprise amyloid-like fibrils composed of α-synuclein (αS), a small protein (~14 kDa). Because the aggregation of αS in the brain has been implicated as a critical step in the development of these diseases, the research for disease-modifying drugs has focused on modification of the αS aggregation process in the brain. Recent studies using synthetic αS peptides, a cell culture model, transgenic mice models, and human samples such as cerebrospinal fluids and the blood of PD patients have suggested that pre-fibrillar forms of αS (i.e., oligomers) are more critical than fibrillar forms (such as Lewy bodies) in the pathogenesis of α-synucleinopathies. Based on the accumulating evidence that oligomers play a central role in the pathogenesis of PD and other α-synucleinopathies (the "oligomer hypothesis"). This report reviews the recent findings regarding the oligomer hypothesis in the research of α-synucleinopathies.
MeSH term(s)	Amyloid/metabolism ; Animals ; Brain/metabolism ; Dementia/metabolism ; Disease Models, Animal ; Humans ; Lewy Body Disease/pathology ; Parkinson Disease/metabolism
Chemical Substances	Amyloid
Language	English
Publishing date	2017-12
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	199335-5
ISSN	1573-6903 ; 0364-3190
ISSN (online)	1573-6903
ISSN	0364-3190
DOI	10.1007/s11064-017-2382-x
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