Glucocerebrosidase depletion enhances cell-to-cell transmission of α-synuclein

Eun-Jin Bae, Na-Young Yang, Miyoung Song, Cheol Soon Lee, Jun Sung Lee, Byung Chul Jung, He-Jin Lee, Seokjoong Kim, Eliezer Masliah, Sergio Pablo Sardi and Seung-Jae Lee ()
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Eun-Jin Bae: Konkuk University
Na-Young Yang: Konkuk University
Miyoung Song: Konkuk University
Cheol Soon Lee: School of Medicine, Konkuk University
Jun Sung Lee: Konkuk University
Byung Chul Jung: Konkuk University
He-Jin Lee: School of Medicine, Konkuk University
Seokjoong Kim: ToolGen, Inc., Biotechnology Incubating Center, Seoul National University
Eliezer Masliah: University of California, San Diego
Sergio Pablo Sardi: Genzyme, a Sanofi Company
Seung-Jae Lee: Konkuk University

Nature Communications, 2014, vol. 5, issue 1, 1-11

Abstract: Abstract Deposition of α-synuclein aggregates occurs widely in the central and peripheral nervous systems in Parkinson’s disease (PD). Although recent evidence has suggested that cell-to-cell transmission of α-synuclein aggregates is associated with the progression of PD, the mechanism by which α-synuclein aggregates spread remains undefined. Here, we show that α-synuclein aggregates are transmitted from cell to cell through a cycle involving uptake of external aggregates, co-aggregation with endogenous α-synuclein and exocytosis of the co-aggregates. Moreover, we find that glucocerebrosidase depletion, which has previously been strongly associated with PD and increased cognitive impairment, promotes propagation of α-synuclein aggregates. These studies define how α-synuclein aggregates spread among neuronal cells and may provide an explanation for how glucocerebrosidase mutations increase the risk of developing PD and other synucleinopathies.

Date: 2014
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DOI: 10.1038/ncomms5755

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