TY - JOUR
T1 - Human androgen receptor expressed in HeLa cells activates transcription in vitro
AU - De Vos, Piet
AU - Schmitt, Jacky
AU - Verhoeven, Guido
AU - Stunnenberg, Hendrik G.
N1 - Funding Information:
The authors wish to thank Dr D.Huylebroeck (Celgen, University of Leuven) for the use of the Vaccinia facility in his laboratory and for his helpful suggestions in the development of the Vaccinia system. We thank Prof. W.Heyns and Prof. W.Rombauts for their helpful discussions. We are grateful to Vera Sonntag-Buck and to Liset Beek for excellent assistance in tissue culture. The AR antiserum was kindly provided by M.Esquenet and Prof. W.Heyns. This research was supported by a grant 'Geconcerteerde Onderzoeksactie van de Vlaamse gemeenschap' and by grant 3.0048.94 from the 'Nationaal Fonds voor Wetenschappelijk Onderzoek van Belgie". Piet De Vos received a short term fellowship from the European Molecular Biology Organization.
PY - 1994/4/11
Y1 - 1994/4/11
N2 - The androgen receptor (AR) is a ligand-responsive transcription factor, belonging to the class of steroid receptors. AR mutations have been associated with various X-llnked diseases, characterized by complete or partial resistance to androgens. To further analyse the molecular mechanism of action of the AR, we have produced the human AR in HeLa cells with a Vaccinia virus expression system. Binding studies on infected HeLa cells demonstrate that the recombinant AR interacts specifically and with high affinity with natural and synthetic androgens. In a gel retardation assay the partially purified AR specifically recognizes an androgen response element of the rat prostatic binding protein gene. Moreover, the recombinant AR activates transcription in vitro from a synthetic promoter construct containing glucocortlcold response elements (GRE).
AB - The androgen receptor (AR) is a ligand-responsive transcription factor, belonging to the class of steroid receptors. AR mutations have been associated with various X-llnked diseases, characterized by complete or partial resistance to androgens. To further analyse the molecular mechanism of action of the AR, we have produced the human AR in HeLa cells with a Vaccinia virus expression system. Binding studies on infected HeLa cells demonstrate that the recombinant AR interacts specifically and with high affinity with natural and synthetic androgens. In a gel retardation assay the partially purified AR specifically recognizes an androgen response element of the rat prostatic binding protein gene. Moreover, the recombinant AR activates transcription in vitro from a synthetic promoter construct containing glucocortlcold response elements (GRE).
UR - https://www.scopus.com/pages/publications/0028227479
U2 - 10.1093/nar/22.7.1161
DO - 10.1093/nar/22.7.1161
M3 - Article
C2 - 8165128
AN - SCOPUS:0028227479
SN - 0305-1048
VL - 22
SP - 1161
EP - 1166
JO - Nucleic acids research
JF - Nucleic acids research
IS - 7
ER -