Minakuchi R, Takai Y, Yu B, Nishizuka Y
J Biochem. 1981 May;89(5):1651-4. doi: 10.1093/oxfordjournals.jbchem.a133362.
Ca2+-activated, phospholipid-dependent multifunctional protein kinase originally found in rat brain occurs in a variety of mammalian tissues. In most tissues the enzyme activity is comparable to that of cyclic AMP-dependent protein kinase when assayed with calf thymus H1 histone as phosphate acceptor. In some tissues such as platelets, brain, and lymphocytes the enzyme far exceeds the cyclic AMP-dependent enzyme. This species of protein kinase found in various tissues shows very similar physical, kinetic, and catalytic properties, and does not appear to show tissue and species specificities. It is conceivable that this protein kinase plays roles in transmembrane control of protein phosphorylation by a large number of extracellular messengers which induce phosphatidylinositol turnover in their target tissues.
钙激活的、磷脂依赖性多功能蛋白激酶最初在大鼠脑中发现，存在于多种哺乳动物组织中。在大多数组织中，当以小牛胸腺H1组蛋白作为磷酸受体进行测定时，该酶的活性与环磷酸腺苷依赖性蛋白激酶相当。在某些组织如血小板、脑和淋巴细胞中，该酶的活性远远超过环磷酸腺苷依赖性酶。在各种组织中发现的这种蛋白激酶表现出非常相似的物理、动力学和催化特性，似乎没有表现出组织和物种特异性。可以想象，这种蛋白激酶在大量细胞外信使对蛋白质磷酸化的跨膜控制中发挥作用，这些信使在其靶组织中诱导磷脂酰肌醇周转。
