Affiliations: [a] Department of Neural Plasticity, Tokyo Institute of Psychiatry, Tokyo 156-8585, Japan | [b] Sino-Japan Joint Laboratory on Neurodegenerative Diseases, Beijing Institute of Geriatrics, Xuanwu Hospital, Capital University of Medical Sciences, Beijing 100053, China
Correspondence:
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Corresponding author: Dr. Kenji Uéda, Department of Neural Plasticity, Tokyo Institute of Psychiatry, 2-1-8 Kamikitazawa, Setagaya-ku, Tokyo 156-8585, Japan. Tel.: +81 3 3304 5701 ext. 511; Fax: +81 3 3329 8035; E-mail: kenueda@prit.go.jp.
Abstract: α-Synuclein is a neuronal protein originally identified in Alzheimer's disease (AD) amyloid plaques in 1993 and named non-Aβ component precursor (NACP) [92]. Later, the discovery of two missense mutations (G88C and G209A), which resulted in Ala30Pro (A30P) and Ala53Thr (A53T) substitutions, of the α-synuclein gene in certain autosomal-dominant early onset familial Parkinson's disease (PD) has greatly promoted the understanding of the role of α-synuclein in the pathogenesis of neurodegenerative diseases, such as PD, dementia with Lewy bodies (DLB) and multiple system atrophy (MSA) [5,6,51,75]. At present, it is widely accepted that α-synuclein may play a central role in several neurodegenerative disorders because of the presence of insoluble α-synuclein as the major fibrillar component of inclusion bodies. From the cloning of the human α-synuclein cDNA in 1993 to the present, α-synuclein has been carefully documented in many aspects. In this article, we review the progress of studies on α-synuclein and its role inα-synuclein-related neurodegenerative diseases.
