Spangenberg P, Wenzel C, Till U
Institute of Pathological Biochemistry, Medical Academy of Erfurt, GDR.
Folia Haematol Int Mag Klin Morphol Blutforsch. 1988;115(4):421-4.
The status of platelet actin has been studied analytically by the DNase-I inhibition assay. Exposure of platelets to diamide, which oxidizes sulphydryl groups, results in an increase of filamentous actin. Neutralization of the effect of diamide by addition of 2-mercaptopropionylglycine (2-MPG) or washing out the excess of diamide is associated with a normalization of the cellular actin status. These findings strongly suggest that the redox state of platelets is somehow involved in the process of actin polymerization. Alterations of the redox state in metabolically altered platelets could therefore account for changes in the G- to F-actin equilibrium. In the thrombin-induced actin polymerization the redox state of the cell seems to be not involved, since 2-MPG preincubation of platelets (1.25 mM, 30 min) does not inhibit the filament assembly.
已通过脱氧核糖核酸酶I抑制试验对血小板肌动蛋白的状态进行了分析研究。将血小板暴露于能氧化巯基的二酰胺中，会导致丝状肌动蛋白增加。通过添加2-巯基丙酰甘氨酸（2-MPG）中和二酰胺的作用或洗去过量的二酰胺，可使细胞肌动蛋白状态恢复正常。这些发现有力地表明，血小板的氧化还原状态以某种方式参与了肌动蛋白聚合过程。因此，代谢改变的血小板中氧化还原状态的改变可能是G-肌动蛋白与F-肌动蛋白平衡变化的原因。在凝血酶诱导的肌动蛋白聚合过程中，细胞的氧化还原状态似乎未参与其中，因为血小板经2-MPG预孵育（1.25 mM，30分钟）不会抑制丝状组装。
