Proteomic identification of dopamine-conjugated proteins from isolated rat brain mitochondria and SH-SY5Y cells.
Proteomic identification of dopamine-conjugated proteins from isolated rat brain mitochondria and SH-SY5Y cells.
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DOI：
10.1016/j.nbd.2009.03.004
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发表时间：
2009-06
影响因子：
6.1
通讯作者：
Hastings TG
中科院分区：
文献类型：
--
作者：
Van Laar VS;Mishizen AJ;Cascio M;Hastings TG
Dopamine oxidation has been previously demonstrated to cause dysfunction in mitochondrial respiration and membrane permeability, possibly related to covalent modification of critical proteins by the reactive dopamine quinone. However, specific mitochondrial protein targets have not been identified. In this study, we utilized proteomic techniques to identify proteins directly conjugated with 14C-dopamine from isolated rat brain mitochondria exposed to radiolabeled dopamine quinone (150 μM) and differentiated SH-SY5Y cells treated with 14C-dopamine (150 μM). We observed a subset of rat brain mitochondrial proteins that were covalently modified by 14C-dopamine, including chaperonin, ubiquinol-cytochrome c reductase core protein 1, glucose regulated protein 75/mitochondrial HSP70/mortalin, mitofilin, and mitochondrial creatine kinase. We also found the Parkinson’s disease associated proteins ubiquitin carboxy-terminal hydrolase L1 and DJ-1 to be covalently modified by dopamine in both brain mitochondrial preparations and SH-SY5Y cells. The susceptibility of the identified proteins to covalent modification by dopamine may carry implications for their role in the vulnerability of dopaminergic neurons in Parkinson’s disease pathogenesis.
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