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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 |
1987-2-19
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pubmed:abstractText |
Data indicating that the 21-kDa protein (p21) Harvey-ras gene product shares sequence homology with guanine nucleotide-binding proteins (G proteins) has stimulated research on the influence(s) of p21 on G-protein-regulated systems in vertebrate cells. Our previous work demonstrated that NIH-3T3 mouse cells expressing high levels of the cellular ras oncogene isolated from the EJ human bladder carcinoma (EJ-ras) exhibited reduced hormone-stimulated adenylate cyclase activity. We now report that in these cells another enzyme system thought to be regulated by G proteins is inhibited, namely phospholipases A2 and C. NIH-3T3 cells incubated in plasma-derived serum release significant levels of prostaglandin E2 (PGE2) as determined by radioimmunoassay when exposed to platelet-derived growth factor (PDGF) at 2 units/ml; the levels of PGE2 released from EJ-ras-transfected cells are only 3% those of controls despite a similar basal (unstimulated) release from control and EJ-ras-transfected cells. The lack of PDGF-stimulated PGE2 release from EJ-ras-transfected cells is not due to a defect in the prostaglandin cyclooxygenase enzyme, since incubation of control cells and EJ-ras-transfected cells in 0.33, 3.3, or 33 microM arachidonate resulted in identical levels of PGE2 release. The lack of PDGF-stimulated PGE2 release from EJ-ras-transfected cells also does not result from the loss of functional PDGF receptors. EJ-ras-transformed cells bind 70% as much 125I-labeled PDGF as control cells and are stimulated to incorporate [3H]thymidine and to proliferate after exposure to PDGF. Moreover, this inhibition is not likely the result of a secondary cellular effect related to the transformed phenotype, since NIH-3T3 cells transformed by v-src released PGE2 at wild-type levels after exposure to PDGF. Determination of total water-soluble inositolphospholipids and changes in the specific activities of phosphatidylcholine in control and EJ-ras-transfected cells demonstrated that PDGF-stimulated phospholipase C and A2 activities are inhibited in the EJ-ras-transfected cells.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-13671378,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-17805690,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-216415,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-287022,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-2989702,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-3001936,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-3012529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-3864604,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-3919305,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-3922980,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-3936489,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-5903721,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-6089758,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-6094010,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-6147754,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-6148703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-6148751,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-6265801,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-6279659,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-6290897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-6304521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-6683594,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-6768732,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-6866079,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-7063039,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-7133135,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099298-7177195
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
84
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
546-50
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:3099298-Animals,
pubmed-meshheading:3099298-Arachidonic Acid,
pubmed-meshheading:3099298-Arachidonic Acids,
pubmed-meshheading:3099298-Cell Transformation, Neoplastic,
pubmed-meshheading:3099298-Cells, Cultured,
pubmed-meshheading:3099298-Dinoprostone,
pubmed-meshheading:3099298-Humans,
pubmed-meshheading:3099298-Kinetics,
pubmed-meshheading:3099298-Mice,
pubmed-meshheading:3099298-Mice, Inbred Strains,
pubmed-meshheading:3099298-Oncogenes,
pubmed-meshheading:3099298-Phospholipases,
pubmed-meshheading:3099298-Platelet-Derived Growth Factor,
pubmed-meshheading:3099298-Prostaglandins E
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pubmed:year |
1987
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pubmed:articleTitle |
Loss of platelet-derived growth factor-stimulated phospholipase activity in NIH-3T3 cells expressing the EJ-ras oncogene.
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pubmed:publicationType |
Journal Article
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