Badwey J A, Heyworth P G, Karnovsky M L
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115.
Biochem Biophys Res Commun. 1989 Feb 15;158(3):1029-35. doi: 10.1016/0006-291x(89)92825-8.
Neutrophils stimulated with activators of protein kinase C (i.e., 4 beta-phorbol 12-myristate 13-acetate; sn-1,2-dioctanoylglycerol) exhibit a dramatic, dose-dependent incorporation of 32P[Pi] into two proteins with molecular weights of ca. 47 and 49kDa. Proteins of the same molecular weights are also labelled when the cells are stimulated with a chemotactic peptide. However, with the latter stimulus, labelling of the 47kDa species is transient whereas that of the 49kDa entity persists. Labelling of both proteins always accompanied the release of O2-stimulated by these agents. The kinetics of labelling are compatible with the involvement of both phosphoproteins in the stimulation of these cells.
用蛋白激酶C激活剂（即4β-佛波醇12-肉豆蔻酸酯13-乙酸酯；sn-1,2-二辛酰甘油）刺激的中性粒细胞表现出将32P[Pi]显著且剂量依赖性地掺入到两种分子量约为47和49kDa的蛋白质中。当用趋化肽刺激细胞时，相同分子量的蛋白质也会被标记。然而，在后一种刺激下，47kDa物种的标记是短暂的，而49kDa实体的标记持续存在。这两种蛋白质的标记总是伴随着这些试剂刺激下O2的释放。标记动力学与这两种磷蛋白参与这些细胞的刺激作用一致。
