磷酸化酶激酶缺陷小鼠灌注心脏中肌钙蛋白抑制亚基的磷酸化。体内3':5'-环磷酸腺苷依赖性蛋白激酶对肌钙蛋白磷酸化的证据。
Phosphorylation of the inhibitory subunit of troponin in perfused hearts of mice deficient in phosphorylase kinase. Evidence for the phosphorylation of troponin by adenosine 3':5'-phosphate-dependent protein kinase in vivo.
作者信息
England P J
出版信息
Biochem J. 1977 Nov 15;168(2):307-10. doi: 10.1042/bj1680307.
Abstract
When hearts from control and phosphorylase kinase-deficient (I strain) mice were perfused with 0.1 micrometer-DL-isoprenaline, there was a parallel increase in contraction, cyclic AMP concentration and troponin I phosphorylation. However, there was no increase in phosphorylase a in the I-strain hearts, whereas the control hearts showed a large increase. Assays of I-strain heart extracts showed a normal cyclic AMP-dependent protein kinase activity but no phosphorylase kinase activity. It is concluded that troponin I is phosphorylated in intact hearts by protein kinase and not phosphorylase kinase.
摘要
当用0.1微摩尔的DL-异丙肾上腺素灌注对照小鼠和磷酸化酶激酶缺陷型（I品系）小鼠的心脏时，收缩、环磷酸腺苷（cAMP）浓度和肌钙蛋白I磷酸化呈平行增加。然而，I品系心脏中的磷酸化酶a没有增加，而对照心脏中则大幅增加。对I品系心脏提取物的检测显示，其环磷酸腺苷依赖性蛋白激酶活性正常，但没有磷酸化酶激酶活性。得出的结论是：在完整心脏中，肌钙蛋白I是由蛋白激酶而非磷酸化酶激酶磷酸化的。
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