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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1990-2-13
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pubmed:abstractText |
In Ehrlich ascites tumor cells maintained in serum-free medium for 16 h the rate of protein synthesis was about 50% of the rate in control (well-fed) cells. The addition of 10% calf serum led to a 1.5- to 2-fold stimulation of protein synthesis within 10 min. Stimulation was effected through a non-transcriptional mechanism which operated at the level of polypeptide chain initiation. The effect was due to non-dialyzable serum growth factors which were sensitive to treatment with dithiothreitol and iodoacetamide. Replacing the 16-h-conditioned serum-free medium with fresh serum-free medium stimulated protein synthesis about 30% in serum-deprived cells, and the effect of these low molecular weight nutrients was additive with the effect of serum factors. Phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF-2 alpha) inhibits protein synthesis by competitively inhibiting the guanine nucleotide exchange factor (GEF), and modulation of the extent of phosphorylation of eIF-2 alpha has been suggested as a probable regulatory mechanism in serum-deprived mammalian cells. We measured the ratio of phosphorylated to total eIF-2 alpha in serum-deprived cells. The ratio was elevated in serum-deprived cells compared to control (serum-fed) cells. eIF-2 was rapidly dephosphorylated in response to serum refeeding and returned to near control levels after 10 min. The rapidity of this response and the close temporal correlation between eIF-2 dephosphorylation and increased rate of protein synthesis provide evidence that eIF-2 plays an important role in the regulation of protein synthesis by serum growth factors.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media,
http://linkedlifedata.com/resource/pubmed/chemical/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/Dithiothreitol,
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-2,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Iodoacetamide,
http://linkedlifedata.com/resource/pubmed/chemical/Leucine,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
1014
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
282-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2605256-Animals,
pubmed-meshheading:2605256-Blood,
pubmed-meshheading:2605256-Carcinoma, Ehrlich Tumor,
pubmed-meshheading:2605256-Culture Media,
pubmed-meshheading:2605256-Disulfides,
pubmed-meshheading:2605256-Dithiothreitol,
pubmed-meshheading:2605256-Eukaryotic Initiation Factor-2,
pubmed-meshheading:2605256-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:2605256-Iodoacetamide,
pubmed-meshheading:2605256-Kinetics,
pubmed-meshheading:2605256-Leucine,
pubmed-meshheading:2605256-Phosphorylation,
pubmed-meshheading:2605256-Protein Biosynthesis,
pubmed-meshheading:2605256-Proteins,
pubmed-meshheading:2605256-Tumor Cells, Cultured
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pubmed:year |
1989
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pubmed:articleTitle |
Serum growth factors cause rapid stimulation of protein synthesis and dephosphorylation of eIF-2 in serum deprived Ehrlich cells.
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pubmed:affiliation |
University of Rochester Cancer Center, Department of Biochemistry, NY.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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