Changes in endoplasmic reticulum stress proteins and aldolase A in cells exposed to dopamine.
Changes in endoplasmic reticulum stress proteins and aldolase A in cells exposed to dopamine.
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DOI：
10.1111/j.1471-4159.2008.05392.x
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发表时间：
2008-07
影响因子：
4.7
通讯作者：
Hastings TG
中科院分区：
文献类型：
--
作者：
Dukes AA;Van Laar VS;Cascio M;Hastings TG
In Parkinson’s disease (PD), oxidative stress is implicated in protein misfolding and aggregation, which may activate the unfolded protein response (UPR) by the endoplasmic reticulum (ER). Dopamine (DA) can initiate oxidative stress via H2O2 formation by DA metabolism and by oxidation into DA quinone (DAQ). We have previously shown that DAQ induces oxidative protein modification, mitochondrial dysfunction in vitro, and dopaminergic cell toxicity in vivo and in vitro. In this study, we used cysteine- and lysine-reactive fluorescent dyes with 2-D difference in-gel electrophoresis (2D-DIGE), mass spectrometry, and peptide mass fingerprint analysis to identify proteins in PC12 cell mitochondrial-enriched fractions that were altered in abundance following DA exposure (150μM,16h). Quantitative changes in proteins labeled with fluorescent dyes indicated increases in a subset of proteins after DA exposure: calreticulin, ERp29, ERp99, Grp58, Grp78, Grp94, and Orp150 (149-260%), and decreased levels of aldolase A (39-42%). Changes in levels of several proteins detected by 2D-DIGE were confirmed by Western blot. Using this unbiased proteomics approach, our findings demonstrated that in PC12 cells, DA exposure leads to a cellular response indicative of ER stress prior to the onset of cell death, providing a potential link between DA and the UPR in the pathogenesis of PD.
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