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A more recent version of this article appeared on August 2, 2002
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M200666200v1
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Papers In Press, published online ahead of print May 28, 2002
J. Biol. Chem, 10.1074/jbc.M200666200
Submitted on January 22, 2002
Revised on May 28, 2002
Accepted on May 28, 2002

Effect of wild-type or mutant parkin on oxidative damage, nitric oxide, antioxidant defences and the proteasome

Dong-Hoon Hyun, MoonHee Lee, Nobutaka Hattori, Shin-Ichiro Kubo, Yoshikuni Mizuno, Barry Halliwell, and Peter Jenner

Wolfson Centre for Age-Related Diseases, GKT School of Biomedical Sciences, London SE1 1UL

Corresponding Author: div.pharm{at}kcl.ac.uk

Mutations in parkin (a ubiquitin protein ligase) are involved in autosomal recessive juvenile parkinsonism (AR-JP), but it is not known how they cause nigral cell death. We examined the effect of parkin overexpression on cellular levels of oxidative damage, antioxidant defences, nitric oxide production and proteasomal enzyme activity. Increasing expression of parkin by gene transfection in NT-2 and SK-N-MC cells led to increased proteasomal activity, decreased levels of protein carbonyls and 3-nitrotyrosine-containing proteins, and a trend to a reduction in ubiquitinated protein levels. Transfection of these cells with DNA encoding three mutant parkins associated with AR-JP (Del 3-5, T240R and Q311X) gave smaller increase in proteasomal activity, and led to elevated levels of protein carbonyls and lipid peroxidation. Turnover of the mutant proteins was slower than that of the wild-type protein, and both could be blocked by the proteasome inhibitor, lactacystin. A rise in levels of nitrated proteins and increased levels of NO2-/NO3- were also observed in cells transfected with mutant parkins, apparently due to increased levels of neuronal nitric oxide synthase. The presence of mutant parkin in substantia nigra in juvenile parkinsonism may increase oxidative stress and nitric oxide production, sensitizing cells to death induced by other insults.


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