Perchellet J P, Sharma R K
Endocrinology. 1979 Oct;105(4):879-83. doi: 10.1210/endo-105-4-879.
The decline of the ACTH-stimulated cGMP to the basal level in isolated adrenocortical carcinoma cells was inhibited by cyclic phosphodiesterase inhibitors. Time-course experiments showed that the ACTH-induced level of cGMP preceded the activation of phosphodiesterase. Cells incubated with increasing concentrations of exogenous cGMP responded with a corresponding increase in the cGMP-phosphodiesterase activity. cAMP was 100-fold less effective than cGMP in the activation of cGMP-phosphodiesterase, indicating the nucleotide specificity of enzyme activation. The activation of cGMP-phosphodiesterase by ACTH-induced cGMP or exogenous cGMP was rapid. In contrast to these observations, there was no activation of cAMP-phosphodiesterase by exogenous cAMP or cGMP. These results indicate that one mechanism by which isolated adrenocortical carcinoma cells regulate the ACTH-induced increase in cGMP is the cyclic nucleotide control of the activity of its phosphodiesterase, thereby regulating cGMP degradation.
环磷酯酶抑制剂可抑制促肾上腺皮质激素（ACTH）刺激的环磷酸鸟苷（cGMP）在分离的肾上腺皮质癌细胞中降至基础水平。时间进程实验表明，ACTH诱导的cGMP水平先于磷酸二酯酶的激活。用浓度不断增加的外源性cGMP孵育细胞，cGMP-磷酸二酯酶活性相应增加。在激活cGMP-磷酸二酯酶方面，环磷酸腺苷（cAMP）的效力比cGMP低100倍，表明酶激活具有核苷酸特异性。ACTH诱导的cGMP或外源性cGMP对cGMP-磷酸二酯酶的激活迅速。与这些观察结果相反，外源性cAMP或cGMP不会激活cAMP-磷酸二酯酶。这些结果表明，分离的肾上腺皮质癌细胞调节ACTH诱导的cGMP增加的一种机制是通过环核苷酸控制其磷酸二酯酶的活性，从而调节cGMP的降解。
