Reilly C F, Tewksbury D A, Schechter N M, Travis J
J Biol Chem. 1982 Aug 10;257(15):8619-22.
Human neutrophil cathepsin G and human skin mast cell chymase rapidly convert angiotensin I to angiotensin II with only minor cleavage elsewhere in the molecule. The rate of cleavage is consistent with a potential role for either or both of these enzymes in an alternate pathway for angiotensin II synthesis. Since neither enzyme in inhibited by captopril, an angiotensin converting enzyme inactivator, it is possible that leukocyte and mast cell enzymes may play a significant role in the development of abnormally high local concentrations of angiotensin II, associated with various inflammatory processes.
人类中性粒细胞组织蛋白酶G和人类皮肤肥大细胞糜蛋白酶可迅速将血管紧张素I转化为血管紧张素II,且仅在分子的其他部位有少量裂解。裂解速率与这两种酶中的一种或两种在血管紧张素II合成的替代途径中的潜在作用一致。由于这两种酶均不受血管紧张素转换酶灭活剂卡托普利的抑制,白细胞和肥大细胞酶可能在与各种炎症过程相关的局部血管紧张素II异常高浓度的形成中起重要作用。