Corticotropin and angiotensin induce dephosphorylation of a Mr-20,000 protein in bovine adrenal cells.

ACTH (1-24) and Angiotensin II, both able to activate steroidogenesis in bovine fasciculata-reticularis cells, each reduced the [32P] incorporation in a cytosolic Mr-20,000 pI 6.8 protein in this cell. Cells preincubated with Sar1-Angiotensin prevented the effect of Angiotensin. Angiotensin 10(-8)M and ACTH 10(-10)M led to an almost complete disappearance of the corresponding radioactive spot on the autoradiograph. The effect was observed as soon as 2 minutes after addition of hormones to the cells. Other activators of steroidogenesis such as 8-bromocyclicAMP (8-BrcAMP), 4 beta-Phorbol-12 beta-Myristate-13 alpha-acetate (PMA) and [9-tryptophan (o-nitrophenylsulfenyl)] substituted ACTH (NPS-ACTH), also reduced the labeling of the Mr-20,000 polypeptide. On the other hand, this effect was not reproduced by insulin or human growth hormone (hGH). On 2-D gels from control, the coincidence of this polypeptide with phosphorylated myosin light chain was not observed. We suggest that the apparent dephosphorylation of this polypeptide may represent a common effect of all steroidogenic agents regardless of their seemingly distinct early actions.