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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2000-11-20
pubmed:abstractText
Phospholipase D2 (PLD2) is expressed in brain and inhibited by synuclein, which is involved in Parkinson's and Alzheimer's diseases. However, the activation mechanism of PLD2 in neuronal cells has not been defined clearly. Hydrogen peroxide (H(2)O(2)) plays roles in the neurodegenerative diseases and also acts as a second messenger of various molecules such as nerve growth factor. To study regulation mechanisms of PLD2 by H(2)O(2) in neuronal cells, we have made stable PC12 cell lines expressing PLD2 (PLD2-PC12 cells). H(2)O(2) treatment stimulated PLD activity in PLD2-PC12 cells in a dose- and time-dependent manner. This activation was inhibited by the treatment with protein kinase C (PKC) inhibitors or by depletion of PKCalpha, -delta, and -epsilon. Phorbol ester markedly activated PLD2. Co-treatment with phorbol ester and H(2)O(2) did not show an additive effect. Chelation of extracellular calcium substantially blocked the H(2)O(2)-induced activation of PLD2. A calcium ionophore induced PLD2 activation in a PKC-dependent manner. Protein-tyrosine kinase inhibitors inhibited H(2)O(2)-induced PLD activation slightly. These data indicate that H(2)O(2) can activate PLD2 in PC12 cells and that this activation is largely dependent on PKC and Ca(2+) ions and minimally dependent on tyrosine phosphorylation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0022-3042
pubmed:author
pubmed:issnType
Print
pubmed:volume
75
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2445-54
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Regulation of phospholipase D2 by H(2)O(2) in PC12 cells.
pubmed:affiliation
Department of Biochemistry, College of Medicine, Chungnam National University, Taejeon, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't