Ohlsson K
Scand J Gastroenterol Suppl. 1986;126:18-20. doi: 10.3109/00365528609091886.
Cleavage of C3 and kininogen in human plasma following the addition of increasing amounts of human cationic trypsin was studied using an in vitro model. The cleavage was correlated to the degree of saturation of the plasma protease inhibitors alpha 2-macroglobulin and alpha 1-proteinase inhibitor, and also with varying amounts of human pancreatic secretory trypsin inhibitor. When alpha 2-macroglobulin reached about 70% saturation, there was a prompt cleavage of most of the C3 and kininogen in spite of the presence of 90% free alpha 1-proteinase inhibitor. The consumption of alpha 1-proteinase inhibitor decreased with increasing concentrations of the pancreatic secretory trypsin inhibitor. This inhibitor was needed in a concentration of about 10 mumol to block trypsin-induced C3 and kininogen cleavage completely. As trypsin is thought to be the key trigger enzyme of the pathophysiological changes in acute pancreatitis, it seems reasonable to propose that the pancreatic secretory trypsin inhibitor might be of therapeutic interest in severe acute pancreatitis provided large enough amounts can be made available.
使用体外模型研究了在添加越来越多的人阳离子胰蛋白酶后，人血浆中C3和激肽原的裂解情况。这种裂解与血浆蛋白酶抑制剂α2-巨球蛋白和α1-蛋白酶抑制剂的饱和程度相关，也与不同量的人胰腺分泌型胰蛋白酶抑制剂有关。当α2-巨球蛋白达到约70%的饱和度时，尽管存在90%的游离α1-蛋白酶抑制剂，大多数C3和激肽原仍会迅速裂解。随着胰腺分泌型胰蛋白酶抑制剂浓度的增加，α1-蛋白酶抑制剂的消耗减少。该抑制剂需要约10 μmol的浓度才能完全阻断胰蛋白酶诱导的C3和激肽原裂解。由于胰蛋白酶被认为是急性胰腺炎病理生理变化的关键触发酶，因此似乎有理由提出，只要能获得足够量的胰腺分泌型胰蛋白酶抑制剂，它可能对重症急性胰腺炎具有治疗意义。
