Musci G, Berliner L J
Department of Chemistry, Ohio State University, Columbus 43210.
J Biol Chem. 1987 Oct 15;262(29):13889-91.
This report documents attempts to mimic the rate enhancement effect of thrombomodulin on human alpha-thrombin-catalyzed activation of human protein C in the absence of exogenous calcium. Specifically the following tryptamine analogs at 1 mM concentration were shown to enhance the protein C activation rate relative to a control with no added effector at pH 8.3 (50 mM Tris-HCl, 0.1 M NaCl, 37 degrees C): serotonin, 1.2; tryptamine, 2.9; 5-fluorotryptamine, 4.4; 6-fluorotryptamine, 7.2. At much higher levels, e.g. 10 mM, all of the above effectors, as well as indole, showed a moderate inhibition of human protein C activation. ATP, a platelet release product, showed a sigmoidal inhibition pattern similar to that found previously for thrombin amidase, clotting, and esterase activity (Conery, B.G., and Berliner, L.J. (1983) Biochemistry 22, 369-375). Overall, the enhancement factors for human alpha-thrombin activation of protein C with the tryptamine analogs described above were remarkable when considering the effect of a simple ligand versus the natural activator, thrombomodulin.
本报告记录了在无外源钙的情况下,模拟血栓调节蛋白对人α-凝血酶催化人蛋白C活化的速率增强作用的尝试。具体而言,在pH 8.3(50 mM Tris-HCl、0.1 M NaCl、37℃)条件下,相对于未添加效应物的对照,1 mM浓度的以下色胺类似物显示出可提高蛋白C的活化速率:血清素,1.2;色胺,2.9;5-氟色胺,4.4;6-氟色胺,7.2。在高得多的水平(例如10 mM)下,上述所有效应物以及吲哚均显示出对人蛋白C活化的中度抑制。ATP是一种血小板释放产物,其呈现出S形抑制模式,类似于先前发现的凝血酶酰胺酶、凝血和酯酶活性的抑制模式(Conery, B.G., and Berliner, L.J. (1983) Biochemistry 22, 369 - 375)。总体而言,考虑到简单配体与天然激活剂血栓调节蛋白的作用,上述色胺类似物对人α-凝血酶活化蛋白C的增强因子是显著的。