rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
5070
|
pubmed:dateCreated |
1992-9-4
|
pubmed:abstractText |
Serum and growth factors can increase the proportion of Ras in the active guanosine triphosphate (GTP)-bound form. Growth factors might stimulate guanine nucleotide exchange or decrease the activity of the guanosine triphosphatase-activating proteins GAP and neurofibromin (NF1). In NIH 3T3 cells that overexpress the mutant Ras protein His116, which releases bound guanine nucleotide at a constitutively high rate and retains sensitivity to GAP and NF1, the proportion of GTP bound to the His116 protein was not altered by serum or platelet-derived growth factor. However, these mitogens increased the proportion of Ras in the GTP-bound form in cells that overexpressed control Ras proteins with a normal intrinsic rate of guanine nucleotide release. The amount of GTP-bound His116 or control Ras proteins was higher in cells at low density than in cells at high density, which have more GAP-like activity. The lower proportion of GTP-bound Ras in NIH 3T3 cells at high density may result from increased GAP-like activity. By contrast, serum and platelet-derived growth factors appear to stimulate guanine nucleotide exchange.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
0036-8075
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
31
|
pubmed:volume |
257
|
pubmed:geneSymbol |
c-ras
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
671-4
|
pubmed:dateRevised |
2007-3-19
|
pubmed:meshHeading |
pubmed-meshheading:1496380-3T3 Cells,
pubmed-meshheading:1496380-Animals,
pubmed-meshheading:1496380-Blood,
pubmed-meshheading:1496380-Cell Line, Transformed,
pubmed-meshheading:1496380-Fibroblasts,
pubmed-meshheading:1496380-GTPase-Activating Proteins,
pubmed-meshheading:1496380-Gene Expression,
pubmed-meshheading:1496380-Genes, ras,
pubmed-meshheading:1496380-Growth Substances,
pubmed-meshheading:1496380-Guanosine Triphosphate,
pubmed-meshheading:1496380-Histidine,
pubmed-meshheading:1496380-Methionine,
pubmed-meshheading:1496380-Mice,
pubmed-meshheading:1496380-Mutagenesis,
pubmed-meshheading:1496380-Neurofibromin 1,
pubmed-meshheading:1496380-Platelet-Derived Growth Factor,
pubmed-meshheading:1496380-Proteins,
pubmed-meshheading:1496380-Proto-Oncogene Proteins p21(ras),
pubmed-meshheading:1496380-Signal Transduction,
pubmed-meshheading:1496380-ras GTPase-Activating Proteins
|
pubmed:year |
1992
|
pubmed:articleTitle |
Mechanistic aspects of signaling through Ras in NIH 3T3 cells.
|
pubmed:affiliation |
Laboratory of Cellular Oncology, National Cancer Institute, Bethesda, MD 20892.
|
pubmed:publicationType |
Journal Article
|