In vitro transformation of androgen receptor from murine skeletal muscle by cAMP.
Sedimentation constants and DNA-cellulose-binding of cytosolic androgen receptor from murine skeletal muscle were determined in presence of cyclic nucleotides. Without cAMP, two testosterone-binding fractions of similar amount at 4-5S and 8-9S were obtained. With 3 microM cAMP the receptor sedimented predominantly at 4-5S. Binding of testosterone-receptor-complexes to DNA-cellulose was enhanced by increasing cAMP-concentrations and reached a maximum at 20-90 nM cAMP depending on the DNA-concentrations in the test. A similar DNA-binding characteristic was obtained after partial purification of the receptor by affinity chromatography. cGMP had no effect. We conclude that the androgen receptor is transformed in vitro by cAMP.
D000818:Animals; D002846:Chromatography, Affinity; D000242:Cyclic AMP / Q000378:metabolism*; D003600:Cytosol / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism*; D008297:Male; D051379:Mice; D009132:Muscles / Q000378:metabolism*; D011944:Receptors, Androgen / Q000302:isolation & purification / Q000378:metabolism*; D013739:Testosterone / Q000378:metabolism
D004268:DNA-Binding Proteins; D011944:Receptors, Androgen; D013739:Testosterone; D000242:Cyclic AMP