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• W1973239281 endingPage "870" @default.
• W1973239281 startingPage "863" @default.
• W1973239281 abstract "Neutral endopeptidase (NEP) is a zinc metallopeptidase ubiquitously distributed in various tissues in mammals. This peptidase is involved in the post-secretory metabolism of various neuropeptides and peptide hormones in vivo, such as enkephalins, bradykinin, atrial natriuretic peptide, substance P and endothelins. In this paper we show that NEP is expressed in ovaries as a 110-kDa glycosylated integral membrane protein with enzymatic properties similar to those of the kidney protein. Using immunohistochemistry, we localize the peptidase in the granulosa cells of follicles at all stages of maturation, with the exception of atretic follicles. We also observe immunoreactive staining in the epithelia that lines the blood vessels in the medulla and the surface of the ovary. The co-localization of NEP and bioactive peptides known to be physiological substrates of NEP in other tissues suggests an important role for this protein in processes such as follicle maturation, ovulation, and/or regulation of ovarian blood flow, by modulating the physiological function of these peptides." @default.
• W1973239281 created "2016-06-24" @default.
• W1973239281 creator A5059476929 @default.
• W1973239281 creator A5069230752 @default.
• W1973239281 date "2001-07-01" @default.
• W1973239281 modified "2023-10-02" @default.
• W1973239281 title "Neutral endopeptidase is expressed on the follicular granulosa cells of rabbit ovaries" @default.
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• W1973239281 doi "https://doi.org/10.1016/s1096-4959(01)00390-6" @default.
• W1973239281 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11435141" @default.
• W1973239281 hasPublicationYear "2001" @default.
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