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• Vol.48 No.11
• CLINICA NEUROL, 48: 984−985, 2008
• Vol.48 No.11 contents

The 49th Annual Meeting of the Japanese Society of Neurology

Cellular pathophysiology of Parkinson's disease

Atsushi Takeda, M.D., Naoto Sugeno, M.D., Takafumi Hasegawa, M.D., Michiko Kobayashi, M.D. and Akio Kikuchi, M.D.

Division of Neurology, Department of Neuroscience & Sensory Organs, Tohoku University, Graduate School of Medicine

To explore pathogenesis of synucleinopathy including Parkinson's disease and multiple system atrophy, we developed cellular model for synucleinopathy. In this experimental model, α-synuclein was overexpressed in SH-SY5Y cells, which were then exposed to mitochondrial toxins. The data thus obtained suggested the followings.
1) By the treatment with rotenone, wild type α-synuclein overexpressing cells demonstrated intracellular aggregations, which shared a number of features with Lewy bodies.
2) The aggregate formation of α-synuclein may be cytoprotective.
3) The catechol-derived quinones are candidate molecules to facilitate the oligomer formation of α-synuclein.
4) The cells overexpressing S129A mutant showed few aggregations. It is suggested that phosphorylation at serine 129 is essential for aggregate formation.
5) In wild-type α-synuclein cells treated with rotenone, unfolded protein response (UPR) markers were induced prior to the induction of mitochondrial disruption and caspase-3 activation.
6) On the other hand, the S129A mutant failed to activate these UPRs. Thus it seems plausible that α-synuclein toxicity is dependent on the phosphorylation at S129.
Full Text of this Article in Japanese PDF (156K)

(CLINICA NEUROL, 48: 984−985, 2008)
key words: synucleinopathy, ER stress, quinines, aggregation

(Received: 17-May-08)