Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1994-5-23
|
| pubmed:abstractText |
We describe different single-amino acid aberrations in the DNA-binding domain (DBD) of the human androgen receptor (hAR) in three families with complete androgen insensitivity. No additional alteration was found in the translated portion of each mutant gene. In one family, an in-frame 3 nt deletion removes codon 581-(or 582) and, thereby, one of two phenylalanines that invariably occupy adjacent positions in the N-terminal alpha-helical region of the DBD in the steroid/thyroid/vitamin D receptor superfamily. In the second, an in-frame 3 nt loss deletes Arg614, an invariant residue in the C-terminal alpha-helix of the DBD. In the third, a G-->A transition causes Arg614His. Following transient transfection of COS cells with each mutant AR plasmid, there is a normal concentration of specific androgen-binding activity that has a reduced ability to bind two types of androgen response element (ARE), and to transregulate an androgen-responsive human growth hormone reporter gene. In genital skin fibroblasts with delta Phe581 or Arg614His, androgen-binding, AR protein and AR mRNA are markedly reduced; in gonadal fibroblasts with delta Arg614, AR mRNA may be reduced. Our data substantiate the primary contributions of Phe581 and Arg614 to normal hAR-ARE binding, and expose important secondary effects of the mutations affecting each residue.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Codon,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylalanine,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Androgen
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0964-6906
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
3
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
21-7
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8162033-Amino Acid Sequence,
pubmed-meshheading:8162033-Animals,
pubmed-meshheading:8162033-Base Sequence,
pubmed-meshheading:8162033-Blotting, Western,
pubmed-meshheading:8162033-Cell Line,
pubmed-meshheading:8162033-Cells, Cultured,
pubmed-meshheading:8162033-Codon,
pubmed-meshheading:8162033-DNA Primers,
pubmed-meshheading:8162033-DNA-Binding Proteins,
pubmed-meshheading:8162033-Exons,
pubmed-meshheading:8162033-Female,
pubmed-meshheading:8162033-Fibroblasts,
pubmed-meshheading:8162033-Humans,
pubmed-meshheading:8162033-Infant,
pubmed-meshheading:8162033-Male,
pubmed-meshheading:8162033-Molecular Sequence Data,
pubmed-meshheading:8162033-Mutagenesis, Site-Directed,
pubmed-meshheading:8162033-Phenylalanine,
pubmed-meshheading:8162033-Point Mutation,
pubmed-meshheading:8162033-Polymerase Chain Reaction,
pubmed-meshheading:8162033-Protein Structure, Secondary,
pubmed-meshheading:8162033-RNA, Messenger,
pubmed-meshheading:8162033-Receptors, Androgen,
pubmed-meshheading:8162033-Sequence Deletion,
pubmed-meshheading:8162033-Skin,
pubmed-meshheading:8162033-Transfection
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Complete androgen insensitivity due to mutations in the probable alpha-helical segments of the DNA-binding domain in the human androgen receptor.
|
| pubmed:affiliation |
Lady Davis Institute, Sir Mortimer B. Davis-Jewish General Hospital, Montreal, Quebec, Canada.
|
| pubmed:publicationType |
Journal Article,
Case Reports,
Research Support, Non-U.S. Gov't
|