Linked Life Data

18261979

Source:http://linkedlifedata.com/resource/pubmed/id/18261979

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2008-3-4
pubmed:abstractText
The glucocorticoid receptor (GR) forms part of a multiprotein complex consisting of chaperones and proteins active in glucocorticoid signaling and other pathways. By immunoaffinity purification of GR, followed by Edman sequencing and Western blotting, we identified the FMS-like tyrosine kinase 3 (Flt3) as a GR-interacting protein in rat liver and hepatoma cells. Flt3 interacts with both non-liganded and liganded GR. The DNA-binding domain of GR is sufficient for Flt3 interaction as shown by GST-pull down experiments. Studies of the effects of Flt3 and its ligand FL in glucocorticoid-driven reporter-gene assays in Cos7 cells, show that co-transfection with Flt3 and FL potentiates glucocorticoid effects. Treatment with FL had no effect on GR location and Dex induced translocation of GR was unaffected by FL. In summary, GR and Flt3 interact, affecting GR signaling. This novel cross-talk between GR and a hematopoietic growth factor might also imply glucocorticoid effects on Flt3-mediated signaling.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
11
pubmed:volume
368
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
569-74
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
FMS-like tyrosine kinase 3 interacts with the glucocorticoid receptor complex and affects glucocorticoid dependent signaling.
pubmed:affiliation
Department of Biosciences and Nutrition, Division of Medical Nutrition, Karolinska Institutet, NOVUM, S-141 86 Stockholm, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't