Oxidation of proteinaceous cysteine residues by dopamine-derived H2O2 in PC12 cells

Cited 31 time in scopus
Metadata Downloads
Oxidation of proteinaceous cysteine residues by dopamine-derived H2O2 in PC12 cells
Jae Ryong kim; Ki Sun Kwon; Hae Won Yoon; Seung Rock Lee; Sue Goo Rhee
Bibliographic Citation
Archives of Biochemistry and Biophysics, vol. 397, no. 2, pp. 414-423
Publication Year
Cellular metabolism of dopamine (DA) generates H2O2, which is further reduced to hydroxyl radicals in the presence of iron. Cellular damage inflicted by DA-derived hydroxyl radicals is thought to contribute to Parkinson's disease. We have previously developed procedures for detecting proteins that contain H2O2-sensitive cysteine (or selenocysteine) residues. Using these procedures, we identified ERP72 and ERP60, two members of the protein disulfide isomerase family, creatine kinase, glyceraldehyde-3-phosphate dehydrogenase, phospholipase C-γ1, and thioredoxin reductase as the targets of DA-derived H2O2. Experiments with purified enzymes identified the essential Cys residues of creatine kinase and glyceraldehyde-3-phosphate dehydrogenase, that are specifically oxidized by H2O2. Although the identified proteins represent only a fraction of the targets of DA-derived H2O2, functional impairment of these proteins has previously been associated with cell death. The oxidation of proteins that contain reactive Cys residues by DA-derived H2O2 is therefore proposed both to be largely responsible for DA-induced apoptosis in neuronal cells and to play an important role in the pathogenesis of Parkinson's disease.
Cysteine oxidationDopamine toxicityHydrogen peroxideParkinson's disease
Appears in Collections:
Aging Convergence Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.

Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.