促肾上腺皮质激素1-24对牛肾上腺细胞微粒体环磷酸腺苷依赖性蛋白激酶同工酶I的激活作用。

Activation of microsomal cAMP-dependent protein kinase isoenzyme I by ACTH1-24 in bovine adrenal cells.

作者信息

Deviller P, Vallier P, Saez J M

出版信息

J Steroid Biochem. 1985 Aug;23(2):133-6. doi: 10.1016/0022-4731(85)90227-4.

Abstract

In microsomes of bovine fasciculata reticularis cells incubated with or without 10(-8) M ACTH during 20 min, we measured covalent and non covalent cAMP binding under exchange or non-exchange conditions and cAMP-kinase activity. ACTH induced a decrease in cAMP-kinase activity and in the number of free cAMP binding sites. These results indicate an activation by ACTH of a part of microsomal cAMP-dependent protein kinase. Photoaffinity labeling of microsomal protein with 8-azido-cAMP revealed the presence of both cAMP-kinase isoenzyme I and II in this cellular fraction. Using this method, it was demonstrated that ACTH1-24 caused a preferential and nearly complete activation of microsomal protein kinase I.

摘要

在与10⁻⁸ M促肾上腺皮质激素（ACTH）一起孵育20分钟或未孵育的牛束状带网状细胞微粒体中，我们在交换或非交换条件下测量了共价和非共价的环磷酸腺苷（cAMP）结合以及cAMP激酶活性。ACTH导致cAMP激酶活性和游离cAMP结合位点数量减少。这些结果表明ACTH激活了微粒体中一部分cAMP依赖性蛋白激酶。用8-叠氮基-cAMP对微粒体蛋白进行光亲和标记显示，在该细胞组分中同时存在cAMP激酶同工酶I和II。使用这种方法证明，促肾上腺皮质激素1-24优先且几乎完全激活了微粒体蛋白激酶I。