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Altered dopamine homeostasis is an accepted mechanism in the pathogene-sis of Parkinson’s disease. a-Synuclein overexpression and impaired dis-posal contribute to this mechanism. However, biochemical alterations associated with the interplay of cytosolic dopamine and increaseda-synuc-lein are still unclear. | ỊFEBS Journal Proteomic analysis of dopamine and a-synuclein interplay in a cellular model of Parkinson s disease pathogenesis Tiziana Alberio1 Alessandra Maria Bossi2 Alberto Milli2 Elisa Parma1 Marzia Bruna Gariboldi1 Giovanna Tosi3 Leonardo Lopiano4 and Mauro Fasano1 1 Department of Structuraland FunctionalBiology and Centre of Neuroscience University of Insubria Busto Arsizio Italy 2 Department of Biotechnology University of Verona Italy 3 Department of Clinicaland BiologicalSciences University of Insubria Varese Italy 4 Department of Neuroscience University of Torino Italy Keywords dopamine network enrichment NF-kB Parkinson s disease SH-SY5Y a-synuclein Correspondence M. Fasano Department of Structural and FunctionalBiology and Centre of Neuroscience University of Insubria via Alberto da Giussano 12 21052 Busto Arsizio Italy Fax 39 0331 339459 Tel 39 0331 339450 E-mail mauro.fasano@uninsubria.it Website http busto.dipbsf.uninsubria.it cns fasano Received 4 June 2010 revised 14 July 2010 accepted 27 September 2010 doi 10.1111 j.1742-4658.2010.07896.x Altered dopamine homeostasis is an accepted mechanism in the pathogenesis of Parkinson s disease. a-Synuclein overexpression and impaired disposal contribute to this mechanism. However biochemical alterations associated with the interplay of cytosolic dopamine and increased a-synuc-lein are still unclear. Catecholaminergic SH-SY5Y human neuroblastoma cells are a suitable model for investigating dopamine toxicity. In the present study we report the proteomic pattern of SH-SY5Y cells overexpressing a-synuclein 1.6-fold induction after dopamine exposure. Dopamine itself is able to upregulate a-synuclein expression. However the effect is not observed in cells that already overexpress a-synuclein as a consequence of transfection. The proteomic analysis highlights significant changes in 23 proteins linked to specific cellular processes such as cytoskeleton structure and regulation mitochondrial function energetic .
