Binding of α-synuclein oligomers to Cx32 facilitates protein uptake and transfer in neurons and oligodendrocytes. View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2019-04-11

AUTHORS

Juan F Reyes, Christopher Sackmann, Alana Hoffmann, Per Svenningsson, Jürgen Winkler, Martin Ingelsson, Martin Hallbeck

ABSTRACT

The intercellular transfer of alpha-synuclein (α-syn) has been implicated in the progression of Parkinson's disease (PD) and multiple system atrophy (MSA). The cellular mechanisms underlying this process are now beginning to be elucidated. In this study, we demonstrate that the gap junction protein connexin-32 (Cx32) is centrally involved in the preferential uptake of α-syn oligomeric assemblies (oα-syn) in neurons and oligodendrocytes. In vitro, we demonstrate a clear correlation between Cx32 expression and oα-syn uptake. Pharmacological and genetic strategies targeting Cx32 successfully blocked oα-syn uptake. In cellular and transgenic mice modeling PD and MSA, we observed significant upregulation of Cx32 which correlates with α-syn accumulation. Notably, we could also demonstrate a direct interaction between α-syn and Cx32 in two out of four human PD cases that was absent in all four age-matched controls. These data are suggestive of a link between Cx32 and PD pathophysiology. Collectively, our results provide compelling evidence for Cx32 as a novel target for therapeutic intervention in PD and related α-synucleinopathies. More... »

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00401-019-02007-x

DOI

http://dx.doi.org/10.1007/s00401-019-02007-x

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1113378569

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30976973


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