期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1981
卷号：78
期号：12
页码：7431-7435
DOI：10.1073/pnas.78.12.7431
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The binding of corticotropin (ACTH) to receptors on isolated rat adrenocortical cells was investigated with the aid of [[125I]ITyr23, Phe2, Nle4]ACTH-(1-38) (125I-ACTH analog) which retained full biological potency and had a specific radioactivity of 1800 +/- 75 Ci/mmol. Binding was highly specific to adrenocortical cells, and the radioactive peptide was displaced by low concentrations of ACTH but not by other basic peptides. Binding was rapid, reversible, and linearly related to the number of cells. 125I-ACTH analog was not significantly degraded by incubation with the cells at 23 degrees C for 1 hr. Scatchard analysis of the binding was compatible with a single class of binding sites with Kd = 1.41 +/- 0.21 nM, and the number of sites was estimated to be 3840 +/- 1045 per cell. The binding curve was superimposable on the concentration-response curve for cyclic AMP. Small, but significant amounts of 125I-ACTH analog were bound at concentrations sufficient for maximal stimulation of steroidogenesis. For a series of ACTH analogs, the concentrations of the peptides required for half-maximal stimulation of cyclic AMP production were in excellent agreement with the concentration required for half-maximal inhibition of binding. These results suggest that the adrenocortical cells contain only one class of ACTH receptors and that stimulation of a small fraction of these receptors (less than 3%) is sufficient for maximal steroidogenesis.
