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Corticotropin positively regulates its own receptors and cyclic amp response in cultured bovine adrenal cells



Corticotropin positively regulates its own receptors and cyclic amp response in cultured bovine adrenal cells



Proceedings of the National Academy of Sciences of the United States of America 86(13): 4977-4981



Bovine fasciculata adrenal cells contain specific high-affinity (KD .apprxeq. 2.3 .+-. 0.4 .times. 10-10 M) and low-capacity (1910 .+-. 300 sites per cell) corticotropin (ACTH) receptors. Pretreatment of cells with ACTH, caused in a time- (maximum effect at 48 hr) and dose- (ED50 .apprxeq. 10-11 M, Vmax = 10-10 to 10-9 M) dependent manner an increase in ACTH binding. This was due to a 4-fold increase in the number of binding sites without modification of the binding affinity. The same pretreatment also enhanced the cAMP response to further ACTH stimulation in a dose-dependent manner (ED50 .apprxeq. 10-11 M) and to a lesser extent the response to forskolin. However, pretreatment with higher concentrations of ACTH (10-8 M) reduced the binding and the cAMP response when compared to the effect of 10-9 M. These ACTH effects, which were mimicked by 8-bromoadenosine 3',5'-cyclic monophosphate, required de novo protein synthesis. Pretreatment with 10-13 to 10-11M ACTH also enhanced the steroidogenic responsiveness to further hormonal stimulation. However, at higher concentrations the hormone induced an apparent steroidogenic desensitization that was probably related to a depletion of endogenous cholesterol, since cortisol production in the presence of 22-(R)-hydroxycholesterol was increased. Neither angiotensin-II nor atrial natriuretic factor alone modified ACTH receptors, but angiotensin II partially blocked the stimulatory effect of ACTH. Thus, ACTH is one of the few polypeptide hormones having a positive trophic effect on its own receptors and target-cell responsiveness.

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