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Endothelin converting enzyme-1 (ECE-1) is a key enzyme in the biosynthesis of endothelin-1 (ET-1), a potent regulator of ovarian function. Different ECE-1 isoforms are localized in distinct intracellular compartments. Thus, the spatial and temporal pattern of ECE-1 expression determines the site of big ET-1 activation and the bioavailability of ET-1. This study was undertaken to investigate the hormonal regulation and cell-specific expression of ECE-1 isoforms in endothelial and steroidogenic cells of bovine follicles and corpora lutea (CL). Using enriched follicular and luteal cell subpopulations and in-situ hybridization techniques we showed that the ECE-1 gene is expressed by endothelial and steroidogenic cell alike, however, the intracellular ECE-1a isoform was present only in ET-1 expressing endothelial cells. Steroidogenic cells in follicles or in CL, deficient in ET-1, expressed only the plasma membrane ECE-1b isoform. The intensity of antisense ECE-1 labeling to the granulosa cell layer increased with follicular size; IGF-1 and insulin up-regulated ECE-1 expression when cultured with granulosa cells, suggesting that these growth factors may increase ECE-1 in growing follicles. In contrast, ET-1 and LH down-regulated ECE-1 in steroidogenic cells. The latter effect could account for low ECE (and ET-1) levels which characterize early luteal phase. These findings suggest that ECE-1 is regulated during different stages of the cycle in a physiologically relevant manner. The hormonal regulation and intracellular localization of bovine ECE-1 isoforms revealed in this study may provide new insights into ET-1 biosynthesis and mode of action in different cellular microenvironment within the ovary.
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