Chapdelaine P, Guérin S, Tremblay R R, Dubé J Y
Laboratoire de Biorégulation Hormonale, Le Centre Hospitalier, Université Laval, Sante-Foy, Que., Canada.
FEBS Lett. 1992 Jun 1;303(2-3):117-20. doi: 10.1016/0014-5793(92)80501-7.
We have studied, by the gel mobility shift assay, the interaction of DNA binding proteins with a fragment of the proximal promoter (from nucleotides -177 to -47) of the androgen-regulated canine prostate arginine esterase gene. Several shifted bands were obtained using nuclear extracts from various tissues. In the case of the prostate, the intensity of some of the shifted bands was decreased or increased when the extracts were prepared from animals that had been castrated 12 days earlier. Several of the DNA-protein complexes could be assigned to an interaction with part or all of the sequence GGGGGTGGGGG from-124 to -114. We also obtained evidence for the presence of protein(s) interacting with an Sp1 motif present in the same fragment. These results suggest that some ubiquitous factors different from the androgen receptors could be involved in the regulation of the arginine esterase gene.
