ArticleThe Biochemical journal2000
Molecular cloning and biochemical characterization of a new mouse testis soluble-zinc-metallopeptidase of the neprilysin family.
Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 74 citations in OpenAlex.
- Neprilysin 4 controls acrosome structure and male fertility in Drosophila melanogaster.Communications biology · 2025Article
- Neprilysin 2 catalyses the degradation of natriuretic peptides despite sacubitrilat Inhibition.Scientific reports · 2025Article
- A comprehensive review of the literature on CD10: its function, clinical application, and prospects.Frontiers in pharmacology · 2024Review
- The Drosophila melanogaster Neprilysin Nepl15 is involved in lipid and carbohydrate storage.Scientific reports · 2021Article
- Neprilysin expression and functions in development, ageing and disease.Mechanisms of ageing and development · 2020Review
- Regulation of Male Fertility by the Renin-Angiotensin System.International journal of molecular sciences · 2020Review
- Amyloid-beta and Alzheimer's disease: the role of neprilysin-2 in amyloid-beta clearance.Frontiers in aging neuroscience · 2014Review
- Dynamic changes in the secondary structure of ECE-1 and XCE account for their different substrate specificities.BMC bioinformatics · 2012Article
- Neprilysin-2 is an important β-amyloid degrading enzyme.The American journal of pathology · 2011Article
- Identification of an endothelin-converting enzyme-2-specific fluorigenic substrate and development of an in vitro and ex vivo enzymatic assay.The Journal of biological chemistry · 2010Article
- Autocrine regulation of human sperm motility by tachykinins.Reproductive biology and endocrinology : RB&E · 2010Article
- Human membrane metallo-endopeptidase-like protein degrades both beta-amyloid 42 and beta-amyloid 40.Neuroscience · 2008Article
- Biosynthesis, processing, trafficking, and enzymatic activity of mouse neprilysin 2.Molecular and cellular biochemistry · 2008Article
- Drosophila melanogaster NEP2 is a new soluble member of the neprilysin family of endopeptidases with implications for reproduction and renal function.The Biochemical journal · 2005Article
- Endothelin-converting enzyme-like 1 (ECEL1) is present both in the plasma membrane and in the endoplasmic reticulum.The Biochemical journal · 2004Article
- Reduced fertility in male mice deficient in the zinc metallopeptidase NL1.Molecular and cellular biology · 2004Article
- Structure, evolutionary conservation, and functions of angiotensin- and endothelin-converting enzymes.International review of cytology · 2004Review
- Computer modeling and nanosecond simulation of the enzyme-substrate complex of the common lymphoblastic leukemia antigen (neprilysin) indicates shared residues at the primary specificity pocket (S1') with matrix metalloproteases.Journal of molecular modeling · 2003Article
- Human recombinant endopeptidase PHEX has a strict S1' specificity for acidic residues and cleaves peptides derived from fibroblast growth factor-23 and matrix extracellular phosphoglycoprotein.The Biochemical journal · 2003Article
- Cell-specific activity of neprilysin 2 isoforms and enzymic specificity compared with neprilysin.The Biochemical journal · 2002Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Because of their roles in controlling the activity of several bio-active peptides, members of the neprilysin family of zinc metallopeptidases have been identified as putative targets for the design of therapeutic agents. Presently, six members have been reported, these are: neprilysin, endothelin-converting enzyme (ECE)-1 and ECE-2, the Kell blood group protein, PHEX (product of the phosphate-regulating gene with homologies to endopeptidase on the X chromosome) and X-converting enzyme (XCE). In order to identify new members of this important family of peptidases, we designed a reverse transcriptase-PCR strategy based on conserved amino acid sequences of neprilysin, ECE-1 and PHEX. We now report the cloning from mouse testis of a novel neprilysin-like peptidase that we called NL1. NL1 is a glycoprotein that, among the members of the family, shows the strongest sequence identity with neprilysin. However, in contrast with neprilysin and other members of the family which are type II integral membrane proteins, NL1 was secreted when expressed in cultured mammalian cells, likely due to cleavage by a subtilisin-like convertase at a furin-like site located 22 amino acid residues in the C-terminus of the transmembrane domain. The recombinant enzyme exhibited neprilysin-like peptidase activity and was efficiently inhibited by phosphoramidon and thiorphan, two inhibitors of neprilysin. Northern blot analysis and in situ hybridization showed that NL1 mRNA was found predominantly in testis, specifically in round and elongated spermatids. This distribution of NL1 mRNA suggests that it could be involved in sperm formation or other processes related to fertility.
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