rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
6
|
pubmed:dateCreated |
1993-9-17
|
pubmed:abstractText |
Treatment of [14C]choline- or [14C]ethanolamine-labeled NIH 3T3 fibroblasts with Bacillus cereus phosphatidyl-choline-specific phospholipase C (PLC) enhanced phospholipase D (PLD)-mediated hydrolysis of the respective 14C-labeled phospholipids. PLD activity was stimulated by 1.5 U/mL of PLC and by 100 nM of the protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) to similar extents. Treatment of [14C]palmitic acid-labeled fibroblasts with PLC in the presence of ethanol also enhanced PLD-mediated formation of phosphatidylethanol; the effects of PLC and PMA were nonadditive. PLC had no effect on PLD activity in fibroblasts in which PKC was down-regulated by prolonged (24 h) treatment with 300 nM PMA. These data indicate that treatment of fibroblasts with exogenous PLC results in PKC-dependent activation of PLD.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0024-4201
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
28
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
479-81
|
pubmed:dateRevised |
2007-11-15
|
pubmed:meshHeading |
pubmed-meshheading:8355574-3T3 Cells,
pubmed-meshheading:8355574-Animals,
pubmed-meshheading:8355574-Choline,
pubmed-meshheading:8355574-Dose-Response Relationship, Drug,
pubmed-meshheading:8355574-Fibroblasts,
pubmed-meshheading:8355574-Hydrolysis,
pubmed-meshheading:8355574-Mice,
pubmed-meshheading:8355574-Phosphatidylcholines,
pubmed-meshheading:8355574-Phosphatidylethanolamines,
pubmed-meshheading:8355574-Phospholipase D,
pubmed-meshheading:8355574-Phospholipids,
pubmed-meshheading:8355574-Phosphorylcholine,
pubmed-meshheading:8355574-Protein Kinase C,
pubmed-meshheading:8355574-Tetradecanoylphorbol Acetate,
pubmed-meshheading:8355574-Type C Phospholipases
|
pubmed:year |
1993
|
pubmed:articleTitle |
Protein kinase C-dependent stimulation of phospholipase D in phospholipase C-treated fibroblasts.
|
pubmed:affiliation |
Hormel Institute, University of Minnesota, Austin 55912.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|