Smiley R M, Paul S, Browning M D, Leibel R L, Hirsch J
Laboratory of Human Behavior and Metabolism, Rockefeller University, New York, NY 10021.
Life Sci. 1990;47(10):849-58. doi: 10.1016/0024-3205(90)90597-k.
The effect of adrenergic agents on protein phosphorylation in human adipocytes was examined. Freshly isolated human fat cells were incubated with 32PO4 in order to label intracellular ATP, then treated with a variety of adrenergic and other pharmacologic agents. Treatment with the beta-adrenergic agonist isoproterenol led to a significant increase in phosphate content of at least five protein bands (Mr 52, 53, 63, 67, 84 kDa). The increase in phosphorylation was partially inhibited by the alpha-2 agonist clonidine. Epinephrine, a combined alpha and beta agonist, was less effective at increasing phosphate content of the proteins than was isoproterenol. Neither insulin nor the alpha-1 agonist phenylephrine had any discernible effect on the pattern of protein phosphorylation. The 84 kDa phosphorylated peptide band appears to contain hormone-sensitive lipase, a key enzyme in the lipolytic pathway which is activated by phosphorylation. These results are somewhat different than previously reported results for rat adipocytes, and represent the first report of overall pattern and adrenergic modulation of protein phosphorylation in human adipocytes.
研究了肾上腺素能药物对人脂肪细胞中蛋白质磷酸化的影响。将新鲜分离的人脂肪细胞与32PO4一起孵育以标记细胞内ATP，然后用多种肾上腺素能药物和其他药理剂进行处理。用β-肾上腺素能激动剂异丙肾上腺素处理导致至少五条蛋白带（分子量52、53、63、67、84 kDa）的磷酸盐含量显著增加。α-2激动剂可乐定部分抑制了磷酸化的增加。肾上腺素是一种α和β联合激动剂，在增加蛋白质的磷酸盐含量方面比异丙肾上腺素效果差。胰岛素和α-1激动剂去氧肾上腺素对蛋白质磷酸化模式均无明显影响。84 kDa磷酸化肽带似乎含有激素敏感性脂肪酶，这是脂解途径中的一种关键酶，可通过磷酸化被激活。这些结果与先前报道的大鼠脂肪细胞的结果有些不同，并且是关于人脂肪细胞中蛋白质磷酸化的整体模式和肾上腺素能调节的首次报道。
