Journal
NEUROBIOLOGY OF DISEASE
Volume 29, Issue 3, Pages 477-489Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.nbd.2007.11.007
Keywords
Parkinson disease; mitochondria; PC12 cells; dopamine; dopamine quinone; proteomics; 2-D DIGE; mitofilin; mitochondrial creatine kinase
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Funding
- NIA NIH HHS [R01 AG020899, R01 AG020899-05, R01 AG020899-04, AG20899] Funding Source: Medline
- NIDA NIH HHS [R01 DA009601-07, R01 DA009601-06, R01 DA009601-08, R01 DA009601-05, DA09601, R01 DA009601] Funding Source: Medline
- NINDS NIH HHS [R01 NS044076-03, R01 NS044076-04, R01 NS044076, NS44076, R01 NS044076-02, R01 NS044076-01, R01 NS044076-05] Funding Source: Medline
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Oxidative stress and mitochondrial dysfunction have been linked to dopaminergic neuron degeneration in Parkinson disease. We have previously shown that dopamine oxidation leads to selective dopaminergic terminal degeneration in vivo and alters mitochondrial function in vitro. In this study, we utilized 2-D difference in-gel electrophoresis to assess changes in the mitochondrial proteome following in vitro exposure to reactive dopamine quinone. A subset of proteins exhibit decreased fluorescence labeling following dopamine oxidation, suggesting a rapid loss of specific proteins. Amongst these proteins are mitochondrial creatine kinase, mitofilin, mortalin, the 75 kDa subunit of NADH dehydrogenase, and superoxide dismutase 2. Western blot analyses for mitochondrial creatine kinase and mitofilin confirmed significant losses in isolated brain mitochondria exposed to dopamine quinone and PC12 cells exposed to dopamine. These results suggest that specific mitochondrial proteins are uniquely susceptible to changes in abundance following dopamine oxidation, and carry implications for mitochondrial stability in Parkinson disease neurodegeneration. (c) 2007 Elsevier Inc. All rights reserved.
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