ArticleThe Biochemical journal2000
N-arginine dibasic convertase (nardilysin) isoforms are soluble dibasic-specific metalloendopeptidases that localize in the cytoplasm and at the cell surface.
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 20 papers.
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Who cites it
20 citing papers in PubMed, 38 citations in OpenAlex.
- Bi-allelic variants in NRDC cause a neurodevelopmental disorder characterized by neonatal lethality, microcephaly, and brain abnormalities.American journal of human genetics · 2026Article
- Nardilysin: classical functions and new horizons in autoimmunity.Frontiers in immunology · 2026Review
- Exercise training-induced extracellular miR-136-3p modulates glucose uptake and myogenesis through targeting of NRDC in human skeletal muscle.Journal of sport and health science · 2025Article
- Function of manchette and intra-manchette transport in spermatogenesis and male fertility.Cell communication and signaling : CCS · 2025Review
- The Myotubularin Related Proteins and the Untapped Interaction Potential of Their Disordered C-Terminal Regions.Proteins · 2025Article
- Altered Surface Expression of Insulin-Degrading Enzyme on Monocytes and Lymphocytes from COVID-19 Patients Both at Diagnosis and after Hospital Discharge.International journal of molecular sciences · 2022Article
- ADAM 17 and Epithelial-to-Mesenchymal Transition: The Evolving Story and Its Link to Fibrosis and Cancer.Journal of clinical medicine · 2021Review
- Nardilysin controls intestinal tumorigenesis through HDAC1/p53-dependent transcriptional regulation.JCI insight · 2018Article
- Unraveling Novel Mechanisms of Neurodegeneration Through a Large-Scale Forward Genetic Screen inFrontiers in genetics · 2018Review
- Nardilysin regulates inflammation, metaplasia, and tumors in murine stomach.Scientific reports · 2017Article
- Article
- Loss of Peripheral Protection in Pancreatic Islets by Proteolysis-Driven Impairment of VTCN1 (B7-H4) Presentation Is Associated with the Development of Autoimmune Diabetes.Journal of immunology (Baltimore, Md. : 1950) · 2016Article
- Nardilysin-dependent proteolysis of cell-associated VTCN1 (B7-H4) marks type 1 diabetes development.Diabetes · 2014Article
- Critical roles of nardilysin in the maintenance of body temperature homoeostasis.Nature communications · 2014Article
- Nardilysin and ADAM proteases promote gastric cancer cell growth by activating intrinsic cytokine signalling via enhanced ectodomain shedding of TNF-α.EMBO molecular medicine · 2012Article
- Reduced neuronal co-localisation of nardilysin and the putative alpha-secretases ADAM10 and ADAM17 in Alzheimer's disease and Down syndrome brains.Age (Dordrecht, Netherlands) · 2009Article
- Mutation of a conserved hydrophobic patch prevents incorporation of ZP3 into the zona pellucida surrounding mouse eggs.Molecular and cellular biology · 2003Article
- Plasma membrane localization and function of the estrogen receptor alpha variant (ER46) in human endothelial cells.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- The metalloendopeptidase nardilysin (NRDc) is potently inhibited by heparin-binding epidermal growth factor-like growth factor (HB-EGF).The Biochemical journal · 2002Article
- N-arginine dibasic convertase is a specific receptor for heparin-binding EGF-like growth factor that mediates cell migration.The EMBO journal · 2001Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-arginine (R) dibasic (NRD) convertase (nardilysin; EC 3.4.24.61), a metalloendopeptidase of the M16 family, specifically cleaves peptide substrates at the N-terminus of arginines in dibasic motifs in vitro. In rat testis, the enzyme localizes within the cytoplasm of spermatids and associates with microtubules of the manchette and axoneme. NRD1 and NRD2 convertases, two NRD convertase isoforms, differ by the absence (isoform 1) or presence (isoform 2) of a 68-amino acid insertion close to the active site. In this study, we overexpressed both isoforms, either by vaccinia virus infection of BSC40 cells or transfection of COS-7 cells. The partially purified enzymes exhibit very similar biochemical and enzymic properties. Microsequencing revealed that NRD convertase is N-terminally processed. Results of immunocytofluorescence, immunoelectron microscopy and subcellular fractionation studies argue in favour of a primary cytosolic localization of both peptidases. Although the putative signal peptide did not direct NRD convertase into microsomes in an in vitro translation assay, biotinylation experiments clearly showed the presence of both isoforms at the cell surface. In conclusion, although most known processing events at pairs of basic residues are achieved by proprotein convertases within the secretory pathway, NRD convertase may fulfil a similar function in the cytoplasm and/or at the cell surface.
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