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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2010-9-30
pubmed:abstractText
DJ-1 is a mitochondrial protein linked to Parkinson's disease. DJ-1 has been suggested to have several possible functions, although it has been mainly associated to oxidative stress defence. Changes in the two-dimensional electrophoresis pattern have been thoroughly described as a consequence of oxidative modification of the Cys106 residue. There is accumulating evidence supporting a specific role of DJ-1 in protecting dopaminergic neurons from dopamine itself. By exposing SH-SY5Y human neuroblastoma catecholaminergic cells to dopamine, we observed a specific increase in the most acidic forms in the DJ-1 two-dimensional electrophoresis pattern together with a significant decrease of the most basic spot. Unlike cells exposed to generic oxidative conditions, no additional shift was observed. The results are corroborated by a meta-analysis of the literature showing that in the absence of dopamine treatment the specific acidic form is underrepresented.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1521-6551
pubmed:author
pubmed:copyrightInfo
© 2010 IUBMB IUBMB Life.
pubmed:issnType
Electronic
pubmed:volume
62
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
688-92
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Changes in the two-dimensional electrophoresis pattern of the Parkinson's disease related protein DJ-1 in human SH-SY5Y neuroblastoma cells after dopamine treatment.
pubmed:affiliation
Department of Structural and Functional Biology, Center of Neuroscience, University of Insubria, Busto Arsizio, VA, Italy.
pubmed:publicationType
Journal Article