Response to Treatment in Patients with Partial Androgen Insensitivity due to Mutations in the DNA-Binding Domain of the Androgen Receptor

2000 ◽  
Vol 53 (2) ◽  
pp. 83-88 ◽  
Author(s):  
Yvonne Lundberg Giwercman ◽  
Andrej Nikoshkov ◽  
Kristina Lindsten ◽  
Birgitta Byström ◽  
Åke Pousette ◽  
...  
Keyword(s):  
Androgen Receptor ◽  
Dna Binding ◽  
Binding Domain ◽  
Response To Treatment ◽  
Dna Binding Domain ◽  
Androgen Insensitivity

Androgen Insensitivity Syndrome in a Family of Warmblood Horses Caused by a 25-bp Deletion of the DNA-Binding Domain of the Androgen Receptor Gene

2017 ◽  
Vol 11 (1) ◽  
pp. 40-45 ◽  
Author(s):  
G. Eastman Welsford ◽  
Rikke Munk ◽  
Daniel A.F. Villagómez ◽  
Poul Hyttel ◽  
W. Allan King ◽  
...  
Keyword(s):  
Androgen Receptor ◽  
Dna Binding ◽  
Receptor Gene ◽  
Androgen Receptor Gene ◽  
Androgen Insensitivity Syndrome ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Androgen Insensitivity

Androgen insensitivity syndrome due to new mutations in the DNA-binding domain of the androgen receptor

1996 ◽  
Vol 120 (1) ◽  
pp. 15-24 ◽  
Author(s):  
Kyosuke Imasaki ◽  
Taijiro Okabe ◽  
Hiroshi Murakami ◽  
Yoko Tanaka ◽  
Masafumi Haji ◽  
...  
Keyword(s):  
Androgen Receptor ◽  
Dna Binding ◽  
Androgen Insensitivity Syndrome ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Androgen Insensitivity ◽  
New Mutations

A mutant androgen receptor from patients with Reifenstein syndrome: identification of the function of a conserved alanine residue in the D box of steroid receptors

1993 ◽  
Vol 13 (12) ◽  
pp. 7850-7858
Author(s):  
F Kaspar ◽  
H Klocker ◽  
A Denninger ◽  
A C Cato
Keyword(s):  
Androgen Receptor ◽  
Dna Binding ◽  
Steroid Receptors ◽  
Regulatory Elements ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Wild Type ◽  
Binding Studies ◽  
Mutant Receptor ◽  
Alanine Residue

Reifenstein syndrome is an eponymic term that describes partial androgen-insensitive disorders. Androgen receptor isolated from five patients with this syndrome contains a specific mutation in the DNA binding domain of the receptor. This mutation converts an alanine to a threonine at position 596 next to the zinc catenation site at the second finger. The threonine 596 mutant receptor mediated normal androgen response at promoters with closely positioned multiple regulatory elements for the androgen receptor and other transcription factors. Promoters with single isolated androgen response elements were not transactivated by the mutant receptor. In in vitro receptor-DNA binding studies, interaction with DNA by the mutant receptor was achieved only in the presence of an anti-androgen receptor antibody. Exchanging alanine 596 in the wild-type androgen receptor with serine or valine produced mutants with properties indistinguishable from those of the naturally occurring threonine 596 mutant receptor. These results indicate that an alanine residue at position 596 contributes important structural and functional activities to the androgen receptor. In the androgen receptor from the patients with Reifenstein syndrome, in which this alanine is converted to a threonine, wild-type receptor properties can be restored by exchanging an additional threonine at position 602 to an alanine. An alanine residue at position 596 or 602 in the DNA binding domain of the androgen receptor is therefore important for the full function of this receptor. In all steroid receptors that bind the core sequence AGAACANNNTGTTCT, an alanine residue is also present at a position equivalent to alanine 596 in the androgen receptor.

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