Heparin-activated protein kinase from rabbit muscle: relationship to enzymes of the glycogen synthase kinase-3 category.
Heparin-activated protein kinase from rabbit muscle: relationship to enzymes of the glycogen synthase kinase-3 category.
复制标题
兔肌肉中的肝素激活蛋白激酶：与糖原合酶激酶 3 类酶的关系。
DOI：
10.1016/0003-9861(86)90734-4
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发表时间：
1986
影响因子：
3.9
通讯作者：
Roach,PJ
中科院分区：
文献类型：
--
作者：
Ahmad,Z;Lee,FT;DePaoli-Roach,AA;Roach,PJ
肝素活化蛋白激酶先前已在兔骨骼肌提取物中鉴定（Z.艾哈迈德特179，96-100）。进一步的研究表明，这种酶在与蛋白激酶FA/GSK-3（糖原合成酶激酶-3）相同的胰蛋白酶肽中磷酸化兔肌肉糖原合成酶，并且能够激活ATP-Mg 2+依赖性蛋白磷酸酶。这些结果表明两种蛋白激酶之间的性质相似。肝素灭活的酶暴露于胰蛋白酶导致肝素活化损失，从3倍到1.3倍。该结果提出的一个假设是，酶FA/GSK-3可能是失去肝素敏感性的肝素活化酶的衍生物。这一假说在概念上的重要性在于，它可能为这类重要的蛋白激酶的调节模式提供线索。
A heparin-activated protein kinase has been previously identified in rabbit skeletal muscle extracts (Z. Ahmadet al.(1985)FEBS Lett.179, 96–100). Further study has indicated that this enzyme phosphorylates rabbit muscle glycogen synthase in the same tryptic peptide(s) as the protein kinase FA/GSK-3 (glycogen synthase kinase-3) and is able to activate the ATP-Mg2+-dependent protein phosphatase. These results indicate similarities in properties between the two protein kinases. Exposure of the heparinactivated enzyme to trypsin resulted in loss of heparin activation, from 3-fold to 1.3-fold. One hypothesis suggested by this result is that the enzyme FA/GSK-3 could be a derivative of the heparin-activated enzyme that has lost heparin sensitivity. The conceptual importance of this hypothesis is that it may provide a clue to the mode of regulation of this important class of protein kinases.