Calcium ionophore A23187 elevates angiotensin-converting enzyme in cultured bovine endothelial cells.
Calcium ionophore A23187 elevates angiotensin-converting enzyme in cultured bovine endothelial cells.
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DOI：
10.1016/0167-4889(89)90178-x
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发表时间：
1989-01
期刊：
影响因子：
--
通讯作者：
Y. Dasarathy;B. Fanburg
中科院分区：
文献类型：
--
作者：
Y. Dasarathy;B. Fanburg
Calcium ionophore A23187 (0.3–0.4 μM) elevated cellular angiotensin-converting enzyme activity (ACE) 2–7-fold after 48 h incubation with bovine pulmonary artery endothelial cells in culture. Cycloheximide (0.1 μg/ml) blocked the elevation in ACE produced by A23187. The increase in ACE was inhibited by 0.2 mM EGTA, 50 μM verapamil and 50 μM nifedipine, and was not associated with changes in cellular cAMP. Melittin, a phospholipase A2activator, or addition of exogenous arachidonic acid failed to reproduce the elevation, and indomethacin only partially blocked the A23187 effect. The elevation of ACE was also inhibited by the calcium-calmodulin inhibitor, calmidazolium. Thus, we postulate that the ionophore A23187 elevates ACE in endothelial cells through a calcium-dependent mechanism other than phospholipase A2activation. The elevation depends on new protein synthesis and involves calcium-calmodulin-dependent cellular mechanisms.
