Ferrario C M, Chappell M C
Hypertension Center, Bowman Gray School of Medicine, Winston-Salem, North Carolina.
Curr Opin Cardiol. 1994 Sep;9(5):520-6. doi: 10.1097/00001573-199409000-00004.
The therapeutic benefits of angiotensin-converting enzyme inhibitors in the treatment of hypertension, congestive heart failure, and atherosclerotic heart disease are undeniable. Recent studies, however, suggest that the cardioprotective effect produced by these drugs is complex and may not be solely related to inhibition of the generation of angiotensin II. An alternative pathway for the generation of angiotensin II from angiotensin I has been proposed, following the recent identification of a chymotrypsin-like protease (chymase) that may contribute to the formation of angiotensin II in human heart tissue. The enzyme is present in cardiac mast cells and displays unusual substrate specificity for the conversion of angiotensin I to angiotensin II. While biochemical studies have provided convincing evidence for a chymase-dependent production of angiotensin II, the contribution of this enzyme to the physiologic or pathological regulation of arterial pressure and cardiac function remains undetermined.
血管紧张素转换酶抑制剂在治疗高血压、充血性心力衰竭和动脉粥样硬化性心脏病方面的治疗益处是不可否认的。然而，最近的研究表明，这些药物产生的心脏保护作用是复杂的，可能不仅仅与抑制血管紧张素II的生成有关。在最近鉴定出一种类胰凝乳蛋白酶（糜酶）后，有人提出了从血管紧张素I生成血管紧张素II的另一条途径，这种酶可能有助于在人心脏组织中形成血管紧张素II。该酶存在于心脏肥大细胞中，对血管紧张素I转化为血管紧张素II表现出不同寻常的底物特异性。虽然生化研究已经为糜酶依赖性血管紧张素II的产生提供了令人信服的证据，但这种酶对动脉血压和心脏功能的生理或病理调节的贡献仍未确定。
