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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1987-8-10
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pubmed:abstractText |
The interaction of 5 alpha-dihydrotestosterone-receptor complexes with purified DNA fragments representing upstream, coding and intervening sequences of the prostate binding protein C3(1) gene was investigated using a DNA-cellulose competition binding assay. The partially purified androgen-receptor complexes which were used in the assay had proven DNA-binding capabilities. Two fragments were identified with relatively high affinity for androgen-receptor complexes. A 300 bp fragment extending from -220 to +80 and a 500 bp fragment derived entirely from the first intron consistently competed most effectively in the system. The presence of a high affinity site or sites in or near the promoter region of the gene is consistent with current models of transcriptional activation of hormone-responsive genes by steroid receptors. High affinity sites for steroid receptors within introns may indicate a role for receptors in regulation of transcription at other stages, or in post-transcriptional modification.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0303-7207
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
51
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
259-65
|
pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:3036627-Androgens,
pubmed-meshheading:3036627-Animals,
pubmed-meshheading:3036627-Binding, Competitive,
pubmed-meshheading:3036627-Cattle,
pubmed-meshheading:3036627-DNA,
pubmed-meshheading:3036627-DNA Restriction Enzymes,
pubmed-meshheading:3036627-Genes,
pubmed-meshheading:3036627-Receptors, Androgen,
pubmed-meshheading:3036627-Transcription, Genetic
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pubmed:year |
1987
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pubmed:articleTitle |
Androgen receptor-binding regions of an androgen-responsive gene.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|