Edgardo Catalán R, Martínez A M, Dolores Aragonés M, Hernández F
Departamento de Biología Molecular, Universidad Autónoma de Madrid, Spain.
Neurochem Int. 1996 Jan;28(1):59-65. doi: 10.1016/0197-0186(95)00060-l.
The protein phosphorylation in rat brain microvessels has been examined; the major phosphorylated proteins correspond to a doublet of molecular weight 134-141 kDa, and four proteins of approx. 25, 55, 80 and 200 kDa. TPA (12-O-tetradecanoylphorbol-13-acetate) enhanced, in a few minutes, the phosphorylation of three major protein substrates with apparent molecular weights of 17.5, 44.5 and 80 kDa. These effects are inhibited by staurosporine. The 80 kDa protein resulted to be myristoylated alanine-rich C kinase substrate (MARCKS). This work demonstrates that protein kinase C plays an important role in protein phosphorylation in blood-brain barrier (BBB).
已对大鼠脑微血管中的蛋白质磷酸化进行了检测；主要的磷酸化蛋白对应于分子量为134 - 141 kDa的双峰，以及四种分子量约为25、55、80和200 kDa的蛋白质。佛波酯（12 - O - 十四酰佛波醇 - 13 - 乙酸酯）在几分钟内增强了三种表观分子量分别为17.5、44.5和80 kDa的主要蛋白质底物的磷酸化。这些效应被星形孢菌素抑制。80 kDa的蛋白质被证明是富含豆蔻酰化丙氨酸的C激酶底物（MARCKS）。这项工作表明蛋白激酶C在血脑屏障（BBB）的蛋白质磷酸化中起重要作用。
