Cross-linking for the analysis of α-synuclein in the enteric nervous system.
Identifieur interne : 000313 ( Main/Exploration ); précédent : 000312; suivant : 000314Cross-linking for the analysis of α-synuclein in the enteric nervous system.
Auteurs : Anne-Gaëlle Corbillé [France] ; Michel Neunlist [France] ; Pascal Derkinderen [France]Source :
- Journal of neurochemistry [ 1471-4159 ] ; 2016.
Abstract
Since the observation that aggregated α-synuclein, the pathological hallmark of Parkinson's disease (PD), is found in the gut in almost all patients, it has been suggested that the enteric nervous system (ENS) could be a starting point for α-synuclein pathology. α-synuclein has long been thought to occur as a monomer in living cells, but recent studies reported that it instead exists as a tetramer in non-neuronal cells and in neurons. Given the possible key role of the ENS in PD pathophysiology, we undertook the current research to characterize the native state of α-synuclein in rat primary culture of ENS and in adult human healthy ENS. Using amine-reactive cross-linking, we showed that, by contrast to cell lines and brain neurons, α-synuclein exists primarily as a monomer in intact enteric neurons, suggesting that the native state of α-synuclein is different between the ENS and the brain. Our results provide new insights into the widely discussed concepts of α-synuclein aggregation and misfolding in PD and raise issue about the possible transmission of α-synuclein from the ENS to the brain.
DOI: 10.1111/jnc.13845
PubMed: 27637918
Affiliations:
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sort="Derkinderen, Pascal" uniqKey="Derkinderen P" first="Pascal" last="Derkinderen">Pascal Derkinderen</name><affiliation wicri:level="3"><nlm:affiliation>Inserm, U913, Nantes, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Inserm, U913, Nantes</wicri:regionArea><placeName><region type="region">Pays de la Loire</region><region type="old region">Pays de la Loire</region><settlement type="city">Nantes</settlement></placeName></affiliation></author></analytic><series><title level="j">Journal of neurochemistry</title><idno type="eISSN">1471-4159</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Since the observation that aggregated α-synuclein, the pathological hallmark of Parkinson's disease (PD), is found in the gut in almost all patients, it has been suggested that the enteric nervous system (ENS) could be a starting point for α-synuclein pathology. α-synuclein has long been thought to occur as a monomer in living cells, but recent studies reported that it instead exists as a tetramer in non-neuronal cells and in neurons. Given the possible key role of the ENS in PD pathophysiology, we undertook the current research to characterize the native state of α-synuclein in rat primary culture of ENS and in adult human healthy ENS. Using amine-reactive cross-linking, we showed that, by contrast to cell lines and brain neurons, α-synuclein exists primarily as a monomer in intact enteric neurons, suggesting that the native state of α-synuclein is different between the ENS and the brain. 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