pubmed-article:8355574 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8355574 | lifeskim:mentions | umls-concept:C0016030 | lld:lifeskim |
pubmed-article:8355574 | lifeskim:mentions | umls-concept:C0031670 | lld:lifeskim |
pubmed-article:8355574 | lifeskim:mentions | umls-concept:C0031671 | lld:lifeskim |
pubmed-article:8355574 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
pubmed-article:8355574 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
pubmed-article:8355574 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:8355574 | pubmed:dateCreated | 1993-9-17 | lld:pubmed |
pubmed-article:8355574 | 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. | lld:pubmed |
pubmed-article:8355574 | pubmed:language | eng | lld:pubmed |
pubmed-article:8355574 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8355574 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8355574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8355574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8355574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8355574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8355574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8355574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8355574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8355574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8355574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8355574 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8355574 | pubmed:month | Jun | lld:pubmed |
pubmed-article:8355574 | pubmed:issn | 0024-4201 | lld:pubmed |
pubmed-article:8355574 | pubmed:author | pubmed-author:KiseTT | lld:pubmed |
pubmed-article:8355574 | pubmed:author | pubmed-author:GaramszegiNN | lld:pubmed |
pubmed-article:8355574 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8355574 | pubmed:volume | 28 | lld:pubmed |
pubmed-article:8355574 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8355574 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8355574 | pubmed:pagination | 479-81 | lld:pubmed |
pubmed-article:8355574 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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pubmed-article:8355574 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8355574 | pubmed:articleTitle | Protein kinase C-dependent stimulation of phospholipase D in phospholipase C-treated fibroblasts. | lld:pubmed |
pubmed-article:8355574 | pubmed:affiliation | Hormel Institute, University of Minnesota, Austin 55912. | lld:pubmed |
pubmed-article:8355574 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8355574 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8355574 | lld:pubmed |