Hollander I J
Immunoinflammatory Diseases Research, G. D. Searle Research and Development, Monsanto Life Sciences Research Center, St. Louis, Missouri.
Crit Rev Biotechnol. 1987;6(3):253-71. doi: 10.3109/07388558709089383.
Plasminogen activators (PAs) are proteases that convert plasminogen to plasmin. Plasmin, in turn, is a protease that can lyse a fibrin clot and, therefore, PAs have a primary role in fibrinolysis. Two PAs, urokinase (UK) and streptokinase (SK), have been available for therapeutic use for years. Unfortunately, both can cause systemic fibrinogenolysis and other side effects which have limited their use. Interest has focused on a different enzyme, tissue plasminogen activator (t-PA), which will cause specific clot lysis without systemic problems. The gene for t-PA has been cloned and many biotechnology firms are preparing to produce t-PA for therapeutic use. The properties and potential for therapy of t-PA are reviewed and compared to new forms of other activators, such as pro-urokinase. How the interactions of PAs and inhibitors may affect the use of PAs is also discussed.
纤溶酶原激活剂（PAs）是将纤溶酶原转化为纤溶酶的蛋白酶。反过来，纤溶酶是一种能够溶解纤维蛋白凝块的蛋白酶，因此，PA在纤维蛋白溶解中起主要作用。两种PA，尿激酶（UK）和链激酶（SK），多年来一直用于治疗。不幸的是，两者都可引起全身性纤维蛋白原溶解和其他副作用，这限制了它们的应用。人们的兴趣集中在另一种酶，组织纤溶酶原激活剂（t-PA）上，它能引起特异性凝块溶解而无全身问题。t-PA的基因已被克隆，许多生物技术公司正准备生产用于治疗的t-PA。本文综述了t-PA的特性和治疗潜力，并与其他激活剂的新形式，如前尿激酶进行了比较。还讨论了PA与抑制剂的相互作用如何可能影响PA的使用。
