The α-Synuclein Gene and Parkinson Disease in a Chinese Population

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Abstract
THE GENE that codes for the presynaptic protein α-synuclein is associated with dominantly inherited parkinsonism in the Italian Contursi kindred and 3 unrelated Greek families.1 In these families, affected members have a missense mutation G209A in exon 4, which results in an exchange of an alanine to a threonine at position 53 of the amino acid sequence (Ala53Thr). A second α-synuclein mutation associated with Parkinson disease (PD) has been recently described by Kruger et al.2 This variant is characterized by a cytosine-to-guanine transversion at nucleotide position 88 of the coding sequence (exon 3), which leads to a change at position 30 of the amino acid sequence (Ala30Pro). α-Synuclein is a precursor to constituents of Alzheimer disease plaques and is found in Lewy bodies, the eosinophilic inclusion bodies that define neuropathological characteristics of PD. The function of α-synuclein is unknown, although it is thought to be involved with neuronal plasticity and may mediate binding between structural proteins.3 Recent studies have failed to find the Ala53Thr mutation in subjects of European Caucasian ancestry with familial,4 younger-onset,5 and sporadic6 PD. As for the Chinese, there has been only one small study7 looking for the Ala53Thr mutation in 65 cases of sporadic PD in Taiwan Chinese patients. We therefore undertook a large-scale study to look for both Ala53Thr and Ala30Pro mutations. We investigated 183 sporadic, 17 younger-onset (onset age of younger than 50 years), and 7 Chinese patients with a positive family history together with 227 unaffected Chinese subjects for the presence of the Ala53Thr and Ala30Pro mutations in the α-synuclein gene.

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