Effect of the micro-environment on α-synuclein conversion and implication in seeded conversion assays.


Journal

Translational neurodegeneration
ISSN: 2047-9158
Titre abrégé: Transl Neurodegener
Pays: England
ID NLM: 101591861

Informations de publication

Date de publication:
2020
Historique:
received: 04 09 2019
accepted: 23 12 2019
entrez: 29 1 2020
pubmed: 29 1 2020
medline: 29 1 2020
Statut: epublish

Résumé

α-Synuclein is a small soluble protein, whose physiological function in the healthy brain is poorly understood. Intracellular inclusions of α-synuclein, referred to as Lewy bodies (LBs), are pathological hallmarks of α-synucleinopathies, such as Parkinson's disease (PD) or dementia with Lewy bodies (DLB). Understanding of the molecular basis as well as the factors or conditions promoting α-synuclein misfolding and aggregation is an important step towards the comprehension of pathological mechanism of α-synucleinopathies and for the development of efficient therapeutic strategies. Based on the conversion and aggregation mechanism of α-synuclein, novel diagnostic tests, such as protein misfolding seeded conversion assays, e.g. the real-time quaking-induced conversion (RT-QuIC), had been developed. In diagnostics, α-synuclein RT-QuIC exhibits a specificity between 82 and 100% while the sensitivity varies between 70 and 100% among different laboratories. In addition, the α-synuclein RT-QuIC can be used to study the α-synuclein-seeding-characteristics of different α-synucleinopathies and to differentiate between DLB and PD. The variable diagnostic accuracy of current α-synuclein RT-QuIC occurs due to different protocols, cohorts and material etc.. An impact of micro-environmental factors on the α-synuclein aggregation and conversion process and the occurrence and detection of differential misfolded α-synuclein types or strains might underpin the clinical heterogeneity of α-synucleinopathies

Sections du résumé

Background
α-Synuclein is a small soluble protein, whose physiological function in the healthy brain is poorly understood. Intracellular inclusions of α-synuclein, referred to as Lewy bodies (LBs), are pathological hallmarks of α-synucleinopathies, such as Parkinson's disease (PD) or dementia with Lewy bodies (DLB).
Main body
Understanding of the molecular basis as well as the factors or conditions promoting α-synuclein misfolding and aggregation is an important step towards the comprehension of pathological mechanism of α-synucleinopathies and for the development of efficient therapeutic strategies. Based on the conversion and aggregation mechanism of α-synuclein, novel diagnostic tests, such as protein misfolding seeded conversion assays, e.g. the real-time quaking-induced conversion (RT-QuIC), had been developed. In diagnostics, α-synuclein RT-QuIC exhibits a specificity between 82 and 100% while the sensitivity varies between 70 and 100% among different laboratories. In addition, the α-synuclein RT-QuIC can be used to study the α-synuclein-seeding-characteristics of different α-synucleinopathies and to differentiate between DLB and PD.
Conclusion
The variable diagnostic accuracy of current α-synuclein RT-QuIC occurs due to different protocols, cohorts and material etc.. An impact of micro-environmental factors on the α-synuclein aggregation and conversion process and the occurrence and detection of differential misfolded α-synuclein types or strains might underpin the clinical heterogeneity of α-synucleinopathies

Identifiants

pubmed: 31988747
doi: 10.1186/s40035-019-0181-9
pii: 181
pmc: PMC6966864
doi:

Substances chimiques

SNCA protein, human 0
alpha-Synuclein 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't Review

Langues

eng

Pagination

5

Informations de copyright

© The Author(s). 2020.

Déclaration de conflit d'intérêts

Competing interestsThe authors declare that they have no competing interests.

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Auteurs

Niccolo Candelise (N)

1Department of Neurology, University Medicine Goettingen and the German Center for Neurodegenerative Diseases (DZNE), Robert-Koch -Straße 40, 37075 Göttingen, Germany.
3Department of Experimental, Diagnostic and Speciality Medicine, University of Bologna, Bologna, Italy.

Matthias Schmitz (M)

1Department of Neurology, University Medicine Goettingen and the German Center for Neurodegenerative Diseases (DZNE), Robert-Koch -Straße 40, 37075 Göttingen, Germany.

Katrin Thüne (K)

1Department of Neurology, University Medicine Goettingen and the German Center for Neurodegenerative Diseases (DZNE), Robert-Koch -Straße 40, 37075 Göttingen, Germany.

Maria Cramm (M)

1Department of Neurology, University Medicine Goettingen and the German Center for Neurodegenerative Diseases (DZNE), Robert-Koch -Straße 40, 37075 Göttingen, Germany.

Alberto Rabano (A)

4Departamento de Neuropatología y Banco de Tejidos (BT-CIEN), Fundación CIEN, Instituto de Salud Carlos III Centro Alzheimer Fundación Reina Sofíac, Valderrebollo n° 5, 28031 Madrid, Spain.

Saima Zafar (S)

1Department of Neurology, University Medicine Goettingen and the German Center for Neurodegenerative Diseases (DZNE), Robert-Koch -Straße 40, 37075 Göttingen, Germany.
2Biomedical Engineering and Sciences Department, School of Mechanical and Manufacturing Engineering (SMME), National University of Sciences and Technology (NUST), Islamabad, Pakistan.

Erik Stoops (E)

ADx NeuroSciences, Technologiepark 4, Ghent, Belgium.

Hugo Vanderstichele (H)

ADx NeuroSciences, Technologiepark 4, Ghent, Belgium.

Anna Villar-Pique (A)

1Department of Neurology, University Medicine Goettingen and the German Center for Neurodegenerative Diseases (DZNE), Robert-Koch -Straße 40, 37075 Göttingen, Germany.
6CIBERNED (Network center for biomedical research of neurodegenerative diseases), Institute Carlos III, Madrid, Spain.

Franc Llorens (F)

1Department of Neurology, University Medicine Goettingen and the German Center for Neurodegenerative Diseases (DZNE), Robert-Koch -Straße 40, 37075 Göttingen, Germany.
6CIBERNED (Network center for biomedical research of neurodegenerative diseases), Institute Carlos III, Madrid, Spain.
7Bellvitge Biomedical Research Institute (IDIBELL), Hospitalet de Llobregat, Barcelona, Spain.

Inga Zerr (I)

1Department of Neurology, University Medicine Goettingen and the German Center for Neurodegenerative Diseases (DZNE), Robert-Koch -Straße 40, 37075 Göttingen, Germany.

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