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胰岛素对3T3-L1细胞中FA和酪蛋白激酶II的刺激作用。

Stimulation of FA and casein kinase II by insulin in 3T3-L1 cells.

作者信息

Villa-Moruzzi E, Crabb J W

机构信息

Dipartimento di Biomedicina Sperimentale, Universita' di Pisa, Italy.

出版信息

Biochem Biophys Res Commun. 1991 Jun 28;177(3):1019-24. doi: 10.1016/0006-291x(91)90640-s.

Abstract

Insulin stimulates protein phosphatase-1 and FA, assayed as phosphatase-1 activator, in 3T3-L1 cells. Since other kinases, such as casein kinase-II may also contribute to such FA activity, we assayed casein kinase-II and FA as peptide kinase on extracts from 3T3-L1 cells that had been exposed to insulin for various times. Under such conditions FA, assayed as phosphatase-1 activator, was stimulated 2-3-fold within 1-2 min. Casein kinase-II was stimulated about 2-fold but at a slightly later time (2-3 min) than FA, making it unlikely that casein kinase-II contributes to FA stimulation. Insulin slightly stimulated also the kinase activity of FA towards a synthetic peptide at 2 min, thus confirming the FA activation seen when FA was assayed as activator of phosphatase-1.

摘要

胰岛素可刺激3T3-L1细胞中的蛋白磷酸酶-1和脂肪酸(FA,作为磷酸酶-1激活剂进行测定)。由于其他激酶,如酪蛋白激酶-II也可能对这种脂肪酸活性有作用,我们在已暴露于胰岛素不同时间的3T3-L1细胞提取物上,将酪蛋白激酶-II和脂肪酸作为肽激酶进行了测定。在这种条件下,作为磷酸酶-1激活剂测定的脂肪酸在1-2分钟内被刺激了2-3倍。酪蛋白激酶-II被刺激了约2倍,但比脂肪酸稍晚(2-3分钟),这使得酪蛋白激酶-II不太可能对脂肪酸刺激有作用。胰岛素在2分钟时也略微刺激了脂肪酸对合成肽的激酶活性,从而证实了将脂肪酸作为磷酸酶-1激活剂测定时所观察到的脂肪酸激活。

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