Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5953
pubmed:dateCreated
1984-4-2
pubmed:abstractText
According to the current model of steroid hormone action oestrogen is thought to bind to its receptor in the cytoplasm of target cells and the oestrogen-receptor complex is then translocated into the nucleus. This model is based on evidence obtained in homogenized cell preparations in which free receptor is associated with the cytosol, whereas steroid-bound receptor is associated with the nuclear fraction. Some data suggest, however, that the unfilled receptor may reside in the nucleus, and that cytosolic localization represents an extraction artefact. We have now reinvestigated the subcellular distribution of unfilled oestrogen receptor using cytochalasin B-induced enucleation to obtain cytoplast and nucleoplast fractions from receptor-containing GH3 cells derived from rat pituitary tumours. We found that cytoplasts prepared from GH3 cells contain little oestrogen-binding activity and that most of the unfilled oestrogen receptors are associated with the nuclear fraction. We therefore suggest that the standard model is in error and that the unoccupied receptor is nuclear in the intact cell.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:volume
307
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
747-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:articleTitle
Nuclear localization of unoccupied oestrogen receptors.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't