Linked Life Data

2668288

Source:http://linkedlifedata.com/resource/pubmed/id/2668288

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1989-9-13
pubmed:abstractText
The expression of the glucocorticoid receptor (GR) gene and the phosphorylation of the GR protein has been studied as a function of time after hormone addition to NIH 3T3 cells. We detected a ligand-induced decrease of GR gene expression at both the level of RNA and protein. GR mRNA declined to 25% of the control within 3 h of dexamethasone treatment and remained at this level for at least 24 h. GR protein was analyzed with a monospecific antiserum directed against the DNA- and hormone-binding domains of the rat GR synthesized in Escherichia coli. Pulse-chase experiments revealed a decrease in GR half-life from 8 h in the absence of hormone to 3 h following hormone treatment. Both effects resulted in a reduction of total GR protein to 20% as determined by quantitative immunoblotting. The level of the GR protein returned to that of untreated cells within 24 h after withdrawal of hormone. Furthermore, dexamethasone treatment led to a 3-4-fold increase in GR phosphorylation within 60 min. The glucocorticoid antagonist 17 beta-hydroxy-11 beta-(4-dimethylamino-phenyl)-17 alpha-(1-propynyl)-oestra-4,9-dien-3-one (RU 486) did not change the phosphorylation state of the receptor, but a down-regulation of the GR was still observed. These results suggest that ligand-dependent receptor phosphorylation is not involved in down-regulation of the GR but may be important in the transcriptional activation of hormone responsive genes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14396-402
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Down-regulation and phosphorylation of glucocorticoid receptors in cultured cells. Investigations with a monospecific antiserum against a bacterially expressed receptor fragment.
pubmed:affiliation
Friedrich Miescher-Institut, Basel, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't