Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
13
|
pubmed:dateCreated |
1993-6-4
|
pubmed:abstractText |
Insulin induces the serine phosphorylation of the nucleolar protein nucleolin at subnanomolar concentrations in differentiated 3T3-442A cells. The stimulation is biphasic with phosphorylation reaching a maximum at 10 pM insulin and then declining to only 40% of basal levels at insulin concentrations of 1 microM. These changes are rapid, reaching half-maximal after 4 min and maximal after 15 min of incubation. The cell-permeable casein kinase II inhibitor 5,6-dichlorobenzimidazole-riboside prevents the insulin-stimulated phosphorylation of nucleolin suggesting that casein kinase II may mediate this effect of the hormone. Insulin-like growth factor 1 mimics the action of insulin on dephosphorylation of nucleolin at nanomolar concentrations suggesting that the latter effect may be mediated by insulin-like growth factor 1 receptors. Insulin treatment of 3T3-442A cells also results in a stimulation of RNA efflux from isolated, intact cell nuclei. The dose dependence of insulin-induced nucleolin phosphorylation and insulin-stimulated RNA efflux from intact cell nuclei are almost identical. Insulin induces an increase in the RNA efflux at subnanomolar concentrations in 3T3-442A adipocytes, while high (micromolar) concentrations of insulin inhibited the efflux of RNA. These data indicate that insulin regulates the phosphorylation/dephosphorylation of nucleolin, possibly via stimulation of casein kinase II, and this may play a role in regulation of the RNA efflux from nuclei.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphorus Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/nucleolin
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
5
|
pubmed:volume |
268
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
9747-52
|
pubmed:dateRevised |
2011-11-17
|
pubmed:meshHeading |
pubmed-meshheading:7683660-3T3 Cells,
pubmed-meshheading:7683660-Amino Acids,
pubmed-meshheading:7683660-Animals,
pubmed-meshheading:7683660-Cell Differentiation,
pubmed-meshheading:7683660-Cell Nucleus,
pubmed-meshheading:7683660-DNA-Binding Proteins,
pubmed-meshheading:7683660-Dose-Response Relationship, Drug,
pubmed-meshheading:7683660-Insulin,
pubmed-meshheading:7683660-Kinetics,
pubmed-meshheading:7683660-Mice,
pubmed-meshheading:7683660-Nuclear Proteins,
pubmed-meshheading:7683660-Phosphates,
pubmed-meshheading:7683660-Phosphoproteins,
pubmed-meshheading:7683660-Phosphorus Radioisotopes,
pubmed-meshheading:7683660-Phosphorylation,
pubmed-meshheading:7683660-RNA,
pubmed-meshheading:7683660-RNA-Binding Proteins,
pubmed-meshheading:7683660-Time Factors
|
pubmed:year |
1993
|
pubmed:articleTitle |
Insulin induces the phosphorylation of nucleolin. A possible mechanism of insulin-induced RNA efflux from nuclei.
|
pubmed:affiliation |
Research Division, Joslin Diabetes Center, Boston, Massachusetts 02215.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|