cAMP-dependent phosphorylation of nuclear proteins in mouse submandibular gland following testosterone administration.

The effect of androgen on protein kinase activities was studied in chromosomal proteins from female mouse submandibular gland. The protein kinase activities in the nuclei were stimulated 3 h after testosterone administration. The in vitro addition of cAMP in the nuclei resulted in the enhancement of the androgen-sensitive protein kinase activities. SDS-PAGE analysis revealed that nonhistone proteins having molecular weights of 20-30 kDa and around 43 kDa were phosphorylated after androgen treatment. The addition of cAMP stimulated phosphorylation of nonhistone proteins having molecular weights with 15-25 kDa, 30 kDa and 35 kDa and the intensity of phosphorylation of these nonhistone proteins was enhanced after androgen treatment. These results suggest that androgen-sensitive protein kinases including cAMP-dependent protein kinase were present and that phosphorylation of nonhistone proteins by these protein kinases may be involved in mediating androgen-induced gene activation.