Demonstrates intracellular and surface localization of endothelin and converting enzymes in human coronary endothelium, suggesting dual secretory pathways.
Sites linked to the storage and transportation of endothelin (ET) were investigated in human coronary artery. ET-like immunoreactivity was detected in secretory vesicles and storage granules, indicating that the peptide may be transported via both constitutive and regulated secretory pathways. The distribution of ECE-like immunoreactivity was also investigated to determine possible sites involved in the cleavage of big ET-1 to ET-1. Sections of coronary artery labeled with antisera raised against the endothelin-converting enzymes (ECE-1 alpha, ECE-1 beta, and ECE-2) showed immunoreactive staining over luminal endothelial cells. An en face coronary artery preparation labeled with antisera raised against ECE-1 alpha and ECE-1 beta revealed only a low level of plasma membrane staining by scanning electron microscopy. The findings indicate cell surface and intracellular expression of ECE in human endothelium.
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Russell et al. (1998) studied this question.
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