. Exogenous α-synuclein fibrils induce Lewy body pathology leading to synaptic dysfunction and neuron death. Neuron. 2011 Oct 6;72(1):57-71. PubMed.


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  1. I think this paper adds to the increasing literature on the consequences of extracellular α-synuclein and its role in PD pathogenesis. It represents an important validation of several recent studies showing that α-synuclein can be taken up by neurons from the extracellular space (Desplats et al., 2009; Danzer et al., 2011), that exogenously applied α-synuclein can seed aggregation of intracellular α-synuclein (Luk et al., 2009; Danzer et al., 2009), that α-synuclein oligomers can be transmitted from neuron to neuron and transported in both anterograde and retrograde direction within neurons (Danzer et al., 2011), and that extracellular α-synuclein can have detrimental effects in the recipient cells (Desplats et al., 2009; Emmanouilidou et al., 2010; Danzer et al., 2011). The paper is an important contribution to the field, demonstrating nicely how extracellular α-synuclein may be affecting neuronal cell health.


    . Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein. Proc Natl Acad Sci U S A. 2009 Aug 4;106(31):13010-5. PubMed.

    . Heat-shock protein 70 modulates toxic extracellular α-synuclein oligomers and rescues trans-synaptic toxicity. FASEB J. 2011 Jan;25(1):326-36. PubMed.

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    . Seeding induced by alpha-synuclein oligomers provides evidence for spreading of alpha-synuclein pathology. J Neurochem. 2009 Oct;111(1):192-203. PubMed.

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