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  Glycation potentiates alpha-synuclein-associated neurodegeneration in synucleinopathies.

Vincente Miranda, H., Szego, E. M., Oliveira, L. M., Breda, C., Darendelioglu, E., de Oliveira, R. M., et al. (2017). Glycation potentiates alpha-synuclein-associated neurodegeneration in synucleinopathies. Brain, 140(5), 1399-1419. doi:10.1093/brain/awx056.

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Vincente Miranda, H., Autor
Szego, E. M., Autor
Oliveira, L. M., Autor
Breda, C., Autor
Darendelioglu, E., Autor
de Oliveira, R. M., Autor
Ferreira, D. G., Autor
Gomes, M. A., Autor
Rott, R., Autor
Oliveira, M., Autor
Munari, F., Autor
Enguita, F. J., Autor
Simoes, T., Autor
Rodrigues, E. F., Autor
Heinrich, M., Autor
Martins, I. C., Autor
Zamolo, I., Autor
Riess, O., Autor
Cordeiro, C., Autor
Ponces-Freire, A., Autor
Lashuel, H. A., AutorSantos, N. C., AutorLopes, L. V., AutorXiang, W., AutorJovin, T. M.1, Autor           Penque, D., AutorEngelender, S., AutorZweckstetter, M.2, Autor           Klucken, J., AutorGiorgini, F., AutorQuintas, A., AutorOuteiro, T. F., Autor mehr..
Affiliations:
1Emeritus Group Laboratory of Cellular Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_578629              
2Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

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Schlagwörter: glycation, Parkinson’s disease, neurodegeneration, alpha-synuclein
 Zusammenfassung: α-Synuclein misfolding and aggregation is a hallmark in Parkinson's disease and in several other neurodegenerative diseases known as synucleinopathies. The toxic properties of α-synuclein are conserved from yeast to man, but the precise underpinnings of the cellular pathologies associated are still elusive, complicating the development of effective therapeutic strategies. Combining molecular genetics with target-based approaches, we established that glycation, an unavoidable age-associated post-translational modification, enhanced α-synuclein toxicity in vitro and in vivo, in Drosophila and in mice. Glycation affected primarily the N-terminal region of α-synuclein, reducing membrane binding, impaired the clearance of α-synuclein, and promoted the accumulation of toxic oligomers that impaired neuronal synaptic transmission. Strikingly, using glycation inhibitors, we demonstrated that normal clearance of α-synuclein was re-established, aggregation was reduced, and motor phenotypes in Drosophila were alleviated. Altogether, our study demonstrates glycation constitutes a novel drug target that can be explored in synucleinopathies as well as in other neurodegenerative conditions.

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Sprache(n): eng - English
 Datum: 2017-04-102017-05
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1093/brain/awx056
 Art des Abschluß: -

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Titel: Brain
Genre der Quelle: Zeitschrift
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Seiten: - Band / Heft: 140 (5) Artikelnummer: - Start- / Endseite: 1399 - 1419 Identifikator: -