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Tofaris, George K.; Reitbock, Pablo Gracia; Humby, Trevor; Lambourne, Sarah L.; O'Connell, Mark; Ghetti, Bernadino; Gossage, Helen; Emson, Piers C.; Wilkinson, Lawrence Stephen; Goedert, Michel; Spillantini, Maria Grazia (2006)
Publisher: Society for Neuroscience
Languages: English
Types: Article
Subjects: BF

Classified by OpenAIRE into

mesheuropmc: nervous system, nervous system diseases
Dysfunction of the 140 aa protein α-synuclein plays a central role in Lewy body disorders, including Parkinson’s disease, as well as in multiple system atrophy. Here, we show that the expression of truncated human α-synuclein(1–120), driven by the rat tyrosine hydroxylase promoter on a mouse α-synuclein null background, leads to the formation of pathological inclusions in the substantia nigra and olfactory bulb and to a reduction in striatal dopamine levels. At the behavioral level, the transgenic mice showed a progressive reduction in spontaneous locomotion and an increased response to amphetamine. These findings suggest that the C-terminal of α-synuclein is an important regulator of aggregation in vivo and will help to understand the mechanisms underlying the pathogenesis of Lewy body disorders and multiple system atrophy.

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