Abstract:
:In the present study, we characterized two new SF-1 binding sites, SF-209 and SF-98, in the promoter of the human ACTH receptor (hACTH-R) gene. Both sites, together with the previously described SF-35 site, are required for full constitutive activity of this gene. This was demonstrated by the use of constructs containing part of the promoter upstream of the luciferase gene and carrying mutation in one of these sites, to transiently transfect H295R cells. Mutations of either SF-35, SF-98, or SF-209 induced a decrease of luciferase activity. This effect was amplified when two or three elements were mutated together in the same construct. Only SF-35 and SF-98 seem to play a major role in the cAMP-induced regulation of the hACTH-R gene, since mutation of either one of these sites reduced the forskolin induction of luciferase activity by 50%. When both elements were mutated, no stimulation was obtained over the control. This indicates that SF-1 protein must bind to both sites for the cAMP response.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Naville D,Penhoat A,Durand P,Begeot Mdoi
10.1006/bbrc.1998.9891subject
Has Abstractpub_date
1999-02-05 00:00:00pages
28-33issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(98)99891-6journal_volume
255pub_type
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