Siebenlist K R, Taketa F
J Biol Chem. 1983 Sep 25;258(18):11384-90.
Triethyltin bromide activates the cyclic AMP-dependent protein kinases of human red cell membranes and of bovine brain. Additions of 25-500 microM triethyltin to red cell ghosts resulted in enhanced phosphorylation of ghost proteins. When added to partially purified cyclic AMP-dependent protein kinases from red cell ghosts or bovine brain, stimulation of the phosphorylation of calf thymus histone was observed. The enhancement of kinase activity was due to release of catalytic subunits from the intact protein kinase. Brief exposure of the partially purified enzymes to triethyltin, followed by DE52 chromatography, resulted in elution profiles for regulatory and catalytic subunits that were similar to the profile resulting after cyclic AMP activation. Triethyltin interacts with both regulatory and catalytic subunits. When it was added to the partially purified cyclic AMP-dependent protein kinases from human red cell ghosts or bovine brain, noncompetitive inhibition of cyclic AMP binding to the regulatory subunit of the enzyme was observed. It interacted with the catalytic subunit to produce slow inhibition of catalytic activity. The inhibition was non-competitive with respect to both histone and ATP. When intact red cells were subjected to brief exposure with triethyltin, enhanced phosphorylation of certain membrane proteins occurred, suggesting that the activation of the cyclic AMP protein kinases by triethyltin may be physiologically significant.
溴化三乙锡可激活人红细胞膜和牛脑的环磷酸腺苷依赖性蛋白激酶。向红细胞血影中添加25 - 500微摩尔的溴化三乙锡会导致血影蛋白磷酸化增强。当添加到从红细胞血影或牛脑中部分纯化的环磷酸腺苷依赖性蛋白激酶中时，可观察到小牛胸腺组蛋白磷酸化受到刺激。激酶活性的增强是由于完整蛋白激酶的催化亚基释放所致。将部分纯化的酶短暂暴露于溴化三乙锡，然后进行DE52层析，得到的调节亚基和催化亚基洗脱图谱与环磷酸腺苷激活后得到的图谱相似。溴化三乙锡与调节亚基和催化亚基均相互作用。当将其添加到从人红细胞血影或牛脑中部分纯化的环磷酸腺苷依赖性蛋白激酶中时，可观察到其对环磷酸腺苷与该酶调节亚基结合的非竞争性抑制作用。它与催化亚基相互作用，对催化活性产生缓慢抑制。这种抑制作用对组蛋白和ATP均无竞争性。当完整红细胞短暂暴露于溴化三乙锡时，某些膜蛋白的磷酸化增强，这表明溴化三乙锡对环磷酸腺苷蛋白激酶的激活可能具有生理意义。
