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• W1968366259 abstract "We have previously reported the intracellular localization of the endothelin-converting enzyme-1 (ECE-1) in human umbilical vein endothelial cells. In the present study, we provide the first immunocytochemical and biochemical evidence for the presence of ECE-2 in human cells. ECE activity was determined by conversion of exogenously added big endothelin-1 (big ET-1) to ET-1 in subcellular fractions obtained by sucrose density gradient centrifugation of human umbilical vein endothelial cell homogenates. ECE-1 and ECE-2 can be differentiated by pH dependence for optimal activity and by sensitivity to phosphoramidon, which shows selectivity for ECE-2 over ECE-1 and PD159790, a novel ECE-1 selective inhibitor. Optimal ECE activity was measured at pH 6.0, a value intermediate between that reported for ECE-1 (pH 6.8) and ECE-2 (pH 5.5), indicating expression of both enzymes. At pH 6.9, conversion of big ET-1 was inhibited markedly by 30 micromol/L PD159790 and by 100 micromol/L phosphoramidon but not by 0.1 micromol/L phosphoramidon. In contrast, ECE activity was unaffected by 30 micromol/L PD159790 but was inhibited markedly by 0.1 and 100 micromol/L phosphoramidon at pH 5. 4 (IC50 1.5 nmol/L), consistent with ECE-2 activity. Confocal microscopy revealed a punctate pattern of ECE-2-like immunoreactive staining in the cell cytosol, suggesting localization to secretory vesicles with a possible role in processing big ET-1 while in transit to the cell surface via the constitutive secretory pathway." @default.
• W1968366259 created "2016-06-24" @default.
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• W1968366259 date "1999-04-30" @default.
• W1968366259 modified "2023-10-03" @default.
• W1968366259 title "Evidence for Intracellular Endothelin-Converting Enzyme-2 Expression in Cultured Human Vascular Endothelial Cells" @default.
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• W1968366259 doi "https://doi.org/10.1161/01.res.84.8.891" @default.
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