Effect of epinephrine and insulin on the phosphorylation of phosphorylase phosphatase inhibitor 1 in perfused rat skeletal muscle
Effect of epinephrine and insulin on the phosphorylation of phosphorylase phosphatase inhibitor 1 in perfused rat skeletal muscle
复制标题
肾上腺素和胰岛素对灌注大鼠骨骼肌磷酸化酶磷酸酶抑制剂1磷酸化的影响
DOI：
10.1016/0014-5793(80)81127-6
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发表时间：
1980
期刊：
影响因子：
3.5
通讯作者：
T. Soderling
中科院分区：
文献类型：
--
作者：
B. Khatra;J. Chiasson;Shikama Hisataka;J. Exton;T. Soderling
抑制低分子量磷酸化酶磷酸酶[1-4]的两种热稳定性胰蛋白酶不稳定蛋白已从兔骨骼肌中分离出来。其中一种抑制剂（称为抑制剂 1 (I,)）的活性由 cAMP 依赖性蛋白激酶催化的磷酸化和 MnF 依赖性磷酸酶催化的去磷酸化控制 [2,5,6]。 I1 的磷酸化形式具有抑制性，而去磷酸化形式则无活性 [2, 6]。鉴于骨骼肌中 I1 浓度高、其作为抑制剂的高效力以及通过磷酸化控制其活性，有人认为它可能在磷蛋白磷酸酶的调节中发挥重要作用 [2, 6, 7]。注射肾上腺素的正常兔子的 I1 磷酸化水平增加 [7]。然而，胰岛素增加了对照和糖尿病动物组织中糖原合酶的激活速率[10]并且可以通过抑制CAMP依赖性蛋白激酶[1l]或通过激活磷蛋白磷酸酶来起作用。这两种变化都可能导致 11 的磷酸化状态降低。
The two heat-stable trypsin-labile proteins which inhibit the low molecular weight phosphorylase phosphatase [l-4] have been isolated from rabbit skeletal muscle. The activity of one of the inhibitors, termed inhibitor 1 (I,), is controlled by phosphorylation catalyzed by cAMPdependent protein kinase and dephosphorylation catalyzed by a MnF-dependent phosphatase [2, 5, 6]. The phosphorylated form of I1 is inhibitory whereas the dephosphorylated form is not active [2, 6].In view of high concentration of I1 in skeletal muscle, its high potency as an inhibitor, and control of its activity by phosphorylation, it has been suggested that It may play an important role in the regulation of phosphoprotein phosphatase [2, 6, 7]. Normal rabbits injected with epinephrine have increased levels of phosphorylated form of I1 [7]. However, insulin increases the rate of activation of glycogen synthase in tissues of control and diabetic animals [&-IO] and may act by inhibiting the CAMP-dependent protein kinase [1 l] or by activating a phosphoprotein phosphatase. Both of these changes may result in a decrease in the phosphorylation state of 11.