Electron Microscopic Analysis of α-Synuclein Fibrils.

Amyloid / metabolism Brain / metabolism Disease Progression Humans Microscopy, Electron / methods Microscopy, Immunoelectron / methods Multiple System Atrophy / metabolism Parkinson Disease / metabolism Recombinant Proteins / metabolism alpha-Synuclein / metabolism
Amyloid-like fibrils Dementia with Lewy bodies Immunoelectron microscopy Multiple system atrophy Negative staining Parkinson’s disease α-Synuclein

Journal

Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969

Informations de publication

Date de publication:
2021
Historique:
entrez: 27 5 2021
pubmed: 28 5 2021
medline: 11 8 2021
Statut: ppublish

Résumé

α-Synuclein (α-syn) is a major component of abnormal protein deposits observed in the brains of patients with synucleinopathies, including Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy (MSA). The synaptic protein α-syn is water-soluble under normal physiological conditions, but in these patients' brains, we see accumulation of insoluble amyloid-like α-syn fibrils with prion-like properties. Intracerebral accumulation of these fibrils is correlated with disease onset and progression. Recombinant α-syn protein also forms amyloid-like fibrils that are structurally akin to those extracted from patients' brains. Recent cryo-electron microscopic studies have identified the core structures of synthetic α-syn fibrils and α-syn fibrils extracted from the brains of patients with MSA at the atomic level. In this chapter, we describe negative staining and immunoelectron microscopy protocols for ultrastructural characterization of synthetic α-syn fibrils and pathological α-syn fibrils.

Identifiants

DOI: 10.1007/978-1-0716-1495-2_2 PMID: 34043188
pubmed: 34043188
doi: 10.1007/978-1-0716-1495-2_2
doi:

Substances chimiques

Amyloid 0
Recombinant Proteins 0
alpha-Synuclein 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

17-25

Références

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Auteurs

Airi Tarutani (A)

Department of Brain and Neurosciences, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
Laboratory of Neuropathology and Neuroscience, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.

Masato Hasegawa (M)

Department of Brain and Neurosciences, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan. hasegawa-ms@igakuken.or.jp.

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Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Amyloïde › Electron Microscopic Analysis of α-Synuclein Fibrils.
questionsmedicales.fr › Système nerveux › Système nerveux central › Encéphale › Electron Microscopic Analysis of α-Synuclein Fibrils.
questionsmedicales.fr › États, signes et symptômes pathologiques › Processus pathologiques › Caractéristiques de la maladie › Évolution de la maladie › Electron Microscopic Analysis of α-Synuclein Fibrils.
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Electron Microscopic Analysis of α-Synuclein Fibrils.
questionsmedicales.fr › Techniques d'investigation › Microscopie électronique › Electron Microscopic Analysis of α-Synuclein Fibrils.
questionsmedicales.fr › Techniques d'investigation › Microscopie électronique › Microscopie immunoélectronique › Electron Microscopic Analysis of α-Synuclein Fibrils.
questionsmedicales.fr › Maladies du système nerveux › Maladies neurodégénératives › Atrophie multisystématisée › Electron Microscopic Analysis of α-Synuclein Fibrils.
questionsmedicales.fr › Maladies du système nerveux › Maladies neurodégénératives › Maladie de Parkinson › Electron Microscopic Analysis of α-Synuclein Fibrils.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines recombinantes › Electron Microscopic Analysis of α-Synuclein Fibrils.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines associées à la maladie de Parkinson › alpha-Synucléine › Electron Microscopic Analysis of α-Synuclein Fibrils.