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Human androgen receptor trans-activation

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Steve Leclerc
Rathanaswami Rajanikanth
Francois Pottiers
Manjappa V. Govinda
Shafali Pillay
BX

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Résumé du colloque

A second human androgen receptor cDNA clone (hARb) encoding an identical amino terminal and DNA binding domains, but differing by four amino acids at the hormone binding domain, did not bind [3H]DHT with high affinity when incubated with protein expressed by in vitro transcription-translation. Co-transfection of hARa in an expression vector with mouse mammary tumor virus (MMTV)-bacterial chloramphenical acetyltransferase (CAT) chimeric plasmids, followed a hormone-dependent trans-activation, defining the binding affinity of hARa between 10^-9 M and 1 x 10^-8 M for [3H]DHT. A similar co-transfection experiment with hARb indicated a Kd of hARb for [3H]DHT to be above 10^-8 M. The amino acid sequence changes at the Gly stretch (16 Gly instead of 22 or 23) of the N-terminal domain gave hARb, the sequence reads L.F.F.F.F.E.L (816-822) instead of K.F.F.F.E.L.F (816-821) in the hARa and other receptor hAR sequences. The interaction of hARa and hARb with synthetic androgen responsive elements was examined and their responsiveness in trans-activation by actual phospho-acceptor prediction demonstrates that hARb can inhibit trans-activation by hARa in this system.

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Section :
Endocrinologie
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Endocrinologie
host icon Hôte : Université Laval

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