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培养的内皮细胞中的蛋白质磷酸化

Protein phosphorylation in cultured endothelial cells.

作者信息

Mackie K, Lai Y, Nairn A C, Greengard P, Pitt B R, Lazo J S

出版信息

J Cell Physiol. 1986 Sep;128(3):367-74. doi: 10.1002/jcp.1041280304.

Abstract

We have investigated the protein phosphorylation systems present in cultured bovine aortic and pulmonary artery endothelial cells. The cells contain cyclic AMP-dependent protein kinase, three calcium/calmodulin-dependent protein kinases, protein kinase C, and at least one tyrosine kinase. No cyclic GMP-dependent protein kinase activity was found. The cells also contained numerous substrates for cyclic AMP-dependent protein kinase and protein kinase C. Fewer substrates were found for the calcium/calmodulin-dependent protein kinases. There was little difference between either protein kinase activities or substrates when pulmonary artery endothelium was compared to aortic endothelium grown under similar culture conditions. It is likely that these various protein kinases and their respective substrate proteins are involved in mediating several of the actions of the hormones and drugs which affect the vascular endothelium.

摘要

我们研究了培养的牛主动脉和肺动脉内皮细胞中存在的蛋白质磷酸化系统。这些细胞含有环磷酸腺苷(cAMP)依赖性蛋白激酶、三种钙/钙调蛋白依赖性蛋白激酶、蛋白激酶C和至少一种酪氨酸激酶。未发现环磷酸鸟苷(cGMP)依赖性蛋白激酶活性。这些细胞还含有许多cAMP依赖性蛋白激酶和蛋白激酶C的底物。钙/钙调蛋白依赖性蛋白激酶的底物较少。在相似培养条件下生长的肺动脉内皮与主动脉内皮相比,蛋白激酶活性或底物之间几乎没有差异。这些不同的蛋白激酶及其各自的底物蛋白可能参与介导影响血管内皮的几种激素和药物的作用。

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