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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
33
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pubmed:dateCreated |
1990-12-28
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pubmed:abstractText |
The mitogenic activity of membrane-associated tyrosine kinases such as Src and the PDGF receptor appear to depend on Ras function. Ras biochemical activity involves regulation of a GTP/GDP cycle and the GTPase activating protein (GAP). Recently, PDGF and v-Src have been shown to stimulate tyrosine phosphorylation of GAP, linking these pathways at the biochemical level. To test whether PDGF and v-Src affect the Ras GTP/GDP cycle, we have measured the guanine nucleotides complexed to Ras in NIH3T3 cells and compared the ratio of GTP to total GTP + GDP detected (percent GTP). In normal quiescent NIH3T3 cells, PDGF stimulated the basal amount of GTP complexed to Ras (7%) by 2.1-fold to 15%. The effect was dependent on PDGF concentration and was observed maximally within 10 min following PDGF challenge. Ras was complexed to 22% GTP in NIH3T3 cells transformed by v-src or v-abl. Overexpression of GAP by 110-fold in NIH3T3 cells reduced the basal level of GTP complexed to Ras to 2.4%; upon challenge with PDGF, Ras was complexed to 6.6% GTP. These results indicate that PDGF receptor activation and tyrosine kinase-encoding oncogene products can stimulate Ras into the GTP complex and that GAP in intact mammalian cells can decrease the amount of GTP complexed to Ras.
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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/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Macrophage Colony-Stimulating Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotide Probes,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet-Derived Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ras GTPase-Activating Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
265
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pubmed:geneSymbol |
ras
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
20437-42
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:2122974-Animals,
pubmed-meshheading:2122974-Base Sequence,
pubmed-meshheading:2122974-Cell Line,
pubmed-meshheading:2122974-GTP-Binding Proteins,
pubmed-meshheading:2122974-GTPase-Activating Proteins,
pubmed-meshheading:2122974-Gene Expression,
pubmed-meshheading:2122974-Genes, ras,
pubmed-meshheading:2122974-Guanine Nucleotides,
pubmed-meshheading:2122974-Guanosine Diphosphate,
pubmed-meshheading:2122974-Guanosine Triphosphate,
pubmed-meshheading:2122974-Kinetics,
pubmed-meshheading:2122974-Macrophage Colony-Stimulating Factor,
pubmed-meshheading:2122974-Mice,
pubmed-meshheading:2122974-Molecular Sequence Data,
pubmed-meshheading:2122974-Oligonucleotide Probes,
pubmed-meshheading:2122974-Platelet-Derived Growth Factor,
pubmed-meshheading:2122974-Protein Binding,
pubmed-meshheading:2122974-Protein-Tyrosine Kinases,
pubmed-meshheading:2122974-Proteins,
pubmed-meshheading:2122974-ras GTPase-Activating Proteins
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pubmed:year |
1990
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pubmed:articleTitle |
Modulation of guanine nucleotides bound to Ras in NIH3T3 cells by oncogenes, growth factors, and the GTPase activating protein (GAP).
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pubmed:affiliation |
Department of Molecular Biology, Merck, Sharp and Dohme Research Laboratories, West Point, Pennsylvania 19486.
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pubmed:publicationType |
Journal Article
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