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首页> 外文期刊>Neurochemistry International: The International Journal for the Rapid Publication of Critical Reviews, Preliminary and Original Research Communications in Neurochemistry >Stimulation of cyclic adenosine 3',5'-monophosphate-dependent protein kinase with brain gangliosides.
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Stimulation of cyclic adenosine 3',5'-monophosphate-dependent protein kinase with brain gangliosides.

机译：用神经节苷脂刺激环状腺苷3'，5'-单磷酸依赖性蛋白激酶。

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摘要

The holoenzyme of cAMP-dependent protein kinase (cAMP-kinase) partially purified from the particulate fraction of rat brain was stimulated by gangliosides. Among various gangliosides tested, GM1 was most potent, giving Ka value of 19.5 microM. The maximal activation of the kinase was obtained with 100 microM GM1 using kemptide as substrate. Gangliosides inhibited the kinase activity of the catalytic subunit of cAMP-kinase. Of various substrates tested, the ganglioside-stimulated cAMP-kinase could phosphorylate microtubule-associated protein 2, synapsin I and myelin basic protein, but not histone H1 and casein. The molecular mechanisms of the stimulatory effect of gangliosides were investigated. The kinase activated with GM1 was inhibited by the addition of PKItide, a specific inhibitor for cAMP-kinase. However, GM1 did not dissociate the holoenzyme into the catalytic and regulatory subunits and did not interfere with the binding ability of cAMP to the holoenzyme. These results suggest that the gangliosides can directly activate cAMP-kinase in a different manner from cAMP.
机译：从大鼠脑颗粒部分纯化的cAMP依赖性蛋白激酶（cAMP激酶）的全酶被神经节苷脂刺激。在测试的各种神经节苷脂中，GM1最有效，Ka值为19.5 microM。以kemptide为底物，使用100 microM GM1获得了激酶的最大活化。神经节苷脂抑制cAMP激酶催化亚基的激酶活性。在测试的各种底物中，神经节苷脂刺激的cAMP激酶可以磷酸化微管相关蛋白2，突触蛋白I和髓磷脂碱性蛋白，但不能磷酸化组蛋白H1和酪蛋白。研究了神经节苷脂刺激作用的分子机理。 GM1激活的激酶被PKItide（一种cAMP激酶的特异性抑制剂）的添加所抑制。但是，GM1不会将全酶解离成催化亚基和调节亚基，并且不会干扰cAMP与全酶的结合能力。这些结果表明神经节苷脂可以以不同于cAMP的方式直接激活cAMP激酶。

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