Receptor characteristics of specific estrogen binding in the renal adenocarcinoma of the golden hamster.
Linear sucrose gradient analyses reveal that all estrogen-induced and -dependent primary renal tumor cytosols examined contain an 8 S and variable amounts of 4 S receptor in low ionic buffer concentrations. Similar results were obtained with extracts of primary metastases of these tumors. Sucrose gradients containing high salt (0.4 M KCl) convert the 8 S receptor in both the hamster renal tumor and uterus to a 4 to 5 S complex. Scatchard plot analysis reveals that the renal tumor cytosol estradiol-receptor complex has a Ka of 1.7 X 10(9) M-1 and 9.2 X 10(-10) M binding sites. Competition for the tritiated 17beta-estradiol binding sites in the renal tumor was similar to that in the uterus with respect to estrogenic compounds. Nonestrogenic steroids exhibited minimal competition at the same concentrations or higher. Substitution in the ring structure, particularly in position 3 of the phenolic A-ring, resulted in a considerable loss in the ability of such compounds to compete for these receptors. Aniestrogens were effective competitors for these estrogen receptors only at higher concentrations relative to the tritiated estradiol.
D000230:Adenocarcinoma / Q000378:metabolism*; D000818:Animals; D001667:Binding, Competitive; D002369:Castration; D006224:Cricetinae; D004958:Estradiol / Q000378:metabolism; D004967:Estrogens / Q000378:metabolism*; D005260:Female; D007680:Kidney Neoplasms / Q000378:metabolism*; D008297:Male; D009374:Neoplasms, Experimental / Q000378:metabolism; D011485:Protein Binding; D011956:Receptors, Cell Surface; D014599:Uterus / Q000378:metabolism
D004967:Estrogens; D011956:Receptors, Cell Surface; D004958:Estradiol