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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1994-10-18
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pubmed:abstractText |
Activating the protein-tyrosine kinase of v-Fps results in a rapid increase in diglyceride (DG) in rat fibroblasts. The v-Fps-induced increases in DG were detected only when phospholipids were prelabeled with [3H]-myristate, which is incorporated primarily into phosphatidylcholine (PC). Inhibition of phosphatidic acid (PA) phosphatase (PAP), which converts PA to DG, blocked v-Fps-induced DG production. PA is a primary metabolite of type D phospholipases (PLD). Consistent with these observations, PLD activity was activated in response to the kinase activity of v-Fps. The increased PLD activity was detected only when the cells were prelabeled with the PC-specific [3H]-myristate. These data support the hypothesis that v-Fps-induced DG is derived from PC via the PLD/PAP pathway.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arachidonic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Diglycerides,
http://linkedlifedata.com/resource/pubmed/chemical/Fusion Proteins, gag-onc,
http://linkedlifedata.com/resource/pubmed/chemical/Myristic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Myristic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidate Phosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylcholines,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase D,
http://linkedlifedata.com/resource/pubmed/chemical/Propranolol,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/v-fps oncogene protein, Fujinami...
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
203
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1195-2003
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8093039-Animals,
pubmed-meshheading:8093039-Arachidonic Acid,
pubmed-meshheading:8093039-Cell Line, Transformed,
pubmed-meshheading:8093039-Diglycerides,
pubmed-meshheading:8093039-Enzyme Activation,
pubmed-meshheading:8093039-Fibroblasts,
pubmed-meshheading:8093039-Fusion Proteins, gag-onc,
pubmed-meshheading:8093039-Myristic Acid,
pubmed-meshheading:8093039-Myristic Acids,
pubmed-meshheading:8093039-Phosphatidate Phosphatase,
pubmed-meshheading:8093039-Phosphatidic Acids,
pubmed-meshheading:8093039-Phosphatidylcholines,
pubmed-meshheading:8093039-Phospholipase D,
pubmed-meshheading:8093039-Propranolol,
pubmed-meshheading:8093039-Protein-Tyrosine Kinases,
pubmed-meshheading:8093039-Rats,
pubmed-meshheading:8093039-Temperature
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pubmed:year |
1994
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pubmed:articleTitle |
Phosphatidylcholine-specific phospholipase D activity is elevated in v-Fps-transformed cells.
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pubmed:affiliation |
Institute for Biomolecular Structure and Function, Hunter College of the City University of New York, NY 10021.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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