ArticleThe Biochemical journal2002
Cell-specific activity of neprilysin 2 isoforms and enzymic specificity compared with neprilysin.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 39 citations in OpenAlex.
- Neprilysin 2 catalyses the degradation of natriuretic peptides despite sacubitrilat Inhibition.Scientific reports · 2025Article
- Neuropeptide inactivation regulates egg-laying behavior to influence reproductive health in Caenorhabditis elegans.Current biology : CB · 2024Article
- Proteolytic Cleavage of Bioactive Peptides and Protease-Activated Receptors in Acute and Post-Colitis.International journal of molecular sciences · 2021Article
- The Drosophila melanogaster Neprilysin Nepl15 is involved in lipid and carbohydrate storage.Scientific reports · 2021Article
- The tripartite architecture of the eukaryotic integral membrane protein zinc metalloprotease Ste24.Proteins · 2020Article
- Phosphoramidon inhibits the integral membrane protein zinc metalloprotease ZMPSTE24.Acta crystallographica. Section D, Structural biology · 2018Article
- Neprilysin Inhibitors and Bradykinin.Frontiers in medicine · 2018Review
- Long-term neprilysin inhibition - implications for ARNIs.Nature reviews. Cardiology · 2017Review
- Neprilysins: an evolutionarily conserved family of metalloproteases that play important roles in reproduction in Drosophila.Genetics · 2014Article
- Amyloid-beta and Alzheimer's disease: the role of neprilysin-2 in amyloid-beta clearance.Frontiers in aging neuroscience · 2014Review
- 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
- Neprilysin impedes islet amyloid formation by inhibition of fibril formation rather than peptide degradation.The Journal of biological chemistry · 2010Article
- Biosynthesis, processing, trafficking, and enzymatic activity of mouse neprilysin 2.Molecular and cellular biochemistry · 2008Article
- Stage-specific modulation of neprilysin and aminopeptidase N in the limbic system during kindling progression.Journal of molecular neuroscience : MN · 2007Article
- Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolism.The Biochemical journal · 2004Article
- 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
- 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
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neprilysin (NEP) 2 is a recently cloned glycoprotein displaying a high degree of sequence identity with neprilysin (EC 3.4.24.11), the prototypical member of the M13 subfamily of metalloproteases. Whereas NEP is involved in the metabolism of several bioactive peptides by plasma membranes of various cells, the enzymic properties and physiological functions of NEP2 are unknown. Here we characterize the cell-expression modalities and enzymic specificity of two alternatively spliced isoforms of NEP2 in Chinese hamster ovary and AtT20 cells. In the two cell lines, both isoforms are type II glycoproteins inserted in the endoplasmic reticulum as inactive precursors. Maturation detected by Western-blot analysis of glycosidase digests was cell-specific and more efficient in the endocrine cell line. The enzymic activity of both isoforms semi-purified from AtT20 cells reveals comparable specificities in terms of model substrates, pH optima and inhibitory patterns. NEP2 activity was compared with that of NEP regarding potencies of transition-state inhibitors, modes of hydrolysis, maximal hydrolysis rates and apparent affinities of bioactive peptides. Although all transition-state inhibitors of NEP inhibited NEP2 activity, albeit with different potencies, and many peptides were cleaved at the same amide bond by both peptidases, differences could be observed, i.e. in the hydrolysis of gonadotropin-releasing hormone and cholecystokinin, which occurred at different sites and more efficiently in the case of NEP2. Differences in cleavage of bioactive peptides, in cell-trafficking patterns and in tissue distribution indicate that NEP and NEP2 play distinct physiological roles in spite of their high degree of sequence identity.
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