Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1990-2-28
pubmed:abstractText
Androgen receptor heterogeneity and phosphorylation were studied in the human LNCaP cell line. Fluorography after photoaffinity labeling as well as immunoblotting with a specific polyclonal antibody revealed that the human androgen receptor migrated as a closely spaced 110 kD doublet on SDS-polyacrylamide gels. A time-dependent change in the ratio between the two isoforms was not observed after R1881 treatment of intact cells. In nuclear extracts of LNCaP cells that were incubated with [32P]orthophosphate in the presence of 10 nM R1881, a 110 kD phosphorylated protein was demonstrated after immunopurification using a monoclonal antibody against the human androgen receptor. Only a very small amount of this phosphoprotein was detected in the nuclear fraction from cells not treated with R1881. These results indicate that the human androgen receptor in LNCaP cells can be phosphorylated.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
166
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
193-200
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Androgen receptor heterogeneity and phosphorylation in human LNCaP cells.
pubmed:affiliation
Department of Biochemistry II, Erasmus University Rotterdam, The Netherlands.
pubmed:publicationType
Journal Article