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Trans-repression of human glucocorticoid receptor expression by transcription factor GRF-1
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Control of transcription of responsive genes by steroid hormones is mediated by receptor proteins. Steroid receptors belong to a family of ligand dependent trans-acting regulatory proteins. The cellular glucocorticoid receptor concentration is modulated by a number of factors including glucocorticoids which down-regulates their own receptor concentration. Using human glucocorticoid receptor gene fused to bacterial chloramphenicol acetyltransferase and clonal human glucocorticoid receptor cDNA in an expression vector, we have directly demonstrated the receptor mediated down regulatory events. Furthermore, we have purified, from human MCF-7 cells a protein factor (GRF-1) that binds to the hGR gene promoter, cloned the cDNA corresponding to …

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Human androgen receptor trans-activation
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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. …

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Human androgen receptor trans-activation
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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. …

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Human androgen receptor trans-activation
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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. …

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pen icon Colloque
Human androgen receptor trans-activation
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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. …

quote
pen icon Colloque
Human androgen receptor trans-activation
quote

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. …

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