Changes in the two-dimensional electrophoresis pattern of the Parkinson's disease related protein DJ-1 in human SH-SY5Y neuroblastoma cells after dopamine treatment.

DJ-1 is a mitochondrial protein linked to Parkinson's disease. DJ-1 has been suggested to have several possible functions, although it has been mainly associated to oxidative stress defence. Changes in the two-dimensional electrophoresis pattern have been thoroughly described as a consequence of oxidative modification of the Cys106 residue.

Proteomics as a tool to investigate cell models for dopamine toxicity.

Dopaminergic neurons are particularly exposed to oxidative stress because dopamine metabolism gives rise to endogenous toxins. Here, two different models for dopamine toxicity have been investigated using proteomics: stable alpha-synuclein-expressing neuroblastoma (SH-SY5Y) cells to understand how alpha-synuclein modulates dopamine toxicity at the central level, and cultured T-cell leukaemia (Jurkat) cells challenged with dopamine or l-dopa to evaluate protein changes on the surface of peripheral cells. alpha-synuclein-expressing cells were more resistant compared with wild-type cells, showing upregulation of antioxidant proteins including the Parkinson's disease-related DJ-1 protein.

alpha-Synuclein protects SH-SY5Y cells from dopamine toxicity.

Dopaminergic human neuroblastoma SH-SY5Y cells were stably transformed to increase expression of alpha-synuclein, a Parkinson's disease-related protein. Transformed cells were more resistant to oxidative insults, showing a cytoprotective role of alpha-synuclein. The expression of redox chaperonins (DJ-1, HSP70, and 14-3-3) was evaluated by Western blotting.