Mirshahi M, Soria J, Soria C, Bertrand O, Mirshahi M, Basdevant A
Laboratory of Haematology, INSERM U 150 (Pr Caen) Hopital Lariboisière, Paris.
Thromb Res. 1987 Nov 1;48(3):279-89. doi: 10.1016/0049-3848(87)90440-3.
As observed for many proteins, glucose has been shown to bind non enzymatically to fibrinogen and to fibrin. The in vitro degree of glycosylation depends upon the concentration of glucose added to fibrinogen and also on the incubation period. This glycosylation induces a decrease in fibrin lysis by plasmin. On the contrary, it does not influence either fibrinogen activity as cofactor in ADP-induced platelet aggregation or the binding of thrombin onto a clot. Despite the 4 day half life of fibrinogen, since clearance of fibrinogen is exponential, it is assumed that very small quantities of fibrinogen may remain for a long time in the circulation leading to the presence of a low level of a highly glycosylated form of fibrinogen. Consequently, poorly degradable fibrin might be derived from this highly glycosylated fibrinogen and thus be responsible for capillary occlusion and also for atherosclerotic complications in the diabetic patient.
正如对许多蛋白质所观察到的那样，已表明葡萄糖可非酶促地与纤维蛋白原和纤维蛋白结合。体外糖基化程度取决于添加到纤维蛋白原中的葡萄糖浓度，也取决于孵育时间。这种糖基化会导致纤溶酶介导的纤维蛋白溶解减少。相反，它既不影响纤维蛋白原作为ADP诱导的血小板聚集的辅因子的活性，也不影响凝血酶与凝块的结合。尽管纤维蛋白原有4天的半衰期，但由于纤维蛋白原的清除是指数性的，因此推测极少量的纤维蛋白原可能会在循环中长时间留存，导致循环中存在低水平的高度糖基化形式的纤维蛋白原。因此，这种高度糖基化的纤维蛋白原可能产生降解不良的纤维蛋白，从而导致糖尿病患者出现毛细血管阻塞以及动脉粥样硬化并发症。
