Findik D, Reuter C, Presek P
Rudolf-Buchheim-Institut für Pharmakologie, Justus-Liebig-Universität, Glessen, FRG.
FEBS Lett. 1990 Mar 12;262(1):1-4. doi: 10.1016/0014-5793(90)80138-9.
Human platelet glycoproteins IIb and IIIa form the receptor for fibrinogen, von Willebrand factor and fibronectin. Isolated human glycoproteins IIb-IIIa are phosphorylated by purified pp60c-src protein tyrosine kinase. Analysis of the phosphorylated proteins on SDS-PAGE showed that under reducing conditions both phosphoproteins change their relative molecular masses from 135 to 120 kDa and from 97 to 105 kDa, which are characteristic properties of glycoproteins IIb-IIIa. Phosphorylated proteins could be immunoprecipitated with an antiserum against glycoproteins IIb-IIIa but not by control serum. Some kinetic properties of the glycoprotein phosphorylations are also investigated. How the glycoprotein IIb-IIIa complex acquires its receptor activity in stimulated platelets is unknown; however, phosphorylation could be an important mechanism.
人血小板糖蛋白IIb和IIIa形成纤维蛋白原、血管性血友病因子和纤连蛋白的受体。纯化的人糖蛋白IIb-IIIa可被纯化的pp60c-src蛋白酪氨酸激酶磷酸化。在SDS-PAGE上对磷酸化蛋白进行分析表明，在还原条件下，两种磷蛋白的相对分子质量分别从135 kDa变为120 kDa，从97 kDa变为105 kDa，这是糖蛋白IIb-IIIa的特征性质。磷酸化蛋白可用抗糖蛋白IIb-IIIa抗血清进行免疫沉淀，但不能用对照血清进行免疫沉淀。还研究了糖蛋白磷酸化的一些动力学性质。糖蛋白IIb-IIIa复合物如何在受刺激的血小板中获得其受体活性尚不清楚；然而，磷酸化可能是一个重要机制。
