Objective: To confirm that α-synuclein aggregation and propagation in marmoset brains deteriorates its motor function.

Background: Recently, the α-synuclein amyloid fibril is thought to be a main component of Lewy pathology. The propagation of α-synuclein aggregates has been reported. The α-synuclein aggregates and Lewy bodies extracted from brain samples of Parkinson’s disease (PD) patients were administered to mice brains. The aggregates were found in ipsilateral brains. As a result, α-synuclein fibril is thought to be pathogenesis of PD.

Methods: We prepared α-synuclein fibrils using recombinant α-synuclein derived from Escherichia coli. We inoculated α-synuclein fibrils to the left striatum of marmoset brains and evaluated its motor function and pathological changes. To detect marmoset motor function, we developed a novel multimodal system, MarmoDetector, for the automated 3D analysis of marmoset behavior under freely moving conditions. To evaluate pathological changes of marmoset brains, we performed immunohistochemical studies including phosphorylated α-synuclein pathology.

Results: Inoculating α-synuclein fibrils to marmoset brains caused α-synuclein aggregation and propagation. Three months after inoculation, we assessed behavioural changes using MarmoDetector for over several days, and marmoset motor activity was decreased by about 30% compared with that before inoculation. In pathological analysis, we also confirmed α-synuclein aggregation and propagation in marmoset brains.

Conclusions: We confirmed α-synuclein aggregation and propagation in marmoset brains and its changes influence on marmoset behaviors. These results suggest that marmoset symptoms correspond to the onset of PD. Our marmoset model can be a new primate model recapitulating the pathology of human PD.

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MDS Abstracts - https://www.mdsabstracts.org/abstract/%ce%b1-synuclein-aggregation-and-propagation-in-marmoset-brains-deteriorates-its-motor-function/