MODULATION OF PROTEOLYTIC ACTIVITY IN TISSUES FOLLOWING CHRONIC INHIBITION OF ANGIOTENSIN-CONVERTING ENZYME
MODULATION OF PROTEOLYTIC ACTIVITY IN TISSUES FOLLOWING CHRONIC INHIBITION OF ANGIOTENSIN-CONVERTING ENZYME
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DOI：
10.1016/0006-2952(93)90044-w
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发表时间：
1993-04-06
影响因子：
5.8
通讯作者：
JUILLERATJEANNERET, L
中科院分区：
文献类型：
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作者：
JUILLERATJEANNERET, L
研究了血管紧张素转换酶（ACE） （EC 3.4.15.1）在主动脉环慢性抑制下的释放及对各脏器蛋白水解平衡的调节。来自大鼠器官的ACE具有比循环酶更高的表观分子质量，但对ACE抑制剂的行为相似。长期使用ACE抑制剂（卡托普利或赖诺普利）治疗25天，随后1天不治疗，血浆ACE升高，但仅轻微改变肺、主动脉、心脏和肾脏特异性ACE活性。肺中两种血管紧张素降解酶氨基肽酶A和B的活性下降，血浆中氨基肽酶A的活性也下降。在体外，丝氨酸蛋白酶、金属蛋白酶、丝氨酸和硫醇蛋白酶或天冬氨酸蛋白酶抑制剂均不抑制主动脉环中ACE的释放。慢性ACE抑制后，蛋白酶抑制剂的存在并未显著改变主动脉环中ACE的释放。凝胶过滤实验表明，ACE只有在从内皮细胞释放后才能从组织形态转化为循环形态。
The release of angiotensin-converting enzyme (ACE) (EC 3.4.15.1) from aortic rings and the modulation of the proteolytic balance of rat organs under chronic ACE inhibition were examined. ACE from rat organs had a higher apparent molecular mass than the circulating enzyme, but a similar behavior towards ACE inhibitors. Chronic treatment with ACE inhibitors (captopril or lisinopril) for 25 days, followed by 1 day without treatment, increased plasma ACE, but only slightly modified lung, aorta, heart and kidney specific ACE activity. In the lung the activities of aminopeptidases A and B, two angiotensin degrading enzymes, decreased, as did the activity of aminopeptidase A in the plasma. In vitro, the release of ACE from aortic rings was not suppressed by inhibitors of either serine proteases, metalloproteases, serine and thiol proteases, or aspartyl proteases. After chronic ACE inhibition, the release of ACE from aortic rings was not significantly modified by the presence of protease inhibitors. As shown by gel filtration experiments, ACE was converted from its tissue form into its circulating form only after release from the endothelium.